1.1.1.2 alcohol dehydrogenase (NADP+) industry expression and strength of the alipathic aldehyde reductase activity are strongly correlated with the flavor quality of the herb Vietnamese coriander 1.1.1.2 alcohol dehydrogenase (NADP+) industry possible uses of this enzyme in the production of wax esters 1.1.1.8 glycerol-3-phosphate dehydrogenase (NAD+) food industry potential use of Saccharomyces cerevisiae-Saccharomyces kudriavzevii hybrids in the wine industry where glycerol content is an important quality parameter 1.1.1.11 D-arabinitol 4-dehydrogenase industry promising method for the production of xylitol from the cheap material glucose if the aArDH gene can be introduced into yeast strains that can convert glucose to D-arabitol 1.1.1.25 shikimate dehydrogenase (NADP+) food industry the biosynthesis of anthocyanins (ATs) and hydrolysable tannins (HTs) competes for the same substrate, 3-DHS, and SDH activity is regulated not only by the NADPH/NADP+ ratio, but also by the expression of the pomegranate shikimate dehydrogenases, PgSDHs. Since the outer peel affects the customer's decision regarding fruit consumption, such knowledge can be utilized for the development of genetic markers for breeding pomegranates having higher levels of both ATs and HTs 1.1.1.49 glucose-6-phosphate dehydrogenase (NADP+) industry production of abundant intermediates for industrially erythritol production 1.1.1.67 mannitol 2-dehydrogenase industry best strain for expression of MDH in both laboratory and industrial applications is Escherichia coli BL21 (DE3) plysS 1.1.1.67 mannitol 2-dehydrogenase industry redox balancing between the intracellular NADP(H) and NAD(H) based on NAD(P)(H)-dependent interconversion of mannitol and fructose by M2DH may be a useful strategy of metabolic engineering 1.1.1.67 mannitol 2-dehydrogenase industry the enzyme synthesizes D-mannitol is commonly known as a sweetener in food manufacturing such as juices, soft drinks, cakes, and sweet cookies, moreover, other processing including alternative sugar for diabetic patients, cosmetics, personal hygiene products, and laxative. D-mannitol is 50% as sweet as sucrose 1.1.1.69 gluconate 5-dehydrogenase food industry production of 5-keto-D-gluconic acid that can be converted effectively into L-(+)-tartaric acid 1.1.1.86 ketol-acid reductoisomerase (NADP+) industry Sac-KARI is one of the rare enzymes that displays high activity at elevated temperatures, a broad range of pH tolerance and is able to utilize both NADH and NADPH as cofactors. These properties make it a potential candidate for use in metabolic engineering or industrial applications under anaerobic or harsh conditions 1.1.1.102 3-dehydrosphinganine reductase food industry naturally occuring missense mutation A175T is linked to animals with bovine spinal muscular atrophy. Protein exhibits no detectable in vitro catalytic activity, but the mutated gene complements the growth defect of a homologous yeast knock-out strain as well as the healthy variant 1.1.1.119 glucose 1-dehydrogenase (NADP+) industry Optimizing whole-cell biocatalysts by integrating a recombinant intracellular NADPH regeneration system through co-expression of a glucose facilitator from Zymomonas mobilis for uptake of unphosphorylated glucose and a NADP+-dependent glucose dehydrogenase from Bacillus megaterium that oxidizes glucose to gluconolactone. 1.1.1.149 20alpha-hydroxysteroid dehydrogenase food industry the enzyme can alter glucocorticoid metabolism in the gut and thereby serves as potential probiotics for the management of androgen-dependent diseases 1.1.1.184 carbonyl reductase (NADPH) food industry mequindox, inhibitor of several Gram-positive and Gram-negative bacteria, is reduced by carbonyl reductase CBR1 1.1.1.184 carbonyl reductase (NADPH) industry enzyme has a promising future for industrial application 1.1.1.184 carbonyl reductase (NADPH) industry improved (R)-1-phenyl-1,2-ethanediol production by a codon optimized R-specific carbonyl reductase whose coding gene rcr is engineered by truncating its disorder sequence of 4-27 bp at 5'-terminus and adaption of codon usage bias in Escherichia coli. It will provide a new method to establish an effective expression system for improving chiral alcohol productivity by codon optimization 1.1.1.184 carbonyl reductase (NADPH) industry modification of coenzyme specificity and alteration of product enantioselectivity in SDRs by using the protein engineering approach, which will have valuable industrial applications 1.1.1.195 cinnamyl-alcohol dehydrogenase industry cofactor recycling catalytic system reveals both 100% selectivity and aldehyde conversion within 3 h by usage of ADH, which provides an inexpensive overall process 1.1.1.202 1,3-propanediol dehydrogenase industry development of an economical and eco-friendly biological process for the production of propane-1,3-diol from renewable resources by construction of a novel operon including YqhD 1.1.1.312 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase industry the authors focus on the metabolic intermediate 2-pyrone-4,6-dicarboxylic acid as a potential raw material for novel, bio-based polymers 1.1.1.343 phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating) industry production of abundant intermediates for industrially erythritol production 1.1.1.422 pseudoephedrine dehydrogenase industry the wide substrate spectrum of these dehydrogenases, combined with their regio- and enantioselectivity, suggests a high potential for the industrial production of valuable chiral compounds 1.1.1.423 (1R,2S)-ephedrine 1-dehydrogenase industry the wide substrate spectrum of these dehydrogenases, combined with their regio- and enantioselectivity, suggests a high potential for the industrial production of valuable chiral compounds 1.1.3.2 L-lactate oxidase food industry L-lactate oxidase based lactate sensors are widely used for clinical diagnostics, sports medicine, and food quality control. Rational engineering of Aerococcus viridans L-lactate oxidase for the mediator modification to achieve quasi-direct electron transfer type lactate sensor 1.1.3.4 glucose oxidase food industry food and beverage additive, used for low alcohol wine production, used for glucose removal from dried egg, improvement of color, flavor, and shelf life of food materials, oxygen removal from fruit juices, canned beverages, and from mayonnaise to prevent rancidity, used as ingredient of toothpaste, for the production of gluconic acid, and as a food preservative 1.1.3.4 glucose oxidase food industry food processing-additive, used for bread making (GOX is an effective oxidant to produce bread with improved texture and increased loaf volume), and in dry egg powder, used as preservative in packaged food and for reduced alcohol wine production 1.1.3.4 glucose oxidase food industry the enzyme is used as food preservative and color stabilizer 1.1.3.4 glucose oxidase food industry Horseradish peroxidase, glucose oxidase, and glucose can be applied efficiently to modify several physicochemical properties (especially rheological and emulsifying properties) of soybean protein isolate. Soybean protein products are widely applied in processed foods as important ingredients, due to their higher nutritive values and desirable functional properties. Physical, chemical, and enzymatic modifications can be used to treat food proteins for property improvement 1.1.3.4 glucose oxidase food industry mutant enzyme Y169C/A211C is a good candidate for the bread baking industry. It has a significant effect on bread volume. Its improved thermostability, pH stability, and catalytic activity, its resistance to SDS, maximal enzymatic activity at low temperatures, and high activity under alkaline conditions are valuable properties that in addition to the bread baking industry 1.1.3.4 glucose oxidase food industry potentially useful in food biopreservation, application for the preservation of aquatic products at low-temperatures, good antimicrobial effect against common fish pathogenic bacteria (Listeria monocytogenes and Vibrio parahaemolyticus), excellent freshness preserving agent in the context of the grass carp 1.1.3.4 glucose oxidase food industry the enzyme is used in clinical, pharmaceutical, food and chemical industries 1.1.3.4 glucose oxidase industry oxygen scavenger, chemical bleaching, used for gluconic acid production and in glucose sensor/assays 1.1.3.4 glucose oxidase industry in the textile industry, enzyme GOX is used for bio-bleaching and in oral care products as antimicrobial agent 1.1.3.4 glucose oxidase industry the enzyme is used in clinical, pharmaceutical, food and chemical industries 1.1.3.4 glucose oxidase pharmaceutical industry enzyme immobilized both independently and together with catalase in gel of polyvinylalcohol in the form of membranes on cotton base, employment in food and pharmaceutical industries 1.1.3.5 hexose oxidase food industry the enzyme is useful for improving the rheological and bread making properties of flour and the quality of the bread, overview 1.1.3.10 pyranose oxidase food industry the enzyme improves dough stability and bread quality 1.1.5.4 malate dehydrogenase (quinone) industry the lactose-oxidizing activity of malate:quinone oxidoreductase can be used for producing lactobionic acid (LBA), a valuable organic acid used in the cosmetic, food, and pharmaceutical industries 1.1.5.14 fructose 5-dehydrogenase food industry the enzyme can be used as biosensor to quantify D-fructose in commercial beverages and honey 1.1.5.14 fructose 5-dehydrogenase industry direct electron-transfer bioelectrocatalysis can be used in biosensors, biofuel cells and bioreactors, FDH immobilised on Ketjen black electroconductive material produces a catalytic oxidation wave of D-fructose without a mediator, the electron in FDH seems to be directly transferred to the electrode via the heme c site 1.1.99.12 sorbose dehydrogenase food industry L-sorbose can be catalyzed into L-ascorbic acid by Ketogulonicigenium vulgare, vitamin C industry 1.1.99.18 cellobiose dehydrogenase (acceptor) industry CDH is involved in the degradation of the two most prominent biopolymers, cellulose and lignin, CDH can produce both reagents needed for fenton chemistry, H2O2 and ferrous iron complexes, which may migrate into and disrupt the lignocellulose matrix 1.1.99.18 cellobiose dehydrogenase (acceptor) industry decolourisation of waste water in textile dyeing industry, CDH displays a synergism with laccases in the decolourisation of ABu62, an anthraquinonic dye, and an antagonism with laccases in the decolourisation of the anthraquinonic dyes ABu281 and RBu19 1.1.99.18 cellobiose dehydrogenase (acceptor) industry the enzyme can be used for bleaching cotton in textile industry 1.1.99.20 alkan-1-ol dehydrogenase (acceptor) industry microbiological degradation appears to be the only means to decompose this group of polymers 1.2.1.8 betaine-aldehyde dehydrogenase food industry the BADH2 could play a role in the improvement of rice fragrance, which could lead to an enhancement in rice quality and market price 1.2.1.30 carboxylate reductase (NADP+) industry vanillic acid reduction in Escherichia coli BL21-CodonPlus(DE3)-RP/pPV2.85 cells containing car, npt and gdh is complete in 6 h, and is faster than in cells containing only car and/or npt. The availability of Escherichia coli BL21-CodonPlus(DE3)-RP/pPV2.85 expressing holo-Car and Gdh provides a means of generating a range of value-added aldehydes or alcohols of importance in pharmaceutical, food and agricultural industries. Uses of directed evolution and related mutant generating processes, may enable a Car-system with broader substrate specificities and one that is capable of achieving much higher product yields 1.2.1.44 cinnamoyl-CoA reductase industry down-regulated CCR lines with a reduced kappa number of small-scale Kraft pulps may be a starting point for constructing double mutants with enhanced properties of significance for practical forestry 1.2.1.44 cinnamoyl-CoA reductase industry downregulation of CCR in transgenic poplar (Populus tremula x Populus alba) is associated with up to 50% reduced lignin content and an orange-brown, often patchy, coloration of the outer xylem. Lignin is relatively more reduced in syringyl than in guaiacyl units. Elevated ferulic acid levels, ferulic acid is incorporated into the lignin via ether bonds. Reduced levels of lignin and hemicellulose are associated with an increased proportion of cellulose. Stress response induced by altered cell wall structure. Chemical pulping of wood derived from 5-year-old, field-grown transgenic lines reveal improved pulping characteristics, but growth is affected in all transgenic lines tested. Trees harboring CCR alleles that result in reduced CCR activity are interesting progenitors for breeding programs. The lower lignin and hemicellulose levels and associated relative increase in cellulose suggest that CCR downregulation may be a good strategy to improve plant biomass for bioethanol production 1.2.1.46 formaldehyde dehydrogenase industry amperometric enzyme-based sensor-system for the direct detection of formaldehyde in air, based on a native bacterial NAD+- and glutathione-independent formaldehyde dehydrogenase as biorecognition element. With the elimination of NAD+ it is much more promising to obtain a sensor device with higher long-term stability 1.2.1.46 formaldehyde dehydrogenase industry construction of a formaldehyde-selective biosensor using NAD+- and glutathione-dependent recombinant formaldehyde dehydrogenase as a bio-recognition element immobilised on the surface of Si/SiO2/Si3N4 structure 1.2.1.46 formaldehyde dehydrogenase industry development of a bi-enzyme biosensor for formaldehyde using diaphorase from Bacillus stearothermophilus, NAD+- and glutathione-dependent FDH as bio-recognition elements. Both enzymes can be immobilized on the top of a graphite electrode together with two osmium-redox polymers. Characteristics of the optimized formaldehyde biosensor are sensitivity, detection limit, and linear dynamic range 1.2.1.46 formaldehyde dehydrogenase industry high thermostability makes FdDH potentially useful for bioanalytic purposes, namely, for formaldehyde assay in food products, wastewater, and pharmaceuticals, and for biotransformation of formaldehyde to formic acid 1.2.3.4 oxalate oxidase industry oxalate oxidase is useful for oxalic acid removal in industrial bleaching plant filtrates 1.2.3.4 oxalate oxidase industry the enzyme is capable of removing oxalic acid from a variety of industrial bleaching filtrates 1.2.3.4 oxalate oxidase industry the oxalate oxidase from Costus pictus is used as a cheap source of oxalate oxidase enzyme which is used in oxalate determination in biological fluids 1.2.4.2 oxoglutarate dehydrogenase (succinyl-transferring) industry ODH is essential for glutamine utilization, regulatory mechanisms of reduced ODH activity that is essential for the industrial production of 1.5 million tons per year of glutamate with Corynebacterium glutamicum 1.3.1.27 2-hexadecenal reductase food industry use of enzyme to improve beer quality by conversion of trans-2-nonenal, the major contributor to the cardboard-like taste of aged beer 1.3.3.5 bilirubin oxidase industry BOX can be used to decolorize synthetic dyes from effluents, especially for anthraquinonic dyes 1.4.1.2 glutamate dehydrogenase food industry plays an essential role during postharvest senescence, its expression most likely is controlled by multigenes and regulated either transcriptionally or posttranscriptionally 1.4.1.2 glutamate dehydrogenase food industry Lactococcus lactis IFPL 953 shows the highest NAD-GDH activity among wild isolates from raw milk cheeses. L. lactis IFPL 953 also demonstrates a remarkable 2-oxoisovalerate decarboxylase activity, which along with its high GDH activity makes the strain particularly useful in enhancing cheese flavour formation 1.4.1.4 glutamate dehydrogenase (NADP+) food industry is responsible for the capacity of Lactococcus lactis strains to catabolize amino acids to aroma compounds, pGdh442 can be naturally transmitted to other Lactococcus lactis strains by using cadmium or zinc resistance as a selectable marker, new prospects to intensify and diversify the production of aroma compounds in cheese 1.4.3.3 D-amino-acid oxidase industry the enzyme is used as a biocatalyst for resolving racemic amino acid mixtures, as a tool for biosensing, and as a mechanism of herbicide resistance 1.4.3.10 putrescine oxidase food industry the immobilized enzyme may be used as a sensor for analysis of beer samples 1.4.3.11 L-glutamate oxidase food industry development of a polarographic biosensor for monosodium glutamate by immobilizing L-GLOD on polycarbonate membrane and attached with oxygen electrode with a push cap system, usage of the membrane for over 20 measurements, showing stability 1.4.3.11 L-glutamate oxidase industry displaying L-glutamate oxidase/L-amino acid oxidase on the Pichia pastoris surface generates a useful whole cell biocatalyst for 2-oxoglutarate production that can be applied in industry 1.4.3.22 diamine oxidase food industry degradation of biogenic amines 1.6.2.2 cytochrome-b5 reductase industry potential use of the enzyme in the food industry 1.6.3.1 NAD(P)H oxidase (H2O2-forming) industry mice lacking the NAD(P)H oxidase gp91phox subunit respond to exposure to single-walled carbon nanotubes with a marked accumulation of polymorphnuclear neutrophils and elevated levels of apoptotic cells in the lungs, production of pro-inflammatory cytokines, decreased production of the anti-inflammatory and pro-fibrotic cytokine, TGF-beta, and significantly lower levels of collagen deposition 1.7.1.6 azobenzene reductase industry azoreductases are favorable for the development of biodegradation process for azo dyes 1.7.1.6 azobenzene reductase industry culture of Bacillus velezensis seems to be a suitable candidate for further study for both decolourization and detoxification of azo dyes, resulting in their safe disposal 1.7.1.6 azobenzene reductase industry industrial use of the enzyme in the biodegradation process of azo compounds 1.8.2.1 sulfite dehydrogenase (cytochrome) food industry an electrochemical sulfite biosensor with SDH can be applied to the determination of sulfite in beer and wine samples 1.8.2.1 sulfite dehydrogenase (cytochrome) food industry the enzyme is used in biosensors for sulfite determination in wine samples 1.8.3.1 sulfite oxidase food industry artificial ETC composed of cytochrome c and sulfite oxidase formed by the layer-by-layer technique using a polyelectrolyte. The multilayer technology, e.g. sulfite oxidase-cyt c multilayer electrode may act as an anode in a bio-fuel cell and furthermore such multilayers may be exploited as a biosensor for the detection of sulfite, which is used as a preservative in wine and other foodstuffs 1.8.3.1 sulfite oxidase food industry biosensor for detection of sulfite in food and beverages 1.8.3.1 sulfite oxidase food industry useful for establishing biosensor systems for detection of sulfite in food and beverages considering the high sensitivity of biosensors and the increasing demand for such biosensor devices 1.8.3.2 thiol oxidase food industry application in flour-processing industry. Supplementation with recombinant rice quiescin sulfhydryl oxidase (rQSOX) improves the farinograph properties of dough, indicated by the increased dough stability time and decreases degree of softening, and enhanced viscoelastic properties of the dough. Addition of rQSOX (10 IU/g flour) provides remarkable improvement in specific volume (37%) and springiness (17%) of the steamed bread, and significantly reduces the hardness by half, which is attributed to the strengthened gluten network 1.10.3.1 catechol oxidase food industry PPO functions as an essential factor in the quality development of semi-finished tea products, especially black tea and Oolong tea 1.10.3.1 catechol oxidase food industry inhibition of catechol oxidase diminishes browning in Ataulfo mango and elevates food quality 1.10.3.1 catechol oxidase food industry inhibition of catechol oxidase diminishes browning in white radish and elevates food quality 1.10.3.1 catechol oxidase food industry inhibition of enzyme PPO is important in the food industry, due its role in browning 1.10.3.2 laccase food industry both laccase and tyrosinase increase the dough strength and improved the bread-making quality of white wheat flour breads, especially when used in combination with xylanase 1.10.3.2 laccase food industry potential for bioconversion of lignin rich agricultural byproducts into animal feed and cellulosic ethanol. The enzyme effectively improves in vitro digestibility of maize straw 1.10.3.2 laccase industry Pycnoporus sp. SYBC-L1 is a potential candidate for industrial application. It can be exploited for a number of industrial and environmental applications, such as paper pulping and bleaching, textile dye bleaching, bioremediation, and detoxification, overview 1.10.3.2 laccase industry the laccase has a wide application in industrial processes, particularly in renewable bio-energy industry 1.10.3.2 laccase industry delignification of sugar beet pulp. Delignification pretreatment is the most challenging and critical step in the recycling process of lignocellulosic materials as the most abundant natural resources on the earth and has a large impact on cellulose extraction, cellulose digestibility, and downstream costs. Amongst the various delignification strategies, the enzymatic method has been demonstrated as a promising eco-friendly process with no inhibitor generation, although it is not highly efficient 1.10.3.2 laccase industry potential use of the laccase in lignin modification 1.10.3.2 laccase industry the enzyme can be usedc in industrial bleaching processes, thermostable and acidophilic laccase that can efficiently decolorize several synthetic dyes without an expensive redox mediator 1.10.3.2 laccase industry the enzyme decoloures up to six different industrial dyes, with or without the use of redox mediators such as ABTS 1.10.3.2 laccase industry advantageous for laccases in industrial application as it acts as broad pH range acting enzyme 1.10.3.2 laccase industry application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry 1.10.3.2 laccase industry laccases can be considered as one of the most important biocatalyst which can be exploited for divergent industrial applications viz. paper pulp bleaching, fiber modification, dye decolorization, bioremediation as well as organic synthesis 1.10.3.2 laccase industry potential for industrial wastewater treatments 1.10.3.2 laccase industry the enzyme is able to decolorize efficiently a variety of chemical dyes, thus, being potentially applicable in textile and environmental industries 1.10.3.2 laccase industry the high thermostability makes LacG potentially useful for industrial applications 1.10.3.3 L-ascorbate oxidase food industry the food enzyme is intended to be used in baking processes and cereal-based processes. It does not raise safety concerns under the intended conditions of use 1.11.1.6 catalase industry enzyme has potential for application in industrial bleaching processes to remove residual hydrogen peroxide from process streams 1.11.1.6 catalase industry hydrogen peroxide scavenging enzyme 1.11.1.7 peroxidase food industry preservation of raw milk, yoghurt, and cheese 1.11.1.7 peroxidase food industry study of kinetic characterization, thermal stability and synergistic effect of temperature and pH for peroxidase (POD) and pectin methylesterase (PME) in tomato puree. Inactivation of both enzymes is very important, since these enzymes can have very negative effects on the color, odor, flavor and texture of juices and vegetable beverages during storage. The browning and loss of stability in juices and vegetable beverages, such as tomato puree, can be controlled by applying temperature and pH combinations capable of inactivating these enzymes in a total or partial way, but while respecting the limits organoleptic and legal for juices and vegetable beverages 1.11.1.7 peroxidase industry the enzyme is resistant towards the salts and thus, might be a good candidate for industrial exploitation 1.11.1.7 peroxidase industry the immobilized enzyme (entrapped onto a carboxymethyl cellulose/Fe3O4 magnetic hybrid material) maintains its activity upon storage at 4 and 25°C for 8 weeks, and upon recycling for up to 15 uses. It appears to be candidate for industrial applications 1.11.1.13 manganese peroxidase industry the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others 1.11.1.14 lignin peroxidase industry the enzyme can be used as biocatalytic in delignification (which is emerging owing to its superior selectivity, low energy consumption, and unparalleled sustainability) iIn the biorefinery utilizing lignocellulosic biomasses, lignin decomposition to value-added phenolic derivatives 1.11.1.16 versatile peroxidase industry the enzyme can be used in the treatment of industrial dye effluents. Paper pulp industries presently employ these ligninolytic enzymes for their pulp bleaching applications 1.12.2.1 cytochrome-c3 hydrogenase industry platinum (IV) recovery from an industrial effluent through a biosulphidogenic sulphate reducing bacteria consortium via a hydrogenase-cytochrome c3 enzyme system that removes electrons from hydrogen to the platinum metal that acts as a final electron acceptor 1.12.99.6 hydrogenase (acceptor) industry inhibition by dioxygen is a major drawback for the application of [FeFe]-hydrogenase in hydrogen fuel production or as electrocatalysts for hydrogen oxidation in fuel cells 1.13.11.12 linoleate 13S-lipoxygenase food industry lipoxygenase is widely used in food industry to improve aroma, rheological, or baking properties of foods 1.13.11.12 linoleate 13S-lipoxygenase food industry addition of LOX1 and LOX2 altered the elasticity as well as viscosity of dough prepared from bleached wheat flour, LOX improves the dough rheology 1.13.11.55 sulfur oxygenase/reductase industry Acidithiobacillus caldus is widely used in bio-leaching. It gains energy and electrons from oxidation of elemental sulfur and reduced inorganic sulfur compounds (RISCs) for carbon dioxide fixation and growth. Its sulfur oxidation system involves a truncated sulfur oxidation (Sox) system (omitting SoxCD), nonSox sulfur oxidation system similar to the sulfur oxidation in A. ferrooxidans, and sulfur oxygenase reductase (SOR) 1.13.12.7 firefly luciferase industry the enzyme is widely used in academia and industry due to its excellent sensitivity and dynamic range, and its ease of use 1.14.13.7 phenol 2-monooxygenase (NADPH) industry the enzyme is useful in degradation of industrial pollutants 1.14.18.1 tyrosinase food industry browning in fruits and vegetables is recognized as a serious problem in the food industry. Further studies are warranted to understand the PPO inhibitor in relation to the browning reaction of fruit during storage and processing 1.14.18.1 tyrosinase food industry inhibitors have good potential as antibrowning agents to be applied in real food systems 1.14.18.1 tyrosinase food industry PPO is a very important enzyme in the food industry because during the processing of fruits and vegetables any wounding may cause cell disruption and lead to the formation of quinones, and their interaction with amino acids and proteins will enhance the brown color produced 1.14.18.1 tyrosinase food industry the presence of this enzyme has a large impact in the food industry because it is the main enzyme involved in the undesirable browning of fruits and vegetables during processing and storage 1.14.18.1 tyrosinase food industry the enzymatic properties of PPO probably provide practical application in inhibiting the PPO activity and preventing enzymatic browning in the process of picking, transportation, processing and storage of fresh lotus seeds 1.14.19.47 acyl-lipid (9-3)-desaturase food industry product yields are markedly enhanced by codon optimization of the Pythium gene. The redundancy in substrate utilization of the enzyme the codon-optimized gene can be exploited as potential genetic tool for production of nutritionally important polyunsaturated fatty acids by reconstituting fatty acid profile in biological systems of commercial interest through n-3 or n-6 pathway 2.1.1.5 betaine-homocysteine S-methyltransferase food industry compared with the prepartum level, overall BHMT expression and enzyme activity increases 0.7-fold and 1.7-fold, respectively, soon after parturition. There is no overall effect of methionine or choline supplementation for BHMT expression or BHMT enzyme activity 2.1.1.159 theobromine synthase food industry large-scale production of transgenic enzyme-deficient Coffea arabica and Camellia sinensis plants are a practical possibilty for production of decaffeinated coffee or tea 2.1.1.159 theobromine synthase food industry treatment of endosperms with 0.05 mM salicylic acid leads to 11.8% increase in theobromine content. Caffeine shows an increase in both methyl jasmonate (14.4% increase) and salicylic acid (50 microM, 14.8% increase) treatments 2.1.1.160 caffeine synthase food industry large-scale production of transgenic enzyme-deficient Coffea arabica and Camellia sinensis plants are a practical possibilty for production of decaffeinated coffee or tea 2.1.1.160 caffeine synthase food industry producing low-caffeine tea through post-transcriptional silencing of caffeine synthase mRNA 2.1.1.160 caffeine synthase food industry treatment of endosperms with 0.05 mM salicylic acid leads to 11.8% increase in theobromine content. Caffeine shows an increase in both methyl jasmonate (14.4% increase) and salicylic acid (50 microM, 14.8% increase) treatments 2.2.1.1 transketolase industry production of abundant intermediates for industrially erythritol production 2.2.1.2 transaldolase industry production of abundant intermediates for industrially erythritol production 2.2.1.7 1-deoxy-D-xylulose-5-phosphate synthase industry Agrobacterium tumefaciens strain KCCM 10413, overexpressing the enzyme might be useful in industrial production of ubiquinone-10, i.e. UbiQ(10) 2.3.1.7 carnitine O-acetyltransferase food industry modulating aroma compounds during wine fermentation by manipulating carnitine acetyltransferases in Saccharomyces cerevisiae 2.3.1.20 diacylglycerol O-acyltransferase industry PtWS/DGAT is a bifunctional enzyme and may serve as a promising target for the engineering of microalga-based oils and waxes for industrial use 2.3.1.84 alcohol O-acetyltransferase food industry after 5 days of fermentation, the concentrations of ethyl acetate, isoamyl acetate, and isobutyl acetate in yellow rice wines fermented with yeasts overexpressing isoform ATF2 increase to 137.79 mg/L (an approximate 4.9fold increase relative to the parent cell), 26.68 mg/L, and 7.60 mg/L, respectively 2.3.1.133 shikimate O-hydroxycinnamoyltransferase industry the global trend toward a biomaterials-based economy makes plant cell walls increasingly important as renewable resources, HCT is a metabolic entry point leading to the biosynthesis of G-lignin in coniferous gymnosperms 2.3.1.158 phospholipid:diacylglycerol acyltransferase industry the strong lipase activity of PDAT with broad substrate specificity might be a potential biocatalyst for industrial lipid hydrolysis and conversion, particularly for biofuel production 2.3.1.165 6-methylsalicylic-acid synthase food industry the identified genes can be used as a target for PCR-based methodologies to detect the fungi responsible for producing patulin in the foodstuffs 2.3.2.2 gamma-glutamyltransferase food industry development of an enzymatic method involving Bacillus licheniformis GGT (BlGGT) for the synthesis of gamma-glutamyl-L-leucine (gamma-Glu-Leu) from glutamine and leucine, since the mass production of Kokumi peptides from natural resources in high purity generally involves several tedious and inefficient operation processes. Parameter optimization of the BlGGT-catalyzed reaction for the biocatalytic synthesis of this Kokumi-imparting molecule 2.3.2.2 gamma-glutamyltransferase food industry GGT has gained importance as a biotechnologically important catalyst in food sector. In food sector, GGT enzyme finds application in soy sauce industry, debittering of amino acids, synthesis of flavor enhancer, and nutraceutical peptides such as L-theanine 2.3.2.13 protein-glutamine gamma-glutamyltransferase food industry enzyme-catalyzed cross-linking is effective in improving functional properties of stirred yak yoghurt (treated yoghurt produces a strong acid gel, higher consistency, cohesiveness, index of viscosity, and creamier mouth feel than the untreated product). Furtermore, enzyme-treated yak yoghurt presents lower wet yak hair or sweat odor, or both. 2.3.2.13 protein-glutamine gamma-glutamyltransferase food industry gelatin is a soluble protein prepared by partial hydrolysis of collagen with widespread utility in food industry, and TGase has been used to enzymatically modify gelatin by forming cross-links to enhance its rheological properties. Gelatin can set to elastic gel on cooling below 35°C from disordered molecules to ordered network predominantly by hydrogen bonds, where TGase introduces additional covalent cross-linkages to improve gelation. Addition of TGase from Euphausia superba at 0.1 U/mg increases the gel strength, setting temperature, setting time, and melting temperature of cold-set gelatin gel. Properties of gelatin with addition of TGase purified from Antarctic krill, overview 2.3.2.13 protein-glutamine gamma-glutamyltransferase food industry microbial transglutaminase (MTG) is an enzyme widely used in the food industry 2.3.2.13 protein-glutamine gamma-glutamyltransferase food industry potential application of AcTG-1 as a biological cross-linker in the food industry, once binding occurs, fish fillets withstand further processing such as frying, boiling, freeze-thawing and chilling. The low-temperature activity and enzymatic properties of AcTG-1 appear to offer advantages over commercially available enzymatic glues in the food industry, overview 2.3.2.13 protein-glutamine gamma-glutamyltransferase food industry recombinant enzyme TGZo from Zea mays is suitable for food processing. Cross-linking in proteins by TGase leads to the change of protein functionalities such as water-holding capacity, solubility, gelation property, emulsifying capacity, and nutritional value. TGZo from Zea mays is tested for cow milk yoghurt production, method evaluation, overview. Plackett-Burman design and response surface methodolog. Texture analysis of cow milk yogurts cross-linked by different concentrations of TGZo 2.3.2.13 protein-glutamine gamma-glutamyltransferase food industry the enzyme is important in the food industry 2.3.2.13 protein-glutamine gamma-glutamyltransferase food industry the enzyme is widely exploited in the meat processing industries. Enzyme mTGase is also widely applied in other food and textile industries by catalysing the formation of isopeptide bonds between peptides or protein substrates 2.3.2.13 protein-glutamine gamma-glutamyltransferase food industry transglutaminase MTG-TX can be used in food-related applications in salty environment, e.g. bacon or seafood 2.3.3.10 hydroxymethylglutaryl-CoA synthase food industry overexpression of Brassica juncea wild-type and mutant (S359A) 3-hydroxy-3-methylglutaryl-coenzyme A synthase in Solanum lycopersicum, causes an accumulation of mevalonate-derived squalene and phytosterols, as well as methylerythritol phosphate (methylerythritol phosphate)-derived alpha-tocopherol (vitamin E) and carotenoids. Genes associated with the biosyntheses of C10, C15 and C20 universal precursors of isoprenoids, phytosterols, brassino-steroids, dolichols, methylerythritol phosphate, carotenoid and vitamin E are upregulated. In S359A tomato fruits, increased squalene and phytosterol contents over wild-type fruits are attributed to heightened SlHMGR2, SlFPS1, SlSQS and SlCYP710A11 expression. In both tomato wild-type and S359A fruits, the up-regulation of SlGPS and SlGGPPS1 in the mevalonate pathway that leads to alpha-tocopherol and carotenoid accumulation indicates cross-talk between the mevalonate and methylerythritol phosphate pathways. The manipulation of Brassica juncea 3-hydroxy-3-methylglutaryl-coenzyme A synthase 1 (HMGS1) represents a promising strategy to simultaneously elevate health-promoting squalene, phytosterols, alpha-tocopherol and carotenoids in tomato, an edible fruit 2.3.3.13 2-isopropylmalate synthase food industry in mutant strain T25 with L-leucine accumulation, a hetero allelic mutation in the LEU4 gene encoding the Gly516Ser variant alpha-isopropylmalate synthase is found. alpha-Isopropylmalate synthase activity of the Gly516Ser variant is less sensitive to feedback inhibition by L-leucine, leading to intracellular L-leucine accumulation. In a laboratory-scale test, awamori (a distilled alcoholic beverage made from steamed rice,) brewed with strain T25 shows higher concentrations of isoamyl alcohol and isoamyl acetate than that brewed with strain HC02-5-2. Such a combinatorial approach to yeast isolation, with whole genome analysis and metabolism-focused breeding, has the potentials to vary the quality of alcoholic beverages 2.4.1.4 amylosucrase food industry amylosucrase has great potential in the biotechnology and food industries, due to its multifunctional enzyme activities. It can synthesize alpha-1,4-glucans, like amylose, from sucrose as a sole substrate. It can also utilize various other molecules as acceptors. In addition, amylosucrase produces sucrose isomers such as turanose and trehalulose. It also efficiently synthesizes modified starch with increased ratios of slow digestive starch and resistant starch, and glucosylated functional compounds with increased water solubility and stability. It produces turnaose more efficiently than other carbohydrate-active enzymes. Amylose synthesized by amylosucrase forms microparticles and these can be utilized as biocompatible materials with various bio-applications, including drug delivery, chromatography, and bioanalytical sciences 2.4.1.4 amylosucrase food industry cyclodextrins are frequently utilized chemical substances in the food, pharmaceutical, cosmetics, and chemical industries. An enzymatic process for cyclodextrin production is developed by utilizing sucrose as raw material instead of corn starch. Cyclodextrin glucanotransferase from Paenibacillus macerans is applied to produce the cyclodextrins from linear alpha-(1,4)-glucans, which are obtained by Neisseria polysaccharea amylosucrase treatment on sucrose. The greatest cyclodextrin yield (21.1%, w/w) is achieved from a one-pot dual enzyme reaction at 40°C for 24 h. The maximum level of cyclodextrin production (15.1 mg/ml) is achieved with 0.5 M sucrose in a simultaneous mode of dual enzyme reaction, whereas the reaction with 0.1 M sucrose is the most efficient with regard to conversion yield. Dual enzyme synthesis of cyclodextrins is successfully carried out with no need of starch material. Efficient bioconversion process that does not require the high temperature necessary for starch liquefaction by thermostable alpha-amylase in conventional industrial processing 2.4.1.4 amylosucrase food industry the enzyme be a promising candidate for food industrial production of linear alpha-(1,4)-glucans and turanose as a next generation sweetener 2.4.1.4 amylosucrase food industry the study investigates the differences in structural and physicochemical properties, especially contents of resistant starch, between native and acid-thinned waxy corn starches treated with amylosucrase from Neisseria polysaccharea. The enzyme exhibits similar catalytic efficiency for both forms of starch. The modified starches have higher proportions of long (DP > 33) and intermediate chains (DP 13-33), and X-ray diffraction showesa B-type crystalline structure for all modified starches. With increasing reaction time, the relative crystallinity and endothermic enthalpy of the modified starches gradually decreases, whereas the melting peak temperatures and resistant starch contents increases. Slight differences are observed in thermal parameters, relative crystallinity, and branch chain length distribution between the modified native and acid-thinned starches. The digestibility of the modified starches is not affected by acid hydrolysis pretreatment, but is affected by the percentage of intermediate and long chains 2.4.1.4 amylosucrase industry cyclodextrins are frequently utilized chemical substances in the food, pharmaceutical, cosmetics, and chemical industries. An enzymatic process for cyclodextrin production is developed by utilizing sucrose as raw material instead of corn starch. Cyclodextrin glucanotransferase from Paenibacillus macerans is applied to produce the cyclodextrins from linear alpha-(1,4)-glucans, which are obtained by Neisseria polysaccharea amylosucrase treatment on sucrose. The greatest cyclodextrin yield (21.1%, w/w) is achieved from a one-pot dual enzyme reaction at 40°C for 24 h. The maximum level of cyclodextrin production (15.1 mg/ml) is achieved with 0.5 M sucrose in a simultaneous mode of dual enzyme reaction, whereas the reaction with 0.1 M sucrose is the most efficient with regard to conversion yield. Dual enzyme synthesis of cyclodextrins is successfully carried out with no need of starch material. Efficient bioconversion process that does not require the high temperature necessary for starch liquefaction by thermostable alpha-amylase in conventional industrial processing 2.4.1.4 amylosucrase industry the beta-carotene embedded amylose microparticles are prepared in one-step by utilizing the unique catalytic activity of amylosucrase from Deinococcus geothermalis, which synthesizes linear amylose chains using sucrose as the sole substrate. Synthesized amylose chains self-assembled with b-carotene to form well-defined spherical microparticles with an encapsulation yield of 65%. The synthetic method enables microparticle formation and beta-carotene encapsulation in one-step using amylosucrase and sucrose as the sole substrates, which indicates that the devised process may be cost-effective and suitable for industrial applications 2.4.1.4 amylosucrase industry the enzyme has great industrial potential owing to its multifunctional activities, including transglucosylation, polymerization, and isomerization 2.4.1.5 dextransucrase food industry the enzyme is used to produce kimchi in a fermentation process, which is improved by addition of Ca2+ salts that reduce lactic acid and elevate the pH for optimal activity of Leuconostoc bacteria 2.4.1.5 dextransucrase food industry the dextransucrase is responsible for production of dextran with predominant alpha-(1->6) linkages that might find applications as food hydrocolloids 2.4.1.5 dextransucrase food industry the enzyme from Weissella confusa strain VTT E-90392 is useful in dextran production during sour dough production. The hydrocolloidal properties of dextran can facilitate a more substantial use of wheat bran and counter the negative effects of bran on bread quality, optimization of enzymatic dextran production in wheat bran 2.4.1.5 dextransucrase food industry the enzyme is a good food additive for improving the textures of dairy products due to dextran synthesis, e.g. solidification of sucrose-supplemented milk by the enzyme 2.4.1.5 dextransucrase food industry the exopolysaccharides of Lactobacillus animalis TMW 1.971 improve the quality of gluten-free breads, they can be produced in situ to levels enabling baking applications 2.4.1.5 dextransucrase food industry the exopolysaccharides of Lactobacillus curvatus TMW 1.624 improve the quality of gluten-free breads, they can be produced in situ to levels enabling baking applications 2.4.1.5 dextransucrase food industry the exopolysaccharides of Lactobacillus reuteri TMW 1.106 improve the quality of gluten-free breads, they can be produced in situ to levels enabling baking applications 2.4.1.5 dextransucrase food industry biocatalytic conversion of sucrose into highly porous dextran. Response surface methodology is performed to optimize production conditions. Enhanced biocatalytic efficiency of 4.62fold is observed. The biopolymer produced under the optimized model can be utilized as an emulsifying, gelling, stabilizing and thickening agent in food industry 2.4.1.5 dextransucrase food industry efficient production of prebiotic glucooligosaccharides in orange juice using immobilized and co-immobilized dextransucrase. Immobilization enhances the operational and storage stability of dextransucrase. Two hundred milligrammes (2.4 IU/mg) of alginate beads (immobilized and co-immobilized) are found to be optimum for the production of glucooligosaccharides (GOS) in orange juice with a high degree of polymerization. The pulp of the orange juice does not interfere in the reaction. In the batch process, coimmobilized dextransucrase (41 g/l) produced a significantly higher amount of GOS than immobilized dextransucrase (37 g/l). Alginate entrapment enhances the thermal stability of dextransucrase for up to 3 days in orange juice at 30°C. The production of GOS in semicontinuous process is 39 g/l in coimmobilized dextransucrase and 33 g/l in immobilized dextransucrase 2.4.1.5 dextransucrase food industry immobilized enzyme is used successfully in synthesis of dextran and maltooligosaccharide with good prebiotic and fibrinolytic activities. Dextran 38397 and 125471 Da are yielded at enzyme protein concentration 4.78 and 5.78 mg, respectively. Proper dextrans (73378 and 117521 Da) demanded in pharmaceutical applications are achieved at 6% and 12% sucrose concentrations and at 4.78 and 5.78 mg enzyme protein concentration, respectively. Optimum temperature for conversion of glucose to dextran is 30°C (73% and 80% at 5.78 and 4.78 mg enzyme protein concentration, respectively). Varieties of maltooligosaccharides are yielded by synergistic cooperation between sucrose and maltose. Six maltooligosaccharide and three dextrans samples in vitro have prebiotic effect on Lactobacillus casei with degree of variation. Two samples of maltooligosaccharide with different degree of polymerization (DP) and three samples of dextran with different molecular weight (MW) reported different fibrinolytic activity 2.4.1.5 dextransucrase food industry important enzyme in food industry. Ultrasound is a tool for increasing the activity, thermal stability and rate of catalysis of dextransucrase and supplies a potential method for expanding the application of dextransucrase 2.4.1.5 dextransucrase food industry synthesis of caffeic acid-3-O-alpha-D-glucopyranoside. The production of caffeic acid-3-O-alpha-D-glucopyranoside at a concentration of 153 mM is optimized using 325 mM caffeic acid, 355 mM sucrose, and 650 mU/ml dextransucrase in the synthesis reaction. In comparison with the caffeic acid, the caffeic acid-3-O-alpha-D-glucopyranoside displays 3fold higher water solubility, 1.66fold higher antilipid peroxidation effect, 15% stronger inhibition of colon cancer cell growth, and 11.5fold higher browning resistance. These results indicate that caffeic acid-3-O-alpha-D-glucopyranoside may be a suitable functional component of food and pharmaceutical products 2.4.1.5 dextransucrase food industry synthesis of chlorogenic acid-4'-O-alpha-D-glucopyranoside, which is a functional component that may be used in the food or pharmaceutical industry. It displays greater physical properties, anti-lipid peroxidation effect, and growth inhibition of colon cancer cell than those of chlorogenic acid 2.4.1.5 dextransucrase food industry synthesis of glucosylated steviosides, which are more stable at pH 2, 60°C for 48 h than stevioside 2.4.1.5 dextransucrase food industry the enzyme catalzes the in vitro synthesis of prebiotic oligosaccharides in mango and pineapple juices. Sucrose content of the juices is eliminated resulting in its lower calorific value. Potential of dextransucrase for production of functional foods 2.4.1.5 dextransucrase food industry the enzyme synthesizes dextran and oligosaccharides, which act as prebiotics and are popularly used in such industries as food and medicine 2.4.1.5 dextransucrase industry the enzyme immobilized on calcium alginate as entrapment matrix can be utilized for synthesis of dextran and can be easily separated from the product, resulting in high purity of dextran 2.4.1.5 dextransucrase industry the immobilized biocatalyst has potential in many industrial applications 2.4.1.5 dextransucrase industry the increased reusability, higher pH range and storage stability of immobilized enzyme as compared with free enzyme can increase the sustainability and applicability of the enzyme in industries 2.4.1.7 sucrose phosphorylase industry the enzyme has a wide range of application in food, cosmetics, and pharmaceutical industries because of its broad substrate specificity 2.4.1.7 sucrose phosphorylase industry the enzyme is widely used in the food, cosmetics, and pharmaceutical industries 2.4.1.10 levansucrase food industry lactosucrose, a rare trisaccharide formed from sucrose and lactose by enzymatic transglycosylation, is a type of indigestible carbohydrate with a good prebiotic effect. Lactosucrose biosynthesis is efficiently carried out by a purified levansucrase from Leuconostoc mesenteroides B-512 2.4.1.10 levansucrase food industry the enzyme is interesting in food and pharmaceutical industries for synthesis of diverse sucrose analogues, hetero-oligosaccharides (especially lactosucrose), and interesting fructosides from a wide range of substrates, i.e. monosaccharides, disaccharides, and aromatic and alkyl alcohols 2.4.1.18 1,4-alpha-glucan branching enzyme food industry involved in the synthesis of highly-branched cyclic dextrin, a dextrin food ingredient 2.4.1.18 1,4-alpha-glucan branching enzyme food industry production of food ingredients 2.4.1.18 1,4-alpha-glucan branching enzyme food industry starch processiong to synthesize a food ingredient, highly branched cyclic dextrin 2.4.1.18 1,4-alpha-glucan branching enzyme food industry analyzation and characterization of reaction products of branching enzymes from different sources for starch processing to synthesize the food ingredient, highly branched cyclic dextrin 2.4.1.18 1,4-alpha-glucan branching enzyme food industry analyzation and characterization of reaction products of branching enzymes from different sources for starch processing to synthesize the food ingredient, highly branched cyclic dextrin. The amount of short chains with a degree of polymerization of 6-8 is signifi cantly increased in the product of Bacillus cereus 2.4.1.18 1,4-alpha-glucan branching enzyme food industry analyzation and characterization of reaction products of branching enzymes from different sources for starch processing to synthesize the food ingredient, highly branched cyclic dextrin. The amount of short chains with a degree of polymerization of 6-8 is significantly increased in the product of Phaseolus vulgaris 2.4.1.18 1,4-alpha-glucan branching enzyme food industry addition of RmGBE to wheat bread results in a 26% increase in specific volume and a 38% decrease in crumb firmness in comparison with the control. Besides, the retrogradation of bread is significantly retarded along with the enzyme reaction. These properties make RmGBE highly useful in the food and starch industries 2.4.1.18 1,4-alpha-glucan branching enzyme food industry addition of enzyme to wheat bread increases specific volume and decreases crumb firmness during bread storage. In addition, the enzyme can significantly retard the retrogradation and improve the quality of bread 2.4.1.18 1,4-alpha-glucan branching enzyme food industry enzyme treatment reduces the rate of starch retrogradation 2.4.1.19 cyclomaltodextrin glucanotransferase food industry the enzyme can be used in the bread-baking process since its addition in the dough mix improved significantly the loaf volume and decreased the firmness of bread during storage 2.4.1.19 cyclomaltodextrin glucanotransferase food industry the enzyme improves the sweetness and edulcorant quality of stevioside 2.4.1.19 cyclomaltodextrin glucanotransferase food industry the enzyme leads to an improvement in the technological quality of gluten-free laminated baked products 2.4.1.19 cyclomaltodextrin glucanotransferase food industry cyclodextrins are frequently utilized chemical substances in the food, pharmaceutical, cosmetics, and chemical industries. An enzymatic process for cyclodextrin production is developed by utilizing sucrose as raw material instead of corn starch. Cyclodextrin glucanotransferase from Paenibacillus macerans is applied to produce the cyclodextrins from linear alpha-(1,4)-glucans, which are obtained by Neisseria polysaccharea amylosucrase treatment on sucrose. The greatest cyclodextrin yield (21.1%, w/w) is achieved from a one-pot dual enzyme reaction at 40°C for 24 h. The maximum level of cyclodextrin production (15.1 mg/ml) is achieved with 0.5 M sucrose in a simultaneous mode of dual enzyme reaction, whereas the reaction with 0.1 M sucrose is the most efficient with regard to conversion yield. Dual enzyme synthesis of cyclodextrins is successfully carried out with no need of starch material. Efficient bioconversion process that does not require the high temperature necessary for starch liquefaction by thermostable alpha-amylase in conventional industrial processing 2.4.1.19 cyclomaltodextrin glucanotransferase industry cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst 2.4.1.19 cyclomaltodextrin glucanotransferase industry cyclodextrins are frequently utilized chemical substances in the food, pharmaceutical, cosmetics, and chemical industries. An enzymatic process for cyclodextrin production is developed by utilizing sucrose as raw material instead of corn starch. Cyclodextrin glucanotransferase from Paenibacillus macerans is applied to produce the cyclodextrins from linear alpha-(1,4)-glucans, which are obtained by Neisseria polysaccharea amylosucrase treatment on sucrose. The greatest cyclodextrin yield (21.1%, w/w) is achieved from a one-pot dual enzyme reaction at 40°C for 24 h. The maximum level of cyclodextrin production (15.1 mg/ml) is achieved with 0.5 M sucrose in a simultaneous mode of dual enzyme reaction, whereas the reaction with 0.1 M sucrose is the most efficient with regard to conversion yield. Dual enzyme synthesis of cyclodextrins is successfully carried out with no need of starch material. Efficient bioconversion process that does not require the high temperature necessary for starch liquefaction by thermostable alpha-amylase in conventional industrial processing 2.4.1.21 starch synthase (glycosyl-transferring) food industry resistant starch (RS) has the potential to protect against diabetes and reduce the incidence of diarrhea, inflammatory bowel disease, colon cancer, and chronic renal and hepatic diseases. Soluble starch synthase SSIIIa has a critical role in synthesizing resistant starch in rice 2.4.1.25 4-alpha-glucanotransferase food industry thermostable 4-alpha-glucanotransferase from Thermus scotoductus is used for rice cake production 2.4.1.25 4-alpha-glucanotransferase food industry TmalphaGT can be used to produce granular corn starch, which contains amylose and amylopectin having lower molecular weights and a thermoreversible gelation property 2.4.1.25 4-alpha-glucanotransferase food industry the disproportionating enzyme 4alphaGTase, is used to modify the structural properties of rice starch to produce a suitable fat substitute in reduced-fat mayonnaise. The mayonnaise fat is partially substituted with the 4alphaGTase-treated starch paste at levels up to 50% in combination with xanthan gum. All mayonnaises exhibit shear thinning behavior and yield stress. Viscoelastic properties of mayonnaise are altered, and the mayonnaises exhibited weak gel-like properties. The magnitude of elastic and loss moduli is also affected by 4alphaGTase-treated starch concentration and presence of xanthan gum, microstructure, method, overview 2.4.1.B34 4,6-alpha-glucanotransferase food industry during the process of cooking wheat, semicrystallized chains of raw starch are hydrated into an amorphous form. After they have cooled for a sufficiently long period, linear molecules, amylose, and linear parts of amylopectin molecules expel water and rearrange into a more crystalline structure. This recrystallization, called retrogradation, often leads to the formation of hard and digestive enzyme-inaccessible textures in some wheat-based foods, resulting in poor sensory quality, short shelf life, and low consumer acceptance. After the GtfB-modified wheat starches are gelatinized and stored at 4°C for 1-2 weeks, their endothermic enthalpies are significantly lower than that of the control sample, indicating low retrogradation rates 2.4.1.210 limonoid glucosyltransferase food industry Limonoid glucosyltransferase is an enzyme that catalyzes the conversion of bitter limonoid into non-bitter limonoid glucoside while retaining the health benefit of limonoids in the juice. The immobilization of this enzyme in a column can solve the juice bitterness problem 2.4.1.210 limonoid glucosyltransferase food industry Citxadrus limonoid glucosyltransferase which is a key playxader for natural debitterness and anticancerous potenxadtial, can be utilized for metabolic engineering of Citxadrus limonoids to get rid of delayed bitterness problem along with enhanced limonoid glucoside molecules. The presence or absence of LGT can serve as a molecxadular indicator for determining the level of accumulaxadtion of limonoid glucoside and may reflect ultimately the possibility of delayed bitterness in available Citrus germplasm. Enhanced activity of LGT in citrus fruits may increase the glucoside level, which in turn will reduce the bitterness problem 2.4.1.210 limonoid glucosyltransferase food industry major problem in the orange industry is delayed bitterness, which is caused by limonin, a bitter compound developing from its non-bitter precursor limonoate A-ring lactone (LARL) during and after extraction of orange juice. The glucosidation of LARL by limonoid UDP-glucosyltransferase (LGT) to form non-bitter glycosyl-limonin during orange maturation has been demonstrated as a natural way to debitter by preventing the formation of limonin. Enzyme LGT activity can be used to develop biotechnology-based approaches for producing orange juice from varietals that traditionally have a delayed bitterness 2.4.1.210 limonoid glucosyltransferase food industry overexpression of the LGT gene can reduce the delayed bitterness problem in citrus juice 2.4.1.236 flavanone 7-O-glucoside 2''-O-beta-L-rhamnosyltransferase food industry the study provides the basis for potentially improving the taste in citrus fruit through manipulation of the network by knocking-out 1,2-rhamnosyltransferase or by enhancing the expression of flavonoid-7-O-di-glucosyltransferases using genetic transformation 2.4.1.242 NDP-glucose-starch glucosyltransferase food industry because waxy wheat starch has greater water absorbance and resistance to retrogradation than normal starch, its inclusion in flour blends has been suggested as a means of improving the texture and appearance of bakery products and noodles. The results indicate that wheat encoding functional homeologs of GBSS1 produces starch that has potential in the production of certain food items, such as Asian noodles 2.5.1.21 squalene synthase industry squalene has industrial value as a lubricant, health promoting agent, and/or drop-in biofuel, establishment of an efficient Escherichia coli-based system for squalene production 2.5.1.29 geranylgeranyl diphosphate synthase food industry the enzyme in Xanthophyllomyces is used for production of astaxanthin, i.e. 3,3'-hydroxy-4,4'-diketo-beta-carotene, which is an industrially important carotenoid used for feeding salmon or trout in farming 2.5.1.32 15-cis-phytoene synthase food industry developement nutritional plants enriched with carotenoids 2.5.1.62 chlorophyll synthase food industry changes of chlorophyll and its derivatives in postharvest tea leaves under different low-temperature treatments. At the initial stage of withering, a significant increase is observed in the chlorophyll content, expression of chlorophyll-synthesis-related enzymes and chlorophyll synthase activity in newly picked tea leaves. CHLG expression exhibits a steady decrease during the withering process. An obvious decrease is found in the content of L-glutamate as the foremost precursor substance of chlorophyll synthesis 2.6.1.B3 aminopentol:pyruvate aminotransferase FumI food industry enzymatic detoxification of fumonisins in animal feed and potentially also in foodstuffs intended for human consumption, improvement of food and feed safety 2.7.1.1 hexokinase industry production of abundant intermediates for industrially erythritol production 2.7.1.23 NAD+ kinase industry preparation of a superparamagnetic NAD kinase catalyst to synthesize NADP in vitro 2.7.2.1 acetate kinase industry enzyme involved in the wasteful production of acetate during conversion of cellulose to ethanol 2.7.2.4 aspartate kinase food industry L-lysine, one of the essential amino acids required for nutrition in animals and humans, is widely used in the food industry, medical industry, etc. L-lysine has been mainly produced by microbial fermentation employing mutant strains of bacteria. An L-lysine high-yielding strain is developed by modification of aspartokinase III and dihydrodipicolinate synthetase 2.7.2.7 butyrate kinase industry development of biologically based chemicals and fuels 2.7.4.1 ATP-polyphosphate phosphotransferase industry copper polyphosphate kinase hybrid nanoflower (ArPPK2-Cu3(PO4)2·3H2O nanoflower) has an application potential in industrial catalytic processes that are coupled with ADP-dependent enzymes 2.7.4.33 AMP-polyphosphate phosphotransferase food industry AMP is known to have potential for use as a reliable indicator in hygiene monitoring, the development of a sensitive method for detecting AMP, by using polyphosphate-AMP phosphotransferase and adenylate kinase in conjugation with firefly luciferase, is useful to detect food samples with high sensitivity 2.7.8.8 CDP-diacylglycerol-serine O-phosphatidyltransferase food industry phospholipids, especially phosphatidylserine, have many applications in functional food and pharmaceutical industries 2.7.9.4 alpha-glucan, water dikinase food industry rice starch contains only low concentrations of starch bound phosphate monoesters, which limits its usage in various industrial processes. Six stable individual transgenic lines with hyper-phosphorylated starch are produced by the overexpression of the StGWD1 in rice (Oryza sativa japonica cv. Zhonghua 11). The transgenic lines have 9fold and double higher Glc-6-P and Glc-3-P, respectively and increased amylose content. The starch granules display only minor morphological alterations, notably the presence of surface pores and moderately distorted edges and surfaces. The novel starch introduces unique combinations of functionality for rice starch, such as reduced gelatinization temperature, decreased pasting viscosity, increased gel formation capacity and increased gel hardness 2.7.11.31 [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase industry AMPK as a molecular target capable of modifying energy substrate utilization may result in the development of new technologies that increase milk production or modify milk composition during periods of increased energy demand 3.1.1.1 carboxylesterase industry the enzyme is highly thermostable (half-life of 107.9 min at 85°C), suggesting that E34Tt-His6 has potential for industrial applications 3.1.1.3 triacylglycerol lipase food industry protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats 3.1.1.4 phospholipase A2 food industry PLA2 stability in the presence of organic solvents, as well as in acidic and alkaline pH and at high temperature makes it a good candidate for its application in food industry 3.1.1.4 phospholipase A2 industry application in oil degumming. In the enzymatic degumming process, the phosphorus content is reduced to 20.74 mg/kg within 6 h, which is promising for the industrial application 3.1.1.6 acetylesterase industry cooperative action on birchwood xylan degradation in combination with Streptomyces sp. xylanase and beta xylosidase, production of biofuels utilizing hemicelluloses containing acetyl xylan, 1.16fold to 1.39fold increased sugar release 3.1.1.6 acetylesterase industry enhancement of sensory quality in alcoholic beverage through higher activity of Saccharomyces cerevisiae EAHase in mixed culture with Pichia anomala low respirating mutant 3.1.1.6 acetylesterase industry enhancement of sensory quality in alcoholic beverage through higher activity of Saccharomyces cerevisiae EAHase in mixed culture with Pichia anomala mutant with respiration deficiency 3.1.1.6 acetylesterase industry use of the very active biocatalyst EST1 for chiral resolution of 1,2-O-isopropylidene glycol esters 3.1.1.B10 p-coumaroyl esterase food industry the enzyme is used to decrease 5-O-chlorogenic acid content in coffee powder. As chlorogenic acids are suspected to cause stomach irritating effects in sensitive people, the enzyme treatment offers a technically feasible approach to improve the quality of coffee beverages by reducing 5-O-chlorogenic acid concentration without significantly affecting the aroma and taste profile 3.1.1.11 pectinesterase food industry added as exogenous enzyme in fruit and vegetable processing, used to increase the yield during extraction, to clarify and concentrate fruit juices, for gelation of fruit, and to modify texture and rheology of fruit and vegetable based products 3.1.1.11 pectinesterase food industry destabilizes pectinaceous materials in fruit juices and concentrates and modifies the texture of fruit and vegetable products 3.1.1.11 pectinesterase food industry enzyme is known to be responsible for cloud loss in juice processing and storage 3.1.1.11 pectinesterase food industry one of the most important enzymes in the industrialization and preservation of fruits, juices or other industrial products that involve the presence or absence of intact pectin 3.1.1.11 pectinesterase food industry responsible for phase separation and cloud loss in fruit juice manufacturing 3.1.1.11 pectinesterase food industry used for juice clarification and gelation of frozen concentrates, destabilizing agent for pectin material in fruit juices and concentrates 3.1.1.11 pectinesterase food industry used for various applications in fruit processing e.g. texture improvement of fruit pieces, juice extraction, concentration and clarification of fruit juices 3.1.1.11 pectinesterase food industry PME has a higher thermal resistance than the bacteria and yeasts existing in orange juice, therefore its inactivation is used as a parameter to define the time/temperature combination of the thermal process of pasteurisation of orange juice, which is necessary to prevent spoilage, overview 3.1.1.11 pectinesterase food industry inhibition of pectin methylesterase directly after juice extraction is crucial in the production of storable citrus juice products 3.1.1.11 pectinesterase food industry PME (0.12% (v/v)) and Ca2+ (0.5% (w/w)) in osmotic sugar solutions positively affect the relative hardness of dehydrated strawberry fruits, which is ascribed to the effect of PME and Ca2+ on the cell wall strength of the tissue (no cell wall damage and tissue particle alterations are observed upon dehydration) 3.1.1.11 pectinesterase food industry exogenous pectin methylesterase is applied in texture engineering of thermally processed intact fruits and vegetables, for example, via enzyme infusion 3.1.1.11 pectinesterase food industry pectin methylesterase can positively or negatively affect structural quality of plant-based foods (cloud stability, viscosity, texture) 3.1.1.11 pectinesterase food industry total pectin methylesterase activity is an indicator of freshness that is universally applicable to Citrus juices derived from orange, mandarin, and lemon or blends thereof 3.1.1.11 pectinesterase food industry due to very high de-esterification activity, easy denaturation and significant efficacy in incrementing clarification of fruit juice makes the enzyme useful for industrial application 3.1.1.11 pectinesterase food industry the enzyme enhances the pectin degradation process in apple juice clarification 3.1.1.11 pectinesterase food industry pectin methylesterase (PME) is a ubiquitous cell wall enzyme, which de-esterifies and modifies pectins for food applications. The papaya PME can be potentially utilized to modify pectin functionality at elevated temperature 3.1.1.11 pectinesterase food industry the enzyme is suitable for both acidic and alkaline processing, such as coffee and tea fermentation 3.1.1.11 pectinesterase food industry study of kinetic characterization, thermal stability and synergistic effect of temperature and pH for peroxidase (POD) and pectin methylesterase (PME) in tomato puree. Inactivation of both enzymes is very important, since these enzymes can have very negative effects on the color, odor, flavor and texture of juices and vegetable beverages during storage. The browning and loss of stability in juices and vegetable beverages, such as tomato puree, can be controlled by applying temperature and pH combinations capable of inactivating these enzymes in a total or partial way, but while respecting the limits organoleptic and legal for juices and vegetable beverages 3.1.1.11 pectinesterase industry CtPME can be potentially used in food and textile industry applications 3.1.1.20 tannase food industry the enzyme could be used in the food processing industry 3.1.1.20 tannase food industry the enzyme could find potential use in the food-processing industry 3.1.1.20 tannase food industry the enzyme is a food processing enzyme used in food, brewing, and feed industry 3.1.1.20 tannase food industry the enzyme is found to be useful in the manufacture of instant tea, acron wine, coffee-flavoured soft drinks, clarification of beer and fruit juices 3.1.1.20 tannase food industry the enzyme is useful in the food-processing industry 3.1.1.20 tannase food industry fruit juice debittering 3.1.1.20 tannase food industry the enzyme is used in food and beverage processing, and some of the major commercial applications are the preparation of instant tea, acorn liquor and production of gallic acid 3.1.1.20 tannase food industry the use of Lactobacillus plantarum tannase is an adequate alternative to the fungal tannases currently used in the food industry. Use of tannase may provide an efficient means for obtaining molecules with valuable activities from the degradation of complex tannins present in food and agricultural wastes 3.1.1.20 tannase food industry tannase is a potential agent for the manufacture of instant tea (tea cream solubilisation) 3.1.1.20 tannase food industry the enzyme is used in the manufacture of instant tea, beer, fruit juices, some wines and gallic acid 3.1.1.20 tannase food industry tannin acyl hydrolase catalyzes the hydrolysis of hydrolyzable tannins. It is used in the manufacture of instant tea and in the production of gallic acid 3.1.1.20 tannase industry in a short period of time the organism produces a large amount of tannase in an agricultural byproduct and cheap substrate like wheat bran, so in future, this organism can be applied for commercial tannase production. Broad range of pH and temperature stability of the enzyme can be exploited in various ways for pollution control in the leather industry and bioprocess industry in future 3.1.1.32 phospholipase A1 food industry the enzyme improves foaming stability and properties of skim milk and whey, implying that phospholipases can be useful tools for modifying the functionality of dairy products and ingredients 3.1.1.32 phospholipase A1 industry enzyme can be used for degumming crude plant oil 3.1.1.42 chlorogenate hydrolase food industry the treatment of the wheat dough with the recombinant enzyme causes a softening. The enzyme does not increase the specific bread volume, but improves dough handling. The enzyme may be effective to improve the taste and digestibility of coffee beverages 3.1.1.73 feruloyl esterase food industry Aspergillus awamori is applicable to food production and Awamori production. 3.1.1.73 feruloyl esterase food industry ferulic acid released from plant cell wall by the action of FAEs is an effective natural antioxidant with potential applications in the pharmaceutical and food industries 3.1.1.73 feruloyl esterase food industry industrial production of ferulic acid for use in the food industry 3.1.1.73 feruloyl esterase food industry release of phenolic acids 3.1.1.73 feruloyl esterase food industry The production of low-cost cell-wall-deconstructing enzymes on agro-industrial by-products could lead to the production of low-cost enzymes for use in the valorisation of food processing wastes. 3.1.1.73 feruloyl esterase food industry the enzyme shows stable activity at pH 3 and 50°C, thus the enzyme is acid tolerant, but not heat tolerant, making this enzyme useful for food production 3.1.1.73 feruloyl esterase food industry potential for the application of Aspergillus tubingensis enzyme extract in coffee processing. Crude enzyme extracts, containing feruloyl esterase and polygalacturonase, removes the mucilage of coffee cherries within 3 h, which is substantially more efficient than traditional fermentation, the viscosity of coffee mucilage is reduced to 80% by a 3-h treatment with the crudeenzyme extract at 50°C. Total chlorogenic acid in the green beans decreases to 67.3%, while a decline of only 14.3% is observed in the traditionally fermented group. On the other hand, chlorogenic acid lactones in the roasted beans are reduced to 63.9%, and a 37.2% decline in the chlorogenic acid content is detected 3.1.1.73 feruloyl esterase industry bioproduction of ferulic acid from triticale bran by alkaline and thermostable FAE 3.1.1.73 feruloyl esterase industry molecular details of Est1E from the suite of fiber-degrading enzymes from important rumen bacterium is a step toward mapping the complex conversion of plant biomass to valuable products-meat and milk-by ruminants 3.1.1.73 feruloyl esterase industry targeting FAEA expression to the Golgi or apoplast is likely to be an effective strategy for improving wall digestibility in grass species used for fodder or cellulosic ethanol production 3.1.1.74 cutinase industry Cutinase is used as a lipolytic enzyme in the composition of laundry and dishwashing detergents to more efficiently remove immobilized fats. The oleochemistry industries and pollutant degradation represent other potential uses of cutinase. 3.1.1.74 cutinase industry key for the design of biocatalysts with sufficient stability for practical applications in detergent industry 3.1.1.74 cutinase industry useful as biocatalysts in systems involving hydrolysis, esterification, and transesterification reactions 3.1.1.74 cutinase industry useful as biocatalysts in systems involving hydrolysis, esterification, and transesterification reactions. Cutinase proves to be the most well fitted enzyme for the detection of pesticide residues in foods even at very low levels. Use in fiber modification due to its hydrophobic nature and activity against biopolyesters present in plant cuticle. Use of cutinase to improve the wetting of cotton fibers. Cutinase is potentially useful for the removal of fats in laundry, but the unfolding of the enzyme in the presence of anionic surfactants limits its widespread use as an additive in industrial laundry detergents. Displays a stability profile that is well-fitted to the industrial process 3.1.1.74 cutinase industry useful as biocatalysts in systems involving hydrolysis, esterification, and transesterification reactions. Displays a stability profile that is well-fitted to the industrial process 3.1.1.74 cutinase industry the enzyme is mainly utilized in textile industry 3.1.1.74 cutinase industry use of enzyme preadsorbed on cotton to esterify the hydroxyl groups of cellulose with the fatty acids from triolein. The cutinase-catalyzed esterification of the surface of cotton fabric leads to modified cotton fabric that shows a significant increase of hydrophobicity 3.1.1.75 poly(3-hydroxybutyrate) depolymerase industry extracellular polyhydroxybutyrate depolymerase is an excellent thermostable candidate biocatalyst for environmental, industrial, and medical applications 3.1.1.81 quorum-quenching N-acyl-homoserine lactonase food industry infectious diseases caused by Aeromonas hydrophila is the major problem in aquaculture production. Effects of dietary Lactobacillus plantarum or/and N-acylated homoserine lactonase (AHL lactonase) on controlling Aeromonas hydrophila infection in juvenile hybrid tilapia. Dietary Lactobacillus plantarum or/and AHL lactonase reduce the extent of intestine damage, to a level similar as control fed fish (tilapia), not exposed to Aeromonas hydrophila 3.1.1.87 fumonisin B1 esterase food industry enzymatic detoxification of fumonisins in animal feed and potentially also in foodstuffs intended for human consumption, improvement of food and feed safety 3.1.1.87 fumonisin B1 esterase food industry feed additive combining two specific biotransformation processes is able to partially or totally neutralize the toxic effects induced by deoxynivalenol and fumonsins 3.1.1.88 pyrethroid hydrolase food industry high potential for bioremediation of pyrethroid-contaminated vegetables 3.1.1.112 isoamyl acetate esteras food industry balance of enzyme activities of alcohol acetyltransferase AATFase and isoamyl acetate esterase Iah1 is important for optimum production of isoamyl acetate in sake brewing. The amount of isoamyl acetate in the sake increases with an increasing ratio of AATFase/Iah1 esterase activity 3.1.1.117 (4-O-methyl)-D-glucuronate---lignin esterase industry the enzyme is a potentially industrially applicable enzyme due to its characteristic as a thermophilic enzyme with the favorable temperature of 40-50°C at pH 5 3.1.2.14 oleoyl-[acyl-carrier-protein] hydrolase industry contribution of FatA to the synthesis of castor oil 3.1.2.14 oleoyl-[acyl-carrier-protein] hydrolase industry contribution of FatB to the synthesis of castor oil 3.1.2.14 oleoyl-[acyl-carrier-protein] hydrolase industry FATB1 can function as a saturated acyl-ACP TE and may potentially modify the seed oil to increase its levels of palmitate 3.1.3.1 alkaline phosphatase food industry quantification of alkaline phosphatase by using a monoclonal antibody-based immunoassay immunoassay is appropriate for determining mild time/temperature treatment of milk and for the control of milk pasteurization 3.1.3.1 alkaline phosphatase food industry marker for milk pasteurization 3.1.3.8 3-phytase food industry Pediococcus pentosaceus strains KTU05-9 and KTU05-8 are recommended to use as a starter for sourdough preparation for increasing of mineral bioavailability from wholemeal wheat bread 3.1.3.8 3-phytase food industry the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes 3.1.3.8 3-phytase food industry the enzyme can be applied in dephytinizing animal feeds, and the baking industry. Effect of phytase supplementation in different doses on bread characteristics, overview 3.1.3.8 3-phytase food industry the phytase from Wickerhamomyces anomalus has adequate thermostability for its applicability as a food and feed additive, applicability of recombinant PPHY in dephytinization of wheat bread, overview 3.1.3.8 3-phytase food industry the recombinant enzyme rSt-Phy is useful in dephytinization of tandoori and naan (unleavened flat Indian breads), and bread, liberating soluble inorganic phosphate that mitigates anti-nutrient effects of phytic acid 3.1.3.26 4-phytase food industry Pediococcus pentosaceus strains KTU05-9 and KTU05-8 are recommended to use as a starter for sourdough preparation for increasing of mineral bioavailability from wholemeal wheat bread 3.1.3.26 4-phytase food industry the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes 3.1.3.26 4-phytase food industry the enzyme can be applied in dephytinizing animal feeds, and the baking industry. Effect of phytase supplementation in different doses on bread characteristics, overview 3.1.4.3 phospholipase C food industry the enzyme is used in vegetable oil refining by enzymatic phospholipid removal (degumming ) 3.1.4.11 phosphoinositide phospholipase C food industry the enzyme is used in industrial soybean oil degumming 3.2.1.1 alpha-amylase food industry starch has a protective effect on thermal stability of honey amylase. Therefore, it might be critical to process or control the amylase in honey before incorporation into starch-containing foods to aid in the preservation of starch functionality 3.2.1.1 alpha-amylase food industry the maltooligosaccharide forming endo-alpha-amylase is useful in bread making as an antistaling agent and it can be produced economically using low-cost sugarcane bagasse 3.2.1.1 alpha-amylase food industry important industrial enzyme in brewing and alcohol production 3.2.1.1 alpha-amylase industry could be useful in industrial operations such as brewing and food processing, due to their activity at low and high temperatures 3.2.1.1 alpha-amylase industry the alkaphilic nature of the enzyme with its stability is a interesting feature for possible industrial application 3.2.1.1 alpha-amylase industry the high cumulative activity and seven successive reuses obtained at liquefaction temperature render the covalently bound thermostable enzyme to calcium alginate matrix, a promising candidate for use in industrial starch hydrolysis process 3.2.1.1 alpha-amylase industry thermal stability of the wild-type and mutant enzymes fulfill the stability requirements for industrial processes 3.2.1.1 alpha-amylase industry application of the recombinant enzyme from Thermomyces dupontii expressed in Pichia pastoris in maltose syrup production 3.2.1.1 alpha-amylase industry possible applications of the immobilized alpha-amylase in the starch processing industry 3.2.1.2 beta-amylase industry the enzyme is important in industrial maltose production 3.2.1.2 beta-amylase industry the recombinant purified alpha-amylase enzyme from Thermotoga petrophila can be a potential candidate for use in many industrial processes; particularly, it can be helpful in starch saccharification due to the adaptive capability of the alpha-amylase to withstand unreceptive conditions used in industrial processes 3.2.1.2 beta-amylase industry amylases are important industrial enzymes used in starch liquefaction to produce glucose, fructose and maltose and also in brewing, baking, textile, paper, detergent and sugar industries 3.2.1.3 glucan 1,4-alpha-glucosidase food industry key enzyme in ripening and production of good taste in fermented tofu production, overview 3.2.1.3 glucan 1,4-alpha-glucosidase food industry ethanol production, production of sugars 3.2.1.3 glucan 1,4-alpha-glucosidase food industry glucoamylase is an important group of enzymes in starch processing in the food industries, as it is used for the production of glucose and fructose syrup from liquefied starch 3.2.1.3 glucan 1,4-alpha-glucosidase food industry the enzyme performs highly efficient hydrolysis of raw starches and direct conversion of raw corn and cassava flours via simultaneous saccharification and fermentation to ethanol suggesting that the enzyme has a number of potential applications in industrial starch processing and starch-based ethanol production. Effective hydrolysis of raw starch flour by the recombinant rPoGA15A preparation and alpha-amylase 3.2.1.3 glucan 1,4-alpha-glucosidase industry immobilization of the enzyme on polyaniline polymer allows an improved catalytic performance and application of the enzyme in industrial processes 3.2.1.3 glucan 1,4-alpha-glucosidase industry Rhizopus enzymes are useful in industrial applications 3.2.1.3 glucan 1,4-alpha-glucosidase industry the enzyme can be useful in industrial processing and hydrolysis of starch 3.2.1.3 glucan 1,4-alpha-glucosidase industry the enzyme is used in industrial starch degradation 3.2.1.3 glucan 1,4-alpha-glucosidase industry the enzyme is useful in industrial applications 3.2.1.3 glucan 1,4-alpha-glucosidase industry the enzyme is useful in industrial applications as glycoside hydrolase 3.2.1.3 glucan 1,4-alpha-glucosidase industry glucoamylase is used industrially to catalyze the hydrolysis of alpha-1,4-glycosidic bonds to release beta-D-glucose from the nonreducing ends of starch or oligosaccharides 3.2.1.3 glucan 1,4-alpha-glucosidase industry glucoamylases have been used with alpha-amylases for the industrial conversion of starch into glucose, intact cells of thermotolerant yeasts can be used as colloidal biocatalysts in starch degradation processes 3.2.1.3 glucan 1,4-alpha-glucosidase industry improvement in enzymatic desizing of starched cotton cloth using yeast codisplaying glucoamylase and cellulose-binding domain, overview 3.2.1.3 glucan 1,4-alpha-glucosidase industry an important industrial enzyme used in starch enzymatic saccharification 3.2.1.3 glucan 1,4-alpha-glucosidase industry glucoamylase from Aspergillus niger is an industrially important biocatalyst that is utilized in the mass production of glucose from raw starch or soluble oligosaccharides 3.2.1.3 glucan 1,4-alpha-glucosidase industry this glucoamylase may find important applications in the starch saccharification industry and in bioethanol production 3.2.1.3 glucan 1,4-alpha-glucosidase industry biotechnological applications of this glucoamylase from Aspergillus japonicus in the recycling and deinking process by the paper industries. Glucoamylases are used in food, pharmaceutical and textile industries 3.2.1.4 cellulase food industry extraction of pectins from apple pomace with monoactive preparation of endoxylanase and endcellulase. Pectin extracted with endocellulase has 1.5fold lower molecular mass but contains significantly more galacturonic acid (70.5%) of a high degree of methylation (66.3%). The simultaneous application of both enzymaticpreparations results in their cooperation, leading to a decrease of both the extraction efficiency and the molecular mass of pectin. This pectin displays the highest galacturonic acid (74.7%) and rhamnose contents 3.2.1.4 cellulase food industry the capacity of Cel8A to cleave 1,3-1,4-beta-glucans is significantly affected by the presence of the barley-based feed for broilers. Exogenous 1,3-1,4-beta-glucanases (EC 3.2.1.73) but not 1,4-beta-glucanases are obligatory enzymes to improve the nutritive value of barley-based diets for broilers. Enzyme is completely resistant to proteolytic inactivation after a 30 min incubation with pancreatic proteases 3.2.1.4 cellulase industry the purified enzyme performs well in biostoning of denim fabric at neutral pH 3.2.1.4 cellulase industry due to its acidophilic (pH 3.5) and high temperature stability (up to 90°C), CSCMCase may be useful for industrial application such as animal feed industry and clarification of fruit juices 3.2.1.4 cellulase industry enzyme possesses high power of defibrillation of textile and laundry. Polypeptide can be exploited for mass production and application in local industries 3.2.1.4 cellulase industry potent enzyme for industrial bioprocesses, including the bio-polishing of cotton products, food processing and bioethanol production 3.2.1.4 cellulase industry STCE1 may be appropriate for laundry use 3.2.1.4 cellulase industry because of its ability to hydrolyze celluloses at high temperatures above 90°C, as well as its thermostability, the enzyme is expected to be an excellent tool for industrial hydrolysis of cellulose, particularly for biopolishing of cotton products 3.2.1.4 cellulase industry textile and detergent industry, combination of CBH6A and EgGH45 3.2.1.4 cellulase industry economical analysis of cellulase production by solid-state fermentation in a pilot plant integrated to both a first and a second generation ethanol processes. Growth of Myceliophthora thermophila I-1D3b at 45°C during 96 h on sugarcane bagasse and wheat bran. shows that the process is economically attractive, due to its easy integration to the main process, and its revenue is up to four fold greater than electricity cogeneration 3.2.1.4 cellulase industry endoglucanases from family GH45 are applied in formulation of detergents and in industrial pulp and paper processes 3.2.1.4 cellulase industry enzyme Bc22Cel is a potential and useful candidate for industrial applications, such as the bioconversion of sugarcane bagasse to its derivatives 3.2.1.4 cellulase industry the enzyme is a promising candidate for industrial lignocellulosic biomass conversion. Generation of soluble oligosaccharides from lignocellulose is a critical step in bioethanol production. The enzyme produces cello-oligosaccharides and xylo-oligosaccharides from the continuous enzymatic saccharification of sodium carboxymethyl cellulose and xylan, respectively 3.2.1.4 cellulase industry the fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus has great potential in generating fermentable sugars from renewable agro-residues for biofuel and fine chemical industry. Application of the fusion enzyme (EG-M-Xyn)in combination with Ctec2 (commercial enzyme) in the saccharification leads to a 10-20% net increase in fermentable sugars liberated from pretreated rice straw in comparison to the Ctec2 alone 3.2.1.4 cellulase industry the thermophilic nature and biochemical properties of the enzyme indicate its potential suitability in industrial applications undertaken at high temperature, such as the production of second-generation bioethanol from lignocellulosic feedstocks and in the brewing industry 3.2.1.4 cellulase textile industry enzymatic deinking experiments, the ink removal rate in samples treated with the catalytic module is only slightly higher (about 8%), than that of untreated controls, whereas that of the EG1-treated samples is 100% higher. Bio-stoning of denim with EG1-CM results in increases of 48% and 40% in weight loss and indigo dye removal, respectively compared with untreated controls. These increases are considerably lower than the corresponding values of 219% and 133% obtained when samples are treated with EG1 3.2.1.6 endo-1,3(4)-beta-glucanase food industry construction of a transgenic yeast, Saccharomyces cerevisiae, expressing the enzyme, results in a food-grade yeast that has the potential to improve the brewing properties of beer 3.2.1.6 endo-1,3(4)-beta-glucanase food industry application in malting and brewing industry. Under simulated mashing conditions, addition of Agl9A at 20 U/ml or a commercial xylanase at 200 U/ml reduce the filtration rate by 26.71% and 20.21%, respectively, and viscosity by 6.12% and 4.78%, respectively. Combined use of Agl9A at 10 U/ml and the xylanase at 100 U/ml even more effectively reduces the filtration rate by 31.73% and viscosity by 8.79% 3.2.1.6 endo-1,3(4)-beta-glucanase food industry the enzyme reduces viscosity of mash during brewing peocesses 3.2.1.7 inulinase food industry the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps 3.2.1.7 inulinase industry Bacillus smithii T7 is a new thermophilic bacterium that can highly produce endoinulinase. The higher temperature optimum and greater thermostability of Bacillus smithii T7 are the desirable features for industrial production of inulinase that shall be a potential heat-resistant enzyme candidate for commercial use and enzyme functional research 3.2.1.7 inulinase industry higher inulinase activity from Kluyveromyces marxianus YS-1 is achieved by root powder extract of Asparagus officinalis. This plant material can be opted as a cheap inulin source for the production of inulinase 3.2.1.7 inulinase industry inulinase activity (115.0 U/ml) in liquid production medium by the mutant M-30 is the highest reported so far. Inulinase produced by the mutant M-30 of the marine yeast strain has potentially for use in biotechnological fields 3.2.1.7 inulinase industry inulinase produced by yeast strain CCMB 300 from the Brazilian semi-arid region has great potential to be used for inulin hydrolysis in the food industry 3.2.1.7 inulinase industry yeasts can produce more inulinase than bacteria 3.2.1.8 endo-1,4-beta-xylanase food industry changes in arabinoxylan during the breadmaking process are to a large extent caused by endogenous endoxylanases, whereas the contribution of microbial endoxylanases to these changes are very low. Endogenous endoxylanases affect the arabinoxylan population only during the fermentation phase and not during the mixing phase of breadmaking. Endoxylanases can, on the one hand, positively affect bread volume by solubilization of water unextractable arabinoxylan, but they can, on the other hand, also lead to unwanted stickiness 3.2.1.8 endo-1,4-beta-xylanase food industry contribution of microbial endoxylanases to changes in arabinoxylan during the breadmaking process are very low. Microbial endoxylanases end up in flour as contaminant and affect its functional properties 3.2.1.8 endo-1,4-beta-xylanase food industry high levels of endoxylanase activity in wheat flour should be avoided as they can cause uncontrolled degradation of arabinoxylan during bread dough processing, glutenstarch separation, or refrigerated dough storage 3.2.1.8 endo-1,4-beta-xylanase food industry improvement of cereal-based industrial processing by endoxylanase enzymes insensitive towards inhibitors 3.2.1.8 endo-1,4-beta-xylanase food industry wheat flour-associated endoxylanases are not active during dough mixing but exert their main effect during the fermentation phase of bread making. Wheat flour-associated endoxylanases can alter part of the arabinoxylan in dough, thereby changing their functionality in bread making and potentially affecting dough and end product properties 3.2.1.8 endo-1,4-beta-xylanase food industry endogenous endoxylanase activity during fermentation and storing can have negative effects on dough, the enzyme effect depends on the wheat variety's enzyme content and inhibitor content 3.2.1.8 endo-1,4-beta-xylanase food industry extraction of pectins from apple pomace with monoactive preparation of endoxylanase and endocellulase. Endoxylanase application results in the highest extraction efficiency of pectins (19.8%). The obtained polymer was characterised by a very high molecular mass, high level of neutral sugars (mainly arabinose, galactose and glucose), and very high degree of pectin methylation (73.4). The simultaneous application of both enzymatic preparations results in their cooperation, leading to a decrease of both the extraction efficiency and the molecular mass of pectin. This pectin is distinguished by the highest GalA (74.7%) and rhamnose contents 3.2.1.8 endo-1,4-beta-xylanase food industry extraction of pectins from apple pomace with monoactive preparation of endoxylanase and endcellulase. Pectin extracted with endocellulase has 1.5fold lower molecular mass but contains significantly more galacturonic acid (70.5%) of a high degree of methylation (66.3%). The simultaneous application of both enzymatic preparations results in their cooperation, leading to a decrease of both the extraction efficiency and the molecular mass of pectin. This pectin displays the highest galacturonic acid (74.7%) and rhamnose contents 3.2.1.8 endo-1,4-beta-xylanase food industry use of enzyme as an additive in the bread making process leads to a decrease in firmness, stiffness and consistency, and improvements in specific volume and reducing sugar content 3.2.1.8 endo-1,4-beta-xylanase food industry application of the extremely thermo- and alkali-stable enzyme for preparation of prebiotic xylooligosaccharides 3.2.1.8 endo-1,4-beta-xylanase food industry fruit juice clarification potential of GC25 xylanase at mild conditions. Pediococcus acidilactici strain GC25 xylanase causes a high increase in reducing sugar content after 30 min incubation at 40°C 3.2.1.8 endo-1,4-beta-xylanase food industry the ability of the enzym to produce xylobiose from agricultural and forestry residues proves that it is an excellent candidate enzyme in prebiotic and alternative sweetener industries 3.2.1.8 endo-1,4-beta-xylanase food industry the enzyme is important for industrial applications such as pretreatment of poultry cereals, bio-bleaching of wood pulp and degradation of plant biomass 3.2.1.8 endo-1,4-beta-xylanase food industry xylooligosaccharide derived from enzymatic hydrolysis of biopolymers is of considerable importance in preparing nutritional health oligosaccharides useful in food and pharmaceutical industries. To create added value products from hardwood xylan, xylanase (XynB) and alpha-glucuronidase (AguA) from Thermotoga maritima were co-produced in Escherichia coli through dual-promoter and bicistronic constructs 3.2.1.B8 malto-alpha-amylase (reducing end) food industry the enzyme might be of potential value in the food and starch industries due to its extreme thermostability 3.2.1.8 endo-1,4-beta-xylanase industry used for pulp bleaching 3.2.1.8 endo-1,4-beta-xylanase industry application as a pre-bleaching aid of apparent importance for pulp and paper industries 3.2.1.8 endo-1,4-beta-xylanase industry DNA shuffling improves the catalytic activity and alkaline pH stability of Thermobifida fusca xylanase A toward the hydrolysis of xylan evolved enzyme 2TfxA98 can meet the requirements of biobleaching by its stability and activation under conditions of alkaline and high temperatures 3.2.1.8 endo-1,4-beta-xylanase industry favorable properties of XynAS9, such as high activity over a wide temperature range, good thermal and pH stability, and less complex hydrolysis products, make this xylanase promising for various applications in the animal feed and biofuel industries 3.2.1.8 endo-1,4-beta-xylanase industry high production yields of the modular xylanase Xyl30 by solid-state fermentation and its biochemical features make it a good candidate for use in industrial applications 3.2.1.8 endo-1,4-beta-xylanase industry is thermostable in alkaline buffer favoring its suitability to bio-bleaching of kraft pulp. Xylanases that are more active in pH range of 6.0-10.0 can act as promising agents in paper and pulp industry. Productivity profiles of xylanase in Escherichia coli recombinant are more than 4fold of that produced from Trichoderma reesei RUTC-30, 5fold of that produced by the donor and significantly higher than the values reported on other Escherichia coli, and Saccharomyces cerevisiae recombinants 3.2.1.8 endo-1,4-beta-xylanase industry oligoglycosides have excellent properties as both surfactants and biodegradability enhancers, whereby Xyn1 is probably useful for such synthesis, since Xyn1 has high transglycosylation activity 3.2.1.8 endo-1,4-beta-xylanase industry possible employment in some industrial processes, which require activity in acid pH, wide-ranging pH stability, and absence of cellulase activity 3.2.1.8 endo-1,4-beta-xylanase industry purified recombinant Xyn10A is a useful candidate for producing xylooligosaccharides as thickeners, fat substitutes, and antifreeze food additives in the food industry 3.2.1.8 endo-1,4-beta-xylanase industry the broad temperature profile of the enzyme makes it a potential candidate for its use in the pulp and paper industry 3.2.1.8 endo-1,4-beta-xylanase industry the MS514-Xyn11 enzyme can be useful as an additive to mixtures designed to hydrolyze biomass as well as in applications for which it is desirable to maintain cellulose structure 3.2.1.8 endo-1,4-beta-xylanase industry the suitable temperature range for industrial application of xylanase from Alternaria mali ND-16 is 50-55°C 3.2.1.8 endo-1,4-beta-xylanase industry Thermomyces lanuginosus SSBP has potential applications due to its high productivity of xylanase and its efficiency in pulp bleaching 3.2.1.8 endo-1,4-beta-xylanase industry variants with improved thermal and alkaline stability are ideal candidates for DNA shuffling experiments to produce a robust xylanase for industrial application 3.2.1.8 endo-1,4-beta-xylanase industry xylanase has potential in bleach boosting and reducing the consumption elemental chlorine-free bleaching sequence. Effects produced are dependent on the enzyme and pulp type used. No correlation between the xylanase-induced brightness gains and possible savings of chlorine dioxide. Use of xylanases for pulp bleaching can boost pulp brightness or alternatively decrease the amounts of bleaching chemicals consumed, which in turn may result in respective reductions of the absorbable organic halogens and chloride levels of the bleach wastewaters and alleviate the environmental impact of the industry 3.2.1.8 endo-1,4-beta-xylanase industry Xyn10 can be an important candidate for protease-resistant mechanistic research and has potential applications in the food industry, cotton scouring, and improving animal nutrition 3.2.1.8 endo-1,4-beta-xylanase industry XynAS27 may be a compelling tool for the food industry because it generates xylobiose (85% w/w) as the main product of xylan hydrolysis 3.2.1.8 endo-1,4-beta-xylanase industry XynBS27 has several advantageous properties such as high specific activity, good activity over broad pH range, excellent pH stability, and being suitable for xylobiose production. These significant characteristics suggest that XynBS27 may be a good candidate in industrial application 3.2.1.8 endo-1,4-beta-xylanase industry the enzyme is a potentially strong candidate for industrial and commercial application in pulp bleaching 3.2.1.8 endo-1,4-beta-xylanase industry the xylanase from Bacillus sp. JB 99 is highly compatible for paper and pulp industry 3.2.1.8 endo-1,4-beta-xylanase industry xylanase is an important industrial enzyme used in the pulp and paper industry 3.2.1.8 endo-1,4-beta-xylanase industry XYN10G5 a good candidate for application in the animal feed industry 3.2.1.8 endo-1,4-beta-xylanase industry the enzyme is a promising candidate for industrial lignocellulosic biomass conversion. Generation of soluble oligosaccharides from lignocellulose is a critical step in bioethanol production. The enzyme produces cello-oligosaccharides and xylo-oligosaccharides from the continuous enzymatic saccharification of sodium carboxymethyl cellulose and xylan, respectively 3.2.1.8 endo-1,4-beta-xylanase industry the fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus has great potential in generating fermentable sugars from renewable agro-residues for biofuel and fine chemical industry. Application of the fusion enzyme (EG-M-Xyn)in combination with Ctec2 (commercial enzyme) in the saccharification leads to a 10-20% net increase in fermentable sugars liberated from pretreated rice straw in comparison to the Ctec2 alone 3.2.1.11 dextranase food industry the use of the dextranase enzyme is the most efficient method for hydrolyzing the dextrans at sugar mills 3.2.1.11 dextranase food industry alpha-dextranase removes dextran by 46.6% in mixed sugarcane juice and 14.1% in clarified sugarcane juice 3.2.1.11 dextranase food industry the enzyme is used for dextran elimination in sugar production process 3.2.1.14 chitinase industry the enzyme is used for degradation of chitin-rich waste materials 3.2.1.15 endo-polygalacturonase food industry agro-industrial wastes are suitable for polygalacturonase production 3.2.1.15 endo-polygalacturonase food industry high pressure processing can be used for selective inactivation of PG in tomato processing while keeping pectinmethylesterase intact 3.2.1.15 endo-polygalacturonase food industry properties of the enzyme may be highly beneficial during fruit processing 3.2.1.15 endo-polygalacturonase food industry the enzyme has a considerable potential for commercial application, primarily in the food and animal feedstock industries, due to features such as its optimum activity in acid medium, which remains at a high level at neutral pH, and good pH and temperature stability. The utilization of orange waste in PG production leads to an increase in yield with a reduction in process cost. Moreover, it adds value to the waste from the orange juice industry 3.2.1.15 endo-polygalacturonase food industry the polygalacturonase has a remarkable heat-tolerance, which makes it very attractive for industrial applications 3.2.1.15 endo-polygalacturonase food industry to preserve or improve rheological properties of tomato based products, the combination of 40°C and 400MPa represents an optimal condition to reduce tomato PG activity while maintaining sufficient pectinmethylesterase activity 3.2.1.15 endo-polygalacturonase food industry endo-PG I showed higher efficiency in juice clarification than the pectin lyase alone or the commercial pectinase widely used. Addition of endo-PG I at 3.4 U/ml reduces the intrinsic viscosity of apple juice by 4.5%, and increases the light transmittance by 71.8%. Endo-PG I is an interesting biocatalyst for juice clarification 3.2.1.15 endo-polygalacturonase food industry polygalacturonases are pectin substances degrading enzymes, that are widely used in juice and fruit beverages for quality improvement 3.2.1.15 endo-polygalacturonase food industry the enzyme improves the elimination of coffee mucilage 3.2.1.15 endo-polygalacturonase food industry the enzyme is used for guava juice extraction and clarification. The recovery of juice of enzymatically treated pulp increases from 6% to 23%. Addition of purified enzyme increases the%T650 from 2.5 to 20.4 and °Brix from 1.9 to 4.8. The pH of the enzyme treated juice decreases from 4.5 to 3.02 3.2.1.15 endo-polygalacturonase food industry the enzyme reduces the viscosity of papaya juice by 17.6% and increases its transmittance by 59.1%. Its favourable enzymatic properties make the enzyme attractive for potential applications in the juice industry 3.2.1.15 endo-polygalacturonase food industry the enzyme is able to enhance the clarification of citrus juice 3.2.1.15 endo-polygalacturonase food industry the enzyme is used for grape juice clarification 3.2.1.15 endo-polygalacturonase food industry the enzyme is used for juice clarification of pear, banana and citrus 3.2.1.15 endo-polygalacturonase food industry the enzyme significantly reduces the viscosities and improves the yields of fruit juices from banana, plantain, papaya, pitaya and mango 3.2.1.15 endo-polygalacturonase food industry the enzyme significantly reduces the viscosity and increases the light transmittance of papaya pulp, and increases the recovery of the papaya extraction 3.2.1.15 endo-polygalacturonase industry thermostable nature of the polygalacturonase with a high pH range for activity makes it an industrially important enzyme 3.2.1.15 endo-polygalacturonase industry the enzyme is developed a feasible strategy to achieve a rapid benign of the bioscouring process with the wettability properties of cotton fabrics 3.2.1.17 lysozyme food industry the LD50 value of lysozyme is 4530 mg/kg body weight. 90 days of marine low-temperature lysozyme treatment at three doses shows no significant difference on blood biochemistry and organ index in drug treatment groups compared to saline treatment group. Marine low-temperature lysozyme can be safely used at the dose of experiment applied in food industry and further clinical studies 3.2.1.17 lysozyme food industry dry-heated hen egg white lysozyme simultaneously exhibits enhanced foaming properties and aggregation capacity. It may self-associate at the air/water interface, stabilizing air bubbles 3.2.1.17 lysozyme food industry due to increasing demands for natural food preservatives, lysozyme is increasingly important in food processing 3.2.1.17 lysozyme food industry possible use of lysozyme as an anti-microbial agent during the winemaking process, the enzyme is covalently immobilized on two different micro-size magnetic particles, the tosyl-activated particles are more stable, overview. The insoluble lysozyme provides advantages over the soluble form, such as enabling reutilization of enzyme and an increase in stability, immobilization may impart stable antimicrobial capability to the surface of food packaging polymers and create a more suitable microenvironment for the enzyme. Treated food can be claimed additive-free following removal of immobilized lysozyme 3.2.1.17 lysozyme food industry potential for the use of immobilized lysozyme as an antimicrobial component for antimicrobial packaging 3.2.1.17 lysozyme food industry the enzyme is used as antimicrobial substance or indicator in fish, meat, dairy, fruits, vegetables and wines or serving as the active component integrated into food packaging systems as well as other active functions in the food matrix 3.2.1.17 lysozyme industry immobilization of lysozyme to the surface of stainless steel as a new strategy to protect the surface against the growth of biofilms 3.2.1.21 beta-glucosidase food industry beta-glucosidases play an important role in the flavor formation of fruits, wine and sweet potato by the production of monoterpene alcohols such as linalool, alpha-terpeneol, citronellol, nerol, and geranol, supplementation with beta-glucosidases from external sources may enhance aroma release thus benefiting the winemaking process 3.2.1.21 beta-glucosidase food industry the enzyme is used for fermentation of Sicilian table olives 3.2.1.21 beta-glucosidase industry application in simultaneous saccharification and fermentation, evaluation of the suitability of plant glycosyl hydrolases in lignocellulose conversion 3.2.1.21 beta-glucosidase industry beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass 3.2.1.21 beta-glucosidase industry the enzyme is widely used in cellulose hydrolysis and the biological conversion and transformation of flavonoids and saponins. The properties of the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde, including thermal stability, pH stability, reusability, and tolerance of glucose, are greatly improved compared with free Tpebgl3. The coordinating metal cation Zn2+ enables the immobilized enzyme to exhibit higher catalytic efficiency. The addition of Zn2+ can greatly advance the reusability, thermostability, and glucose tolerance of immobilized enzyme, which is beneficial for industrial applications 3.2.1.21 beta-glucosidase industry potentially an important industrial enzyme due to the broad specificity, catalytic efficiency and thermostability 3.2.1.23 beta-galactosidase food industry enzyme immobilization onto Amberlite MB-150 beads greatly stabilizes the enzyme preparation, with no loss of activity for 12 months at room temperature. Immobilized enzyme hydrolyzes 64.5% and 69.2% of lactose present in milk and milk whey, respectively, within 10 h at room temperature. Enzyme has a reusability of 10 batchwise uses, with almost no loss in activity 3.2.1.23 beta-galactosidase food industry immobilization of recombinant enzyme onto chitosan and use for hydrolyzation of lactose in milk in a packed bed reactor. Immobilized beta-galactosidase is stable at 4°C for six weeks, shows greater relative activity in presence of Ca2+, and hydrolyzes more than 80% of lactose in milk after 2 h of operation in the reactor 3.2.1.23 beta-galactosidase food industry the enzyme is used for hydrolysis of lactose extracted from whey or milk 3.2.1.23 beta-galactosidase food industry the recombinant thermostable beta-galactosidase may be suitable for the hydrolysis of lactose in milk processing 3.2.1.23 beta-galactosidase industry beta-galactosidases are important industrial enzymes used for the hydrolysis of lactose from milk and milk whey, preparation of the improved mutant strain H26-10-7, overview 3.2.1.23 beta-galactosidase industry the beta-galactosidase from Kluyveromyces lactis is a protein of outstanding biotechnological interest in the food industry and milk whey reutilization, optimization of extraction and downstream processing of the intracellular enzyme for reduction of costs in industrial production by genetic modification, overview 3.2.1.23 beta-galactosidase industry assimilation of lactose as a by-product of dairy industry 3.2.1.23 beta-galactosidase industry potentially an important industrial enzyme due to the broad specificity, catalytic efficiency and thermostability 3.2.1.26 beta-fructofuranosidase food industry producing short-chain fructooligosaccarides as functional food ingredients 3.2.1.26 beta-fructofuranosidase food industry production of invert sugar 3.2.1.26 beta-fructofuranosidase food industry invertase 2 has potential to be applied in food industry since its product, inverted sugar, is used in candies and syrup production, while fructooligosacharides are prebiotics, low calorie and noncariogenic sweeteners 3.2.1.26 beta-fructofuranosidase food industry production of invert sugars and prebiotic compounds 3.2.1.B26 Sulfolobus solfataricus beta-glycosidase food industry the enzyme suitable for hydrolysis of lactose at temperatures at 70-80°C 3.2.1.B26 Sulfolobus solfataricus beta-glycosidase food industry the immobilized enzyme is useful for the hydrolysis of lactose in whey or milk by using a packed-bed enzyme reactor operated at 70°C 3.2.1.26 beta-fructofuranosidase industry the expression of INVA and INVB from Zymomonas mobilis in Pichia pastoris yields new catalysts with improved catalytic properties, making them suitable candidates for a number of industrial applications 3.2.1.B28 Pyrococcus furiosus beta-glycosidase food industry the hyperthermostable beta-glycosidase may be useful for food and pharmaceutical applications 3.2.1.B28 Pyrococcus furiosus beta-glycosidase food industry the enzyme suitable for hydrolysis of lactose at temperatures at 70-80°C 3.2.1.B28 Pyrococcus furiosus beta-glycosidase food industry the immobilized enzyme is useful for the hydrolysis of lactose in whey or milk by using a packed-bed enzyme reactor operated at 70°C 3.2.1.B33 Sulfolobus shibatae beta-glycosidase food industry processing of lactose-containing products 3.2.1.37 xylan 1,4-beta-xylosidase food industry the pretreatment of rice straw with ammonia followed by beta-xylosidase hydrolysis by Weisella cibaria FB069 seems to be a promising method for xylooligosaccharide (prebiotic) production from rice straw 3.2.1.37 xylan 1,4-beta-xylosidase industry the relatively broad pH profile is favourable for industrial application as it offers potential flexibility in terms of process pH and is in line with the current pH range of lignocellulose enzymatic hydrolysis processes for bioethanol production 3.2.1.38 beta-D-fucosidase industry potentially an important industrial enzyme due to the broad specificity, catalytic efficiency and thermostability 3.2.1.39 glucan endo-1,3-beta-D-glucosidase food industry BglS27 is a good candidate for utilization in biotechnological applications such as plant protection, feed, and food preservation 3.2.1.39 glucan endo-1,3-beta-D-glucosidase food industry enzyme is able to hydrolyze both polymers, the beta-1,3-glucan from wine-related lactic acid bacterium Pediococcus parvus and that from yeast cell walls, which can make wine filtration difficult or impossible. Enzyme is still active under wine-relevant parameters such as elevated ethanol, sulfite, and phenol concentrations as well as at low pH values. Enzyme seems to be a useful tool to prevent slime production and undesirable yeast growth during vinification 3.2.1.40 alpha-L-rhamnosidase food industry alpha-L-rhamnosidase is an important enzyme with applications in the food industries because it can release terminal L-rhamnose residues from various natural products. The D594Q and G827K/D594Q mutant enzymes are more suitable for the industrial processes of isoquercitrin preparation than the wild-type enzyme 3.2.1.40 alpha-L-rhamnosidase food industry Aspergillus terreus alpha-L-rhamnosidase specifically hydrolyses the glycosidic linkage of dulcoside A (the bitterest compounds in steviol glycoside mixtures), and converts it to rubusoside. During a 12 h biotransformation, the dulcoside A from crude leaf extracts is completely converted by recombinant alpha-L-rhamnosidase from Aspergillus terreus into rubusoside. This process offers a promising approach for reducing the bitterness of steviol glycoside mixtures 3.2.1.40 alpha-L-rhamnosidase food industry efficient and cost-effective enzymatic production method for preparation of the high-valued natural sweetener trilobatin is developed by the combination of hydrogenation and enzymatic hydrolysis reactions with alpha-L-rhamnosidase as the catalyst in aqueous medium. This technology is adopting the cheap and largely available citrus flavanone naringin as the starting material for trilobatin synthesis, and the present enzymatic technology is possibly utilised by commercial for scale-up production. The production is a straightforward two-step process, in which naringin is hydrogenated into naringin dihydrochalcone and followed by removal of the rhamnosyl group of naringin dihydrochalcone by enzymatic hydrolysis using immobilised alpha-L-rhamnosidase as the catalyst. Under optimised conditions, an overall yield of 96% is achieved with a very low loading of alpha-L-rhamnosidase catalyst at 60 °C in a neutral aqueous buffer solution within 2 h. The immobilised alpha-L-rhamnosidase catalyst can be recycled for 10 reactions (90% yield retained) 3.2.1.40 alpha-L-rhamnosidase food industry the characteristics (good thermostability, wide range of pH-stability with the optimum pH of 5.0 and temperature of 60°C, not greatly affected by representative metal ions, excellent tolerance abilities against glucose and ethanol) of the enzyme suggest that it should be considered a potential new biocatalyst for food and drug industrial applications 3.2.1.40 alpha-L-rhamnosidase food industry the enzyme can efficiently remove naringin from pomelo juice without changing its aroma. It is desirable for debittering citrus juice thereby improving the quality of juice 3.2.1.40 alpha-L-rhamnosidase food industry the enzyme can remove the bitter taste of naringin from citrus juices. Improvement of thermostabilty can promote the practical value of the enzyme in citrus juice processing 3.2.1.40 alpha-L-rhamnosidase food industry the enzyme exhibits transglycosylating activity, which can synthesise rhamnosyl mannitol through the reactions of transglycosylation with inexpensive rhamnose as the glycosyl donor. The enzyme has potential value for glycoside synthesis in the food industry 3.2.1.40 alpha-L-rhamnosidase food industry the enzyme is used to enhance wine aromas or to debitter citrus juices by releasing L-rhamnose 3.2.1.40 alpha-L-rhamnosidase food industry the purified enzyme has potential for enhancement of wine aroma 3.2.1.40 alpha-L-rhamnosidase food industry with the enhanced thermostability, the mutant enzyme, K406R/K573R, has potentially broadened the applications of alpha-L-rhamnosidase in food processing industry 3.2.1.40 alpha-L-rhamnosidase industry stable alpha-L-rhamnosidase with cleaving terminal alpha-L-rhamnose activity has great potential in industrial application. Enhancing the thermostability of alpha-L-rhamnosidase from Aspergillus terreus makes it a good candidate for industrial processes of isoquercitrin preparation 3.2.1.40 alpha-L-rhamnosidase industry the enzyme is a promising alternative biocatalyst for industrial applications due to good pH stability, relatively high thermostability and tolerance to low concentration of alcohols 3.2.1.41 pullulanase food industry debranching of guar galactomannan by pullulanase as an alternative and inexpensive route to produce modified guar galactomannan with enhanced functional properties 3.2.1.41 pullulanase food industry maltotriose syrup preparation from pullulan using pullulanase, overview. In a batch system, pullulanase hydrolyzes 94.25% of purified pullulan and the resultant syrup contains 3.8 mg/ml of maltotriose 3.2.1.41 pullulanase food industry break down of starch for the production of high-glucose syrup. The L627R mutant enzyme may be suitable for industrial application because its shortened reaction time translates to reduced energy consumption 3.2.1.41 pullulanase food industry the enzyme can be used directly for maize starch saccharification without adjusting the pH, which reduces cost and improves efficiency 3.2.1.41 pullulanase food industry useful in starch industries. The addition of the enzyme in gelatinized rice and maize starches significantly increases the resistant starch type 3 yields (RS3). RS3 is of great importance for nutritionists and food industry, due to its reduced levels of plasma glucose and insulin, increased faecal bulk, and short-chain fatty acid production through fermentation in the large intestine 3.2.1.41 pullulanase industry in starch processing industry for the production of sugar syrups, a very effective medium for remarkably improved pullulanase production is designed, a new mutant Bacillus cereus FDTA 13/NTG04-B4 with 2fold increase in pullulanase activity 3.2.1.41 pullulanase industry in the starch processing industry for the production of sugar syrups 3.2.1.41 pullulanase industry resistant starch in food is beneficial for human health, a commercial preparation of pullulanase is used to debranch amylopectin of sago starch at subgelatinization temperature and to evaluate the formation of resistant starch 3.2.1.41 pullulanase industry the acidic thermoactive amylopullulanase-MalE fusion protein and the hydrolytic domain of the amylopullulanase can be employed for industrial saccharification of starch 3.2.1.41 pullulanase industry the enzyme can be employed for industrial saccharification of starch 3.2.1.41 pullulanase industry truncation construct with parallel N- and C-terminal truncations facilitate purification and analysis. Thus the truncation construct may be superior for industrial applications over the full-length pullulanase 3.2.1.51 alpha-L-fucosidase food industry the enzyme catalyse the transglycosylation reaction leading to production of fucosylated human milk oligosaccharides 3.2.1.52 beta-N-acetylhexosaminidase food industry silencing of alpha-mannosidase and beta-D-N-acetylhexosaminidase enhances fruit shelf life due to the reduced degradation of N-glycoproteins which result in delayed softening 3.2.1.54 cyclomaltodextrinase food industry the extremely thermostable enzyme might be of potential value in the production of isomaltooligosaccharides in the food industry 3.2.1.55 non-reducing end alpha-L-arabinofuranosidase food industry clarification of fruit juices for wine industry 3.2.1.55 non-reducing end alpha-L-arabinofuranosidase industry alpha-L-arabinanases are essential glycosyl hydrolases participating in the complete hydrolysis of hemicellulose, a natural resource for various industrial processes, such as bioethanol or pharmaceuticals production 3.2.1.58 glucan 1,3-beta-glucosidase food industry use of enzyme as antifungal agent against green and blue mold diseases, in citrus fruits. All tested isolates of Penicillium digitatum and Penicillium italicum are susceptible to panomycocin in vitro. Effective panomycocin concentrations for 50% growth inhibition for Penicillium digitatum and Penicillium italicum are 2 and 1 microg/ml, respectively. In tests on fruit, panomycocin at concentrations equal to the concentration required for complete inhibition in vitro protects lemon fruit from decay 3.2.1.58 glucan 1,3-beta-glucosidase food industry Exg2 is active under typical wine-related conditions, such as low pH (3.5–4.0), high sugar concentrations (up to 20% w/v), high ethanol concentrations (10–15% v/v), presence of sulfites (up to 2 mM) and various cations and may have multiple uses in wine making 3.2.1.60 glucan 1,4-alpha-maltotetraohydrolase food industry utilization of a maltotetraose-producing amylase as a whole wheat bread improver of the baking performance of whole-grain wheat flour, overview. Whole-grain bread dough prepared with the enzyme shows reduced water absorption and increased development time, while the dough stability is not affected. Also, the enzyme-treated samples exhibit lower Mixolab torque values than the control upon heating and cooling. The viscous characteristics of whole-grain bread dough become dominant with increasing levels of the enzyme. The enzyme delays the crumb firming of whole-grain wheat bread during a 7-d storage period and can function as an antiretrogradation agent to enhance the quality attributes of whole-grain wheat bread 3.2.1.65 levanase food industry the enzyme is used for enzymatic analysis of levan produced by lactic acid bacteria in fermented doughs 3.2.1.67 galacturonan 1,4-alpha-galacturonidase food industry properties of PGI may be suitable for food processing 3.2.1.67 galacturonan 1,4-alpha-galacturonidase food industry polygalacturonases are widely used in the food industry for juice extraction and clarification 3.2.1.67 galacturonan 1,4-alpha-galacturonidase food industry exo-polygalacturonase has a wide range of applications in food processing, i.e. juice extraction, clarification of wine, bakery and distillery industries 3.2.1.67 galacturonan 1,4-alpha-galacturonidase food industry the enzyme is used for guava juice extraction and clarification. The recovery of juice of enzymatically treated pulp increases from 6% to 23%. Addition of purified enzyme increases the%T650 from 2.5 to 20.4 and °Brix from 1.9 to 4.8. The pH of the enzyme treated juice decreases from 4.5 to 3.02 3.2.1.67 galacturonan 1,4-alpha-galacturonidase food industry the enzyme is applied in the juice clarification of tangerine, orange, grapefruit, and apple 3.2.1.67 galacturonan 1,4-alpha-galacturonidase food industry the enzyme is suitable for clarification of orange juice 3.2.1.67 galacturonan 1,4-alpha-galacturonidase food industry the enzyme may be used for clarification of different fruit juices 3.2.1.68 isoamylase food industry saccharification potential of isoamylases is employed in food industry for preparation of high glucose syrup, maltose, maltitol, trehalose, cyclodextrin and resistant starch from starch 3.2.1.73 licheninase food industry the enzyme is a good candidate in the malting and brewing industry reducing the filtration time and viscosity of mash from barley grains, overview 3.2.1.73 licheninase food industry the enzyme is considered as a candidate for application particularly in the animal feed industry 3.2.1.73 licheninase food industry the secretively produced beta-1,3-1,4-glucanase shows excellent thermostability up to 80°C and a wide pH range from pH 4 to pH 11 and has a potential in the food and animal feed applications 3.2.1.73 licheninase food industry the thermostable enzyme can be useful in mashing at 72°C of brewing processes 3.2.1.73 licheninase food industry enzyme can promote mashing with a reduced filtration time (14.0%) and viscosity (3.4%) 3.2.1.73 licheninase food industry exogenous 1,3-1,4-beta-glucanases but not 1,4-beta-glucanases (EC 3.2.1.4) are obligatory enzymes to improve the nutritive value of barley-based diets for broilers. Enzyme is completely resistant to proteolytic inactivation after a 30 min incubation with pancreatic proteases 3.2.1.73 licheninase food industry the addition of mutant K20S/N31c/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P in congress mashing decreases the filtration time and viscosity by 21.3 and 9.6 %, respectively 3.2.1.73 licheninase food industry the enzyme is used for production and processing of alcoholic beverages 3.2.1.73 licheninase food industry the enzyme is used for production of oligomers as prebiotics 3.2.1.73 licheninase industry properties make the enzyme highly suitable for industrial applications 3.2.1.78 mannan endo-1,4-beta-mannosidase food industry the enzyme is involved in the degradation of plant cell wall, resulting in an increase in feed conversion efficiency of animal feed and improvement in the growth performance of broilers. The enzyme can also be used for hydrolyzing galactomannans present in coffee extract to inhibit gel formation during freezed-drying of the instant coffee 3.2.1.78 mannan endo-1,4-beta-mannosidase food industry the enzyme is used for clarification of fruit juices such as grape, peach, orange and pomegranate juices 3.2.1.78 mannan endo-1,4-beta-mannosidase food industry the purified enzyme can be used in clarifying kiwi juice 3.2.1.78 mannan endo-1,4-beta-mannosidase food industry the purified enzyme is used to clarify some fruit juices like orange, grape fruit and apple juices 3.2.1.78 mannan endo-1,4-beta-mannosidase industry when used to treat softwood pulp, enzyme hydrolyzes mainly glucomannan and exhibits a positive effect as a prebleaching agent 3.2.1.78 mannan endo-1,4-beta-mannosidase industry the enzyme is highly useful in the food/feed, paper and pulp, and detergent industries 3.2.1.80 fructan beta-fructosidase food industry a typical solution product consists of a mixture of fructose (155 g/l), glucose (155 g/l), sucrose (132 g/l) and fructooligosaccharides (50 g/l). The concentrations are suitable for applications in most food industries, in products such as sweets, candies, chocolates and yogurts. Besides, the prebiotic function of fructooligosaccharides as stimulants of the beneficial intestinal flora will give the product a functional and differentiated feature 3.2.1.80 fructan beta-fructosidase food industry diabetics 3.2.1.80 fructan beta-fructosidase food industry production of fuel ethanol and ultra-high fructose syrup 3.2.1.81 beta-agarase industry use of enzyme as a cosmetic additive. The oligosaccharides produced by the enzyme have a whitening effect and inhibit tyrosinase activity in the murine melanoma cell line, B16F10. They are not cytotoxic to B16F10 or normal cells 3.2.1.81 beta-agarase industry approaches for the preparation of a series of neoagaro-oligosaccharides by beta-agarase digestion. This system may be applicable in the production of oligosaccharides by beta-agarase digestion from natural sources such as algae 3.2.1.81 beta-agarase industry creation of a thermostable mutant L122Q/N446I of beta-agarase AgaB by directed evolution. The higher thermostability of mutant L122Q/N446I, in conjunction with its high specific activity and product specificity, will allow this enzyme to have potentials in industrial applications 3.2.1.81 beta-agarase industry strain HZ105 may be useful to produce stable agarases 3.2.1.82 exo-poly-alpha-digalacturonosidase food industry properties of PGI may be suitable for food processing 3.2.1.91 cellulose 1,4-beta-cellobiosidase (non-reducing end) industry development of efficient degradation of cellulosic biomass using cellulolytic enzymes, e.g. Ex-4, of white rot fungi 3.2.1.96 mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase food industry the enzyme can be used in dairy industry to efficiently release N-glycans from milk proteins 3.2.1.98 glucan 1,4-alpha-maltohexaosidase food industry production of maltohexaose with low sweetness, low viscosity, and high efficiency for the uptake of energy by humans 3.2.1.98 glucan 1,4-alpha-maltohexaosidase food industry the enzyme can be applied to manufacture high maltose syrup 3.2.1.98 glucan 1,4-alpha-maltohexaosidase food industry the enzyme preparation is effective in removing starch based stains 3.2.1.98 glucan 1,4-alpha-maltohexaosidase industry high compatibility and performance of engineered alpha-amylase AmyUS100DIG/M197A, suggesting its potential application in detergent industry 3.2.1.98 glucan 1,4-alpha-maltohexaosidase industry applications in starch processing technologies because of its highly specific activity, halotolerance, unique substrate specificity, and end product pattern 3.2.1.99 arabinan endo-1,5-alpha-L-arabinanase industry endo-1,5-alpha-L-arabinanases belonging to glycoside hydrolase family 43 are of great industrial interest for use in food technology, organic synthesis and biofuel production owing to their ability to catalyze the hydrolysis of alpha-1,5-arabinofuranosidic bonds in arabinose-containing polysaccharides 3.2.1.108 lactase food industry the enzyme is used for the production of dairy products 3.2.1.116 glucan 1,4-alpha-maltotriohydrolase food industry formation of type III resistant starch is affected by branch chain lengths, especially medium-length chains (DP 30-130), and it can be improved when hydrolysis by glucan 1,4 alpha-maltotriohydrolase precedes debranching. Type III resistant starch (RS3) is of particular interest as a food ingredient, because of its nutritional functionality and thermal stability in most normal cooking operations 3.2.1.116 glucan 1,4-alpha-maltotriohydrolase food industry the enzyme may be effective in retarding starch retrogradation in baked products 3.2.1.118 prunasin beta-glucosidase food industry beta-glucosidase as a tool in marker-assisted selection against bitter almonds 3.2.1.131 xylan alpha-1,2-glucuronosidase food industry xylooligosaccharide derived from enzymatic hydrolysis of biopolymers is of considerable importance in preparing nutritional health oligosaccharides useful in food and pharmaceutical industries. To create added value products from hardwood xylan, xylanase (XynB) and alpha-glucuronidase (AguA) from Thermotoga maritima are co-produced in Escherichia coli through dual-promoter and bicistronic constructs 3.2.1.132 chitosanase food industry has potential in the production of functional foods 3.2.1.132 chitosanase food industry usage of strain TKU011 on the microbial reclamation of food processing wastes such as shrimp shell wastes for the production of chitosanase 3.2.1.132 chitosanase food industry seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials 3.2.1.132 chitosanase food industry chitosanase from Paenibacillus mucilaginosus TKU032 may have potential applications in production of bioactive chitosan oligosaccharides for the food and pharmaceutical industries 3.2.1.132 chitosanase food industry partially acetylated chitosan oligosaccharides have various potential applications in agriculture, biomedicine, and pharmaceutics due to their suitable bioactivities. A more promising approach is enzymatic depolymerization of chitosan using chitinases or chitosanases, as the substrate specificity of the enzyme determines the composition of the oligomeric products 3.2.1.132 chitosanase industry a cheap chitosanase for large-scale chitosan oligosaccharide production in industry 3.2.1.132 chitosanase industry application of chitosanase-overexpression strains 3.2.1.132 chitosanase industry the enzyme has a great potential for industrial applications due to its high yield and broad pH stability 3.2.1.132 chitosanase industry the fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module BgCBM5 from Burkholderia gladioli (CsnA-CBM5) exhibits higher chitosan binding capacity and catalytic activity than wild-type enzyme and improved thermostability. The hybrid enzyme is a useful candidate for industrial application 3.2.1.132 chitosanase industry the high yield of the extracellular overexpression, relevant thermostability, and effective hydrolysis of commercial grade chitosan shows that this recombinant enzyme has a great potential for industrial applications 3.2.1.133 glucan 1,4-alpha-maltohydrolase food industry Novamyl is currently used in the baking industry as an anti-staling agent in breads at neutral or near neutral pH. It is rapidly inactivated during the baking process. Relative to the Novamyl wild-type the variants exhibit more than 10°C increase in thermal stability at pH 4.5, improving the anti-staling effect 3.2.1.133 glucan 1,4-alpha-maltohydrolase food industry impact on crumb texture, and amylopectin recrystallization: reduction of bread firmness increase during storage compared to control or other amylases, bread firmness is slightly increased at day 0, firmness at day 6 is 9.00, 7.15, and 4.40 N (compared to 16.85 N in control) for BStA dosages of 5.05, 10.1, and 20.2 enzyme units/g flour, respectively, though highest dosage leads to sticky dough and low resilience. Enzyme unit = amount of enzyme releasing 1 micromol maltose/minute at 40°C, pH 6.0, 100 mM sodium maleate buffer with 5.0 mM CaCl2. BStA almost completely suppresses amylopectin recrystallization. Hot water extractable dextrin content is increased largely by BStA 3.2.1.133 glucan 1,4-alpha-maltohydrolase food industry wild-type enzyme is not thermostable at low pH as encountered in recipes such as sourdough and rye dough, recombined variants increase thermal stability more than 10°C at pH 4.0-4.5, application test is performed with wheat flour dough at pH 5.5-5.9 and sourdough at pH 4.0-4.3 baked at 230°C for 22 min, firmness and elasticity tested at days 1, 3, and 7 after baking and vacuum packing 3.2.1.133 glucan 1,4-alpha-maltohydrolase food industry the enzyme is used for the production of maltose syrup from starch 3.2.1.133 glucan 1,4-alpha-maltohydrolase food industry the enzyme is used in baking and brewing industry 3.2.1.133 glucan 1,4-alpha-maltohydrolase food industry maltogenic amylases are used to decrease the maltotriose content of high maltose syrups. However, due to the interplay between the hydrolysis and transglycosylation activities of maltogenic amylases, the maltotriose contents of these syrups are still greater than that necessary for pure maltose preparation. Mutant enzyme W177S, shows decreased transglycosylation activity and enhanced maltose production. It will deliver performance superior to that of the wild-type under industrial conditions 3.2.1.133 glucan 1,4-alpha-maltohydrolase food industry potentially applied in bakery industries 3.2.1.133 glucan 1,4-alpha-maltohydrolase food industry the enzyme has many potential applications in food processing 3.2.1.133 glucan 1,4-alpha-maltohydrolase food industry transglucosidase (TGAN) in combination with maltogenic alpha-amylase and beta-amylase appears to be advantageous to modulate sweet potato starch properties. The treatment increases the alpha-1, 6 glycosidic linkage ratio and short chain proportions. Decrease in chain length, molecular weight and long chain proportions is noticed. The initial C-type starch polymorphic structure transforms to B-type structure along with decreased crystallinity. Solubility increases substantially with concomitant decrease in viscosity, gelatinization temperature and melting enthalpy. The outcome is believed to open new pathways for regulating the physicochemical properties of sweet potato starch especially by enzyme modification to the design and development of novel sweet potato starch based products 3.2.1.135 neopullulanase industry potentially valuable enzyme for starch and detergent industries 3.2.1.136 glucuronoarabinoxylan endo-1,4-beta-xylanase food industry endogenous endoxylanase activity during fermentation and storing can have negative effects on dough, the enzyme effect depends on the wheat variety's enzyme content and inhibitor content 3.2.1.141 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase food industry trehalose has many potential applications in biotechnology and the food industry due to its protective effect against environmental stress. Raising trehalose productivity can be achieved through homologous overexpression of maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase. Overexpression of the treY gene and the treY/treZ synthetic operon significantly increases maltooligosyltrehalose synthase activity, the rate-limiting step, and improves the specific productivity and the final titer of trehalose. Furthermore, a strong decrease is noted in glycogen accumulation. Expression of galU/treY and galU/treYZ synthetic operons show a partial recovery in the intracellular glycogen levels and a significant improvement in both intra- and extracellular trehalose content 3.2.1.142 limit dextrinase food industry the prediction of malt fermentability is achieved by both forward step-wise multi-linear regression and the partial least squares multivariate model development methods. Both methods produce similar identifications of the parameters predicting wort fermentability at similar levels of predictive power. Both models are substantially better at predicting fermentability than the traditional use of diastatic power on its own. Limit dextrinase thermostability is not a substantial predictor of fermentability, presumably due to its negative correlation with total limit dextrinase activity. The application of these insights in the malting and brewing industries is expected to result in substantial improvements in brewing consistency and enable more specific quality targets for barley breeder’s progeny selection cut-off limits to be more precisely defined 3.2.1.142 limit dextrinase food industry limit dextrinase activity is of particular importance for the brewing industry as the branched dextrins produced after the action of alpha-amylase on starch are not fermentable and represent a loss of potential ethanol production 3.2.1.142 limit dextrinase food industry limit dextrinase is a unique debranching enzyme involved in starch mobilization of barley grains during malting, and closely related to malt quality 3.2.1.142 limit dextrinase food industry the enzyme is important for malting, influence of kilning on the enzyme activity, process optimization overview 3.2.1.142 limit dextrinase food industry the enzyme is used in brewing and malting, the enzyme is limited for starch degradation due to its thermolability during kilning at 70°C, overview 3.2.1.157 iota-carrageenase industry CgiF is an excellent candidate for industrial applications in production of iota-carrageen oligosaccharides from seaweed polysaccharides 3.2.1.168 hesperidin 6-O-alpha-L-rhamnosyl-beta-D-glucosidase food industry herperidin occurs in lemons and oranges in high concentrations and contributes to juice clouding. Enzymatic hydrolysis via the diglycosidase is useful to remove the unpleasant taste or for juice clarification, a deglycosylation (hydrolysis and transglycosylation) in a single step 3.2.1.168 hesperidin 6-O-alpha-L-rhamnosyl-beta-D-glucosidase food industry potential use of the enzyme for biotechnoligical applications, e.g. in aroma modulation of fermented foods 3.4.11.1 leucyl aminopeptidase food industry application of recombinant leucine aminopeptidase rLap1 from Aspergillus sojae in debittering 3.4.11.5 prolyl aminopeptidase food industry Aspergillus oryzae enzyme PAP together with alkaline protease and leucine aminopeptidase is used to hydrolyze rice protein. The amount of hydrophobic amino acids is significantly increased, which contributes to a reduction in the bitterness 3.4.11.5 prolyl aminopeptidase industry the effectiveness of enzyme in purified form, membrane bound form and in combination with other enzymes to degrade collagen resulting in pharmaceutically significant collagen hydrolysates and in meat tenderization marks its industrial importance 3.4.11.9 Xaa-Pro aminopeptidase food industry PepX aminopeptidase from Streptococcus thermophilus ACA DC 0022 is used in Greek Feta cheese manufacturing 3.4.13.9 Xaa-Pro dipeptidase food industry prolidase can be used in dietary industry as bitterness reducing agent 3.4.13.9 Xaa-Pro dipeptidase food industry prolidases are employed in the cheese-ripening process to improve cheese taste and texture 3.4.14.5 dipeptidyl-peptidase IV food industry use of enzyme for degradation of food-derived opiods from milk, soybean, wheat 3.4.14.11 Xaa-Pro dipeptidyl-peptidase food industry X-prolyl dipeptidyl aminopeptidase PepX, EC 3.4.14.11, and the general aminopeptidase N, EC 3.4.11.2, exhibit a clear synergistic effect in casein hydrolysis studies. Here, the relative degree of hydrolysis is increased by approx. 132% 3.4.14.11 Xaa-Pro dipeptidyl-peptidase food industry activation of the enzyme is observed after processing at 100-200 MPa and 20-30°C. More intense processing conditions lead to enzyme inactivation. Pressures up to 200 MPa result in a structurally molten globule-like state where PepX maintains its secondary structure but the tertiary structure is substantially affected and enzyme activity increased. Both secondary and tertiary structures are affected severely by higher pressures (450 MPa), which reduce enzyme activity 3.4.14.11 Xaa-Pro dipeptidyl-peptidase food industry during casein hydrolysis, the sequential application of PepX or PepN after prehydrolysis with Alcalase results in an relative degree of hydrolysis (rDH) increase of 1.12- or 2.00fold, respectively, compared to only using Alcalase. The simultaneous application of Alcalase, PepX and PepN from the beginning shows similar results as the sequential application, but only three remaining peptides are observed and the hydrolysis time is reduced from 16 h (sequential approach) to 6.5 h (simultaneous approach) 3.4.14.11 Xaa-Pro dipeptidyl-peptidase food industry immobilization of enzyme as cross-linked enzyme aggregate CLEA results in 66% residual activity at 50°C after 4 d (compared to 50% for the free enzyme), and the optimum temperature increases from 30°C for wild-type to 40°C for PepN-CLEAs. With combined CLEAs of PepX/PepN the highest activity yield is about 18% and 9% for PepX and PepN activity, respectively. The combined CLEAs are suitable for application in protein hydrolysis. The relative degree of hydrolysis is increased by approximately 52% compared to an alcalase pre-hydrolyzed casein solution 3.4.14.11 Xaa-Pro dipeptidyl-peptidase food industry production, characterization and use of cross-linked enzyme aggregates (CLEAs) from a fusion protein of PepN and PepX (FUS-PepN_PepX CLEA). The FUS-PepN_PepX CLEAs produced have activity for both specific enzymes. pH and temperature optima, environmental conditions show that the CLEAs are suitable for application in a complex matrix, such as food protein hydrolysates. The relative degree of hydrolysis of a prehydrolyzed casein solution is increased by 100% and the hydrolysate obtained shows a strong antioxidative capacity (ABTS-IC50 value: 7.85 microg/ml) 3.4.15.6 cyanophycinase food industry the production of beta-dipeptides from cyanophycin by cyanophycinase is economically important, because di- and tripeptides are more efficiently utilized than intact proteins or free amino acids, have a greater nutritional value, and are better absorbed 3.4.17.1 carboxypeptidase A food industry Brassica carinata protein hydrolysates could be used for developing functional foods for the treatment of heart and related diseases 3.4.17.1 carboxypeptidase A food industry hydrolyzates could be used for preparing special diets when there is a need to increase the supply of branched amino acids and/or reduce the intake of aromatic amino acids 3.4.17.1 carboxypeptidase A food industry the application of the novel ochratoxin A hydrolytic enzyme to reduce the ochratoxin A contents on some food or feed products is under evaluation 3.4.17.1 carboxypeptidase A food industry application of enzyme to wheat flour contaminated by ochratoxin A leads to 16.8-78.5% reduction of ochratoxin A and production of ochratoxin alpha 3.4.21.1 chymotrypsin industry the enzyme is successfully immobilized on a non-leaching material surface to provide a new material able to inhibit biofilm colonization. The multiple-target nature of the protease activity allows the new material to be used with a broad-spectrum activity against polymicrobial infections, including drug-resistant strains 3.4.21.1 chymotrypsin industry the enzyme possesses potential applications in the food, leather and silk industries where acidic or slightly alkaline conditions are needed 3.4.21.4 trypsin food industry the enzyme can be used as a possible biotechnological tool in the fish processing and food industries 3.4.21.7 plasmin food industry milk retentate with increased plasmin activity is an interesting starting material for cheese-making. Increased plasmin activity increases cheese flavour and decreases ripening time 3.4.21.7 plasmin food industry the enzyme is responsible for spoilage of directly heated ultra-high temperature milk products 3.4.21.25 cucumisin food industry the high milk-clotting ability of religiosin C supports its use in the food industry 3.4.21.25 cucumisin food industry milk-clotting enzyme for cheese-making 3.4.21.26 prolyl oligopeptidase food industry the enzyme can be used during mashing to produce gluten free beer 3.4.21.62 Subtilisin food industry alcalase-hydrolyzed potato protein has both antioxidant and emulsifying properties which may be of potential use in meat emulsion manufacturing 3.4.21.62 Subtilisin industry improving the kinetic, thermal and thermodynamic stability of subtilisin Carlsberg by means of simple, inexpensive but effective covalent coupling to oxidized sucrose polymers of varying sizes as well as polyglutaraldehyde. Stability is comparable to the most stabilized subtilisin variants obtained by site-directed mutagenesis 3.4.21.62 Subtilisin industry subtilisin JB1 may serve as a potential source material for use in industrial applications of proteolytic enzymes and microorganisms for fishery waste degradation and fish by-product processing 3.4.21.62 Subtilisin industry the enzyme shows excellent performance in stain removal from cotton fabric and good compatibility with several commercial laundry detergent formulations, suggesting that it has high potential for use in various industrial applications 3.4.21.63 Oryzin food industry the enzyme is efficient in producing antihypertensive peptide IPP from beta-casein and a potential debittering agent. The high degree of hydrolysis of the enzyme to soybean protein (8.8%) and peanut protein (11.1%) compared to papain and alcalase makes it a good candidate in the processing of oil industry byproducts 3.4.21.63 Oryzin food industry the salt tolerance of proteases secreted by Aspergillus oryzae 3.042 closely relates to the utilization of raw materials and the quality of soy sauce 3.4.21.63 Oryzin industry immobilization of the enzyme as an important biotechnological aspect 3.4.21.63 Oryzin industry optimization of protease production in fermentation medium with optimal salt, nitrogen and carbon concentrations 3.4.21.63 Oryzin industry possible use of the enzyme in detergent industry and peptide synthesis due to its compatibility with several detergents, oxidants and organic solvents 3.4.21.63 Oryzin industry alkaline proteases are a major group of industrial enzymes that hydrolyze proteins into short peptides and amino acids, and catalyze peptide synthesis 3.4.21.63 Oryzin industry peptidases are important enzymes with applications in many industrial sectors, such as the production of cheese, meat, fish, and wine, protein hydrolysates, the pharmaceutical industry, the leather industry, cosmetics, and fine chemicals 3.4.21.75 Furin industry furin may be applied in mass production of a potent antimicrobial peptide histonin as a natural form, whereby overcoming its inherent toxicity and the low yield of production 3.4.21.96 Lactocepin food industry CEP isolated from Mongolian fermented mare's milk strain SBT11087 is distinct from those from previously reported Lactobacillus helveticus strains in terms of its optimal temperature and its degradation of beta-casein 3.4.21.96 Lactocepin industry method to alter lactocepin specificity in commercial starter cultures with a propensity for bitter flavour defect. PrtP derivatives developed by this approach should be suitable for commercial applications in the US and other countries with a favourable regulatory climate 3.4.21.111 aqualysin 1 food industry presence of aqualysin 1 in bread dough has no impact on the specific bread volume and only limited impact on hardness, cohesiveness, springiness, resilience and chewiness, but impacts bread crumb coherence. Aualysin in dough is inhibited by wheat endogenous serine peptidase inhibitors during dough mixing and fermentation and starts hydrolyzing gluten proteins during baking above 80°C 3.4.21.111 aqualysin 1 food industry the level of protein extractable in sodium dodecyl sulfate containing medium under non-reducing conditions from wheat dough decreases upon heating to a lesser extent when aqualysin is used than in control experiments. The higher level is caused by the release by Aq1 of peptides from the repetitive gluten protein domains during baking. The resultant thermoset gluten network in bread crumb is mainly made up by protein from non-repetitive gluten domains 3.4.22.1 cathepsin B food industry the gel strength of modori gel is increased by suppression of cathepsin B activity using CA-074. Cathepsin B may cause modori phenomenon. Therefore, our results suggest that natural cysteine protease inhibitor, such as oryzacystatin derived from rice may apply to surimi-based product processing of horse mackerel to improve the quality of thermal gels 3.4.22.2 papain food industry combination of ultrasound and papain is more beneficial for improving functional properties of meat compared with the individual treatment 3.4.22.2 papain industry papain has many uses and functions in a variety of industries: clarifying beer, meat tenderization, preservation of spices, contact lens cleaners, detergents, pet food palatability, digestive aids, blood stain remover, blood coagulant and cosmetics 3.4.22.2 papain industry the cotton fabric immobilized modified papain has potential applicationsin the functional textiles field 3.4.22.2 papain industry the enzyme with high biological activity and the decomposing ability is widely used in the lines of medical application, cell isolation, food, detergents, leather, textile, cosmetic and pharmaceutical industry 3.4.22.2 papain industry catalytic properties of papain immobilized on hybrid nanoflowers are enhanced compared with that of free papain. The hybrid nanoflowers exhibit excellent reusability, high thermostability, long storage life and great potential in industrial applications 3.4.22.2 papain industry immobilization on multi-walled carbon nanotubes is beneficial to the industrial applications because of its potential to be easily separated from the end product at the end of the reaction, reuse for multiple times and allow the development of multiple enzyme reaction system 3.4.22.2 papain industry papain combined with chitosan-sodium alginate pretreated with the appropriate ultrasound can be effective technique for improving the activity of immobilized enzymes as a result of changes in its structure and intermolecular interactions. It is important to extend the application of chitosan-sodium alginate gel in the immobilized enzyme industry 3.4.22.3 ficain food industry prolonged stability of ficin at low pH values in comparison to papain can be of importance for industrial processes that run in low pH conditions such as chill haze prevention during winemaking which prompted us to check long term stability of ficin and papain at low pH and in the presence of ethanol 3.4.22.3 ficain industry enzyme is used in the food, pharmaceutical, and detergent industries 3.4.22.7 asclepain food industry asclepain f is less adequate as coagulant in cheesemaking 3.4.22.14 actinidain food industry actinidin is used as a beef tenderizer, use of actinidin-tenderized beef significantly improves emulsion stability, texture, and organoleptic properties of the sausage product 3.4.22.14 actinidain food industry actinidin, particularly at level 20 unit/g of skin, can be used to improve the yield and properties of gelatin from bovine skin 3.4.22.14 actinidain food industry the enzyme can be used in meat tenderisation 3.4.22.B29 calpain 9 food industry single nucleotide polymorphisms G7518A and C7542G are associated with carcass weight, evisceration weight, abdominal fat weight, abdominal fat percentage, and breast muscle percentage. The AA(7518)/GG(7542) genotype has the highest intramuscular fat content, highest breast muscle weight, and lower abdominal fat weight and abdominal fat percentage 3.4.22.30 Caricain food industry the enzyme detoxifies gliadin in wheat dough 3.4.22.B31 calpain 11 food industry in muscle 3 h postmortem, the decrease in unautolyzed and total activities of calpain-11, desmin content and shear force are more rapid in CaCl2-incubated samples than in control, NaCl- and EDTA-incubated samples. In the absence of calpain-1, calpain-11 with an extensive activation by adding exogenous Ca2+ could enhance the postmortem proteolysis and tenderization of ostrich muscle 3.4.22.32 Stem bromelain food industry stem bromelain immobilized on chitosan beads without glutaraldehyde yields a food-safe biocatalyst for unstable real wine future application 3.4.22.32 Stem bromelain food industry the immobilized stem bromelain has productive biotechnological applications in wine-making 3.4.22.41 cathepsin F food industry CTSF gene (encoding cathepsin F) is a suitable marker for screening pigs to improve cured weight and yield for country ham production 3.4.22.41 cathepsin F food industry CTSF gene is a suita marker for screening pigs to leimprove meat quality. CTSF gene is associated with estimated breeding values: average daily gain, lean cuts, and backfat thickness 3.4.22.41 cathepsin F food industry CTSF gene is a suitable marker for screening pigs to improve meat quality. CTSF gene is associated with estimated breeding values: average daily gain, lean cuts, and backfat thickness 3.4.22.52 calpain-1 food industry markers developed at the CAST and CAPN1 genes are suitable for use in identifying animals with the genetic potential to produce meat that is more tender 3.4.22.67 zingipain food industry application of enzyme in food industry for cheese-making or meat tenderization. Optimization of purification protocol via three-phase partitioning system 3.4.22.67 zingipain food industry zingipain can hydrolyze the gelatin from fish skin to peptides with low average molecular weights (below 690 Da) more efficiently than that from pig skin, pig bone and bovine skin. All gelatin hydrolysates show higher antioxidative activities than non-hydrolysed gelatins. Fish skin gelatin hydrolysate obtained using ginger protease exhibits the highest degree of hydrolysis (13.08%) and antioxidant activity towards 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical (97.21%) and lipid peroxidation (48.46%) 3.4.23.1 pepsin A food industry treatment with pepsin at pH 4.0 results in lowering the (pseudo)peroxidase activity of metmyoglobin both at physiological pH and at meat pH, leading to strongly enhanced prooxidative effect of mildly proteolyzed metmyoglobin on lipid oxidation 3.4.23.1 pepsin A food industry the porcine pepsin digests of cheese whey at a specific acidic pH have the potential to be used as natural food preservatives due to the presence of the three peptides with antibacterial activity against Bacillus subtilis (lactoferrin f(20-30) and beta-lactoglobulin f(14-22)) and Escherichia coli (beta-lactoglobulin f(82-103)) 3.4.23.2 pepsin B food industry the enzyme's milk-clotting activity is used for cheese making. Mutant enzyme T218S serves as a milk coagulant that contributes to an optimal flavor development in mature cheese 3.4.23.4 chymosin food industry used as milk coagulant in cheese preparation 3.4.23.4 chymosin food industry used for the production of dairy products 3.4.23.4 chymosin food industry coagulant for cheese making 3.4.23.4 chymosin food industry chymosin constitutes a traditional ingredient for enzymatic milk coagulation in cheese making 3.4.23.4 chymosin food industry the enzyme is used as milk coagulant in the cheese industry 3.4.23.4 chymosin food industry the enzyme is used for the production of Reggianito cooked cheese 3.4.23.4 chymosin food industry the enzyme is used industrially in cheese production 3.4.23.4 chymosin food industry the enzyme plays an essential role in the coagulation of milk in the cheese industry 3.4.23.20 Penicillopepsin food industry the enzyme is used in the dairy industry such as in accelerated cheese ripening 3.4.23.21 Rhizopuspepsin food industry the peptidase may function as an important alternative enzyme in milk clotting during the preparation of cheese 3.4.23.25 saccharopepsin food industry important for the nitrogen release during alcoholic fermentation in wine production which is required for subsequent malolactic fermentation by Oenococcus oeni 3.4.23.25 saccharopepsin food industry possibly involved in ripening processes of fermented meat products 3.4.23.25 saccharopepsin food industry the enzyme is detrimental to beer foam stability 3.4.23.25 saccharopepsin food industry the enzyme significantly affects the safety and quality of alcoholic drinks, especially the foam stability of beer 3.4.23.40 Phytepsin food industry cardosins from Cynara scolymus flower extract are suitable for Gouda-type cheese manufacturing. The type of coagulant has no significant effect upon the chemical parameters analyzed and pH values of the cheeses throughout ripening, and no significant differences are detected in the organoleptic properties between cheeses manufactured with Cynara scolymus brining for 40 h or animal rennet 3.4.23.40 Phytepsin food industry gene expression under postharvest chilling treatment in two pineapple varieties differing in their resistance to blackheart development reveals opposite trends. The resistant variety shows an up-regulation of AP1 precursor gene expression whereas the susceptible shows a down-regulation in response to postharvest chilling treatment. The same trend is observed regarding specific aspartic protease enzyme activity in both varieties 3.4.23.40 Phytepsin food industry use of recombinant enzyme for manufacturing sheep, goat, and cow cheeses result in a higher cheese yield for all three types of cheese when compared with synthetic chymosin 3.4.23.49 omptin food industry the peptidase shows maximal milk clotting activity at 60-65 °C and maintenance of enzymatic activity above 80% in the presence of 20 mM CaCl2 3.4.24.26 pseudolysin industry A2 protease is usable for shrimp waste deproteinization in the process of chitin preparation, percent of protein removal after 3 h hydrolysis at 40°C with an enzyme/substrate ratio of 5 U/mg protein is about 75%. A2 proteolytic preparation also demonstrates powerful depilating capabilities of hair removal from bovine skin 3.4.24.26 pseudolysin industry pseudolysin is a biotechnologically important enzyme in the tanning industry 3.4.24.26 pseudolysin industry potential application in the leather industry and as a therapeutic agent 3.4.24.27 thermolysin food industry the enzyme can be used for production of caseicin A, an antimicrobial active peptide, from alpha-casein, for potential improvement of the safety of infant milk formula using milk-derived bioactive peptides 3.4.24.27 thermolysin industry the enzyme is used for synthesis of N-carbobenzyloxy L-Asp-L-Phe methyl ester, a precursor of the artificial sweetener aspartam 3.4.24.28 bacillolysin food industry in the beer brewing process, the neutral protease during mashing process can release more amino acids from wort such as aspartic acid, arginine, methione, and histidine, resulting in a better amino acid profile in wort 3.4.24.28 bacillolysin food industry the enzyme is an effective food additive for improving the quality of gluten-free rice bread. Bacillolysin together with subtilisin and papain increase the specific volume of gluten-free rice breads by 30-60% compared with untreated breads 3.4.24.75 lysostaphin food industry antistaphylococcal agent 3.5.1.1 asparaginase food industry reduction of acrylamide level in biscuits and bread 3.5.1.1 asparaginase food industry the acrylamide contents in baked dough were reduced to sixty percent after treatment with recombinant enzyme as compared to the untreated control 3.5.1.1 asparaginase food industry the enzyme is used for reducing acrylamide formation during the potato frying process 3.5.1.1 asparaginase food industry the enzyme reduces acrylamide content in starchy fried food commodities 3.5.1.1 asparaginase food industry the final level of acrylamide in biscuits and bread is decreased by about 81.6% and 94.2%, respectively, upon treatment with 10 U asnase per mg flour 3.5.1.1 asparaginase food industry addition of partially purified L-asparaginase to potato products followed by incubation of the mixture at 37°C for 30 min leads to 92% reduction of acrylamide content 3.5.1.1 asparaginase food industry approximately 88.5% (0.978 mg/kg) acrylamide can be removed from fried potato chips by mutant V26A/E30G/D181G/V245G/G276D pre-treatment 3.5.1.1 asparaginase food industry pretreatment of potato chips and mooncakes with Asnase significantly decreases their acrylamide by 86% and 52%, respectively 3.5.1.2 glutaminase food industry microbial glutaminases are enzymes with emerging potential in both the food and the pharmaceutical industries, potential application for bioconversion of glutamine to flavor-enhancing glutamic acid 3.5.1.2 glutaminase food industry the enzyme is used in soy sauce fermentation 3.5.1.4 amidase industry the immobilized, cross-linked enzyme aggregate proves useful as a substitute for soluble amidase as a biocatalyst in the pharmaceutical and chemical industries 3.5.1.5 urease food industry the enzyme is applicable to elimination of urea in Chinese rice wine 3.5.1.5 urease food industry use of recombinant acid urease for enzymatic degradation of urea in rice wine. Ethylcarbamate, a carcinogenic compound, is formed from urea and ethanol in rice wine, therefore enzymatic elimination of urea is always attractive 3.5.1.5 urease industry enhancement of stability of immobilised urease by biocompatible polymer-conjugated magnetic beads for industrial application based on removal of urea 3.5.1.11 penicillin amidase industry PAC is used in industrial synthesis of semi-synthetic antibiotics 3.5.1.11 penicillin amidase industry penicillin acylase are industrially important enzymes that break down different penicillins to give 6-amino penicillanic acid, the precursor for synthesis of semi synthetic penicillins and cephalosporins antibiotics 3.5.1.24 choloylglycine hydrolase food industry enzyme inhibitors are promising feed additives to replace antibiotic growth promoters for enhancing the productivity and sustainability of food animals 3.5.1.24 choloylglycine hydrolase food industry inhibitors are a promising alternatives to antibiotic growth promoters for enhanced animal growth performance and food safety, required since antibiotic growth promoter usage is linked to the emergence of antibiotic resistant bacteria. Enzyme BSH inhibitors are promising feed additives to replace antibiotic growth promoters for enhanced host lipid metabolism and growth performance 3.5.1.44 protein-glutamine glutaminase food industry in food industry, protein deamination is regarded as a promising method to improve protein functionality (solubility, emulsion, foam and gelling properties) desired in food systems. The enzyme produced from Chryseobacterium proteolyticum is not toxigenic so that consumer safety is assured. The enzyme can be reproducibly produced and purified into a consistent enzyme product 3.5.1.44 protein-glutamine glutaminase food industry protein-glutaminase is contributes to improving the quality of various dairy products such as yoghurt, cheese, acid milk drinks, etc. Deamidation by protein-glutaminase improves the emulsion capacity of skim milk solution 3.5.1.44 protein-glutamine glutaminase food industry the commercial enzyme is used for enhancing food proteins solubilization. Optimization of coconut protein deamidation using protein-glutaminase and its effect on solubility, emulsification, and foaming properties of the proteins, overview 3.5.1.75 urethanase food industry urethanase is useful to reduce ethyl carbamate, i.e. urethane, in Chinese rice wine, strain CGMCC 5081 culture condition optimization for enzyme production in immobilized cells 3.5.1.75 urethanase food industry with good ethanol tolerance, the crude urethanase is able to reduce ethyl carbamate, i.e. urethane, in Chinese rice wine without the change of flavor substance in wine 3.5.1.75 urethanase food industry crosslinked enzyme aggregates of Providencia rettgeri urease (PRU-CLEAs) have great potential in the elimination of urethane (ethyl carbamate) from Chinese rice wine. Process flow diagram of PRU-CLEAs applied in membrane reactor, overview 3.5.1.81 N-Acyl-D-amino-acid deacylase industry industrial applications of D-amino acids, produced by several different enzymes on different pathways, including the N-acyl-D-amino acid amidohydrolase, are in the pharmaceutical industry for antibiotics production or as medicine, or in food industry for food sweeteners, or in cosmetics in skin protection products 3.5.1.93 glutaryl-7-aminocephalosporanic-acid acylase industry great potential for industrial application of the lysis genes-assisted cell disruption 3.5.1.93 glutaryl-7-aminocephalosporanic-acid acylase industry the huge production of engineered GLA produced in Escherichia coli under optimized conditions makes this enzyme an economic tool to be used in bioconversion processes at the industrial level, e.g., in 7-ACA production 3.5.1.93 glutaryl-7-aminocephalosporanic-acid acylase industry cephalosporin C acylase (CCA), a proton-forming enzyme, is an important industrial enzyme that can directly catalyze the substrate cephalosporin C (CPC) to 7-aminocephalosporanic acid (7-ACA), which is an intermediate in many types of synthetic cephalosporins. Immobilized CCA on porous carriers is applied in industry for the production of 7-ACA because of its high efficiency and environmentally friendly nature compared with the chemical process and two-step enzymatic process involving two enzymes. Mutational improvement of catalytic efficiency and operational stability 3.5.1.117 6-aminohexanoate-oligomer endohydrolase industry the partial enzymatic hydrolysis of nylon surfaces by NylC can be used to change the smoothness of nylon fibers 3.5.2.2 dihydropyrimidinase industry production of optically pure D-amino acids that are key intermediates in the synthesis of commercial products such as beta-lactam semisynthetic antibiotics, peptides, hormones, pyretroids and pesticides 3.5.2.B2 (+)-gamma-lactamase industry the enzyme can be a promising candidate of biocatalyst for industrial applications of highly valuable chiral pharmaceutical chemicals 3.5.3.1 arginase food industry when milk casein is hydrolyzed at 37°C by using commercial digestive enzymes, pancreatin F and protease A, a significant accumulation of L-ornithine in the hydrolysate and the simultaneous disappearance of L-arginine is noted. Transient but distinct arginase activity, which is sufficiently high for L-ornithine production, is detected in the hydrolysate for a certain period during casein hydrolysis. Findings suggest that an inactive precursor of arginase is contaminated in pancreatin F and is proteolytically activated during the incubation 3.5.3.12 agmatine deiminase food industry development of a multiplex PCR method for the simultaneous detection of four genes involved in the production of histamine, i.e. histidine decarboxylase hdc, tyramine, i.e.tyrosine decarboxylase tyrdc, and putrescine, via either ornithine decarboxylase odc, or agmatine deiminase agdi. A collection of 810 lactic acid bacteria strains isolated from wine and cider was screened. The most frequent gene corresponds to the agdi gene detected in 112 strains, 14% of all lactic acid bacteria strains, of 10 different lactic acid bacteria species 3.5.4.2 adenine deaminase food industry in beer samples treated with adenine deaminase and guanine deaminase, the adenine concentration in beer drops 66-67% and guanine concentration in beer drops from 68.8 microM to a minimal amount 3.5.4.3 guanine deaminase food industry in beer samples treated with adenine deaminase and guanine deaminase, the adenine concentration in beer drops 66-67% and guanine concentration in beer drops from 68.8 microM to a minimal amount 3.5.4.6 AMP deaminase food industry noting the use of the enzyme from Aspergillus oryzae in food intended for human consumption and potential presence at trace levels in finished goods, a series of safety studies including an in vitro Ames test and chromosome aberration assay with Chinese hamster lung fibroblasts are conducted along with a 90-day oral toxicity study in rats. AMP deaminase shows no evidence of genotoxicity in the in vitro tests. Following gavage administration of Sprague-Dawley rats at dosages of 19.8, 198.4, or 1984 mg total organic solids (TOS)/kg body weight (bw)/day for 90 days, no adverse effects on body weight gain, food consumption, hematology, clinical chemistry, urinalysis, ophthalmological and histopathological examinations are observed. The no-observed-adverse-effect level is considered to be 1984 mg TOS/kg bw/day, the highest dose tested. Results of the genotoxicity studies and subchronic rat study support the safe use of AMP deaminase produced from Aspergillus oryzae in food production 3.5.4.6 AMP deaminase food industry production of 5'-IMP as food additives and pharmaceutical intermediate, important enzyme for the food industry 3.5.5.1 nitrilase industry the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation 3.5.5.1 nitrilase industry spore surface display of nitrilases is an effective approach for enzyme immobilization in biochemical engineering on an industrial scale 3.5.5.1 nitrilase industry the high-level production of Arthrobacter aurescens CYC705 nitrilase will meet the need of industrial biosynthesis of iminodiacetic acid 3.5.5.1 nitrilase industry the purified enzyme reveales its selectivity towards dinitriles, which suggests a possible industrial application in the synthesis of cyanocarboxylic acids 3.5.5.7 Aliphatic nitrilase industry the enzyme is engineered for the commercial production of 3-hydroxyvaleric acid 3.5.5.7 Aliphatic nitrilase industry the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation 3.5.5.7 Aliphatic nitrilase industry the enzyme is a potential candidate for industrial applications for biosynthesis of carboxylic acid 3.5.5.7 Aliphatic nitrilase industry the enzyme is a promising biocatalyst for mild nitrile hydrolysis 3.5.5.7 Aliphatic nitrilase industry under optimized conditions, using the fed-batch reaction mode, total of 1050 mM 3-cyanopyridine is hydrolyzed completely in 20.8 h with eight substrate feedings, yielding 129.2 g/l production of nicotinic acid and thus showing a potential for industrial application 3.7.1.1 oxaloacetase food industry oxalate toxicity is a concern for the commercial application of fungi in the food and drug industries 3.7.1.7 beta-diketone hydrolase industry oxidized polyvinyl alcohol hydrolase, OPH, is a key enzyme in the degradation of PVA and might have a great potential for application in textile desizing processes 3.7.1.7 beta-diketone hydrolase industry the improved catalytic efficiency of OPH expressed in recombinant Pichia pastoris makes it favorable for industrial applications 3.8.1.5 haloalkane dehalogenase industry a stable mini protein is successfully designed and may be used as bioreceptors in the haloalkane sensor that is suitable for industrial application 3.12.1.B1 tetrathionate hydrolase industry the enzyme can be employed for optimum enzymatic devulcanisation of rubber tire 4.1.1.2 oxalate decarboxylase industry prevention of scaling in pulp and paper industry, depletion of oxalate from beverage 4.1.1.6 cis-aconitate decarboxylase industry economic production of itaconic acid which is a supplement in many products 4.1.1.12 aspartate 4-decarboxylase industry Asd is a major enzyme used in the industrial production of L-alanine 4.1.1.15 glutamate decarboxylase food industry the specific inhibition of GAD activity or a reduction in the levels of free glutamate may prevent the growth of otherwise resistant GAD+ bacteria in foods where low pH and/or nisin is used as a preservative 4.1.1.15 glutamate decarboxylase food industry Enterococcus avium strain M5 and its gadB gene might be useful when GABA-enriched foods are attempted to be produced, serving as a source of strain and gene 4.1.1.15 glutamate decarboxylase food industry Lactobacillus sakei strain A156 and its gadB gene might be useful when GABA-enriched foods are attempted to be produced, serving as a source of strain and gene 4.1.1.15 glutamate decarboxylase food industry the recombinant Lactobacillus plantarum strain overexpressing the Lactobacillus plantarum enzyme can be used as a starter culture for direct incorporation into a food system during fermentation for production of GABA-rich products 4.1.1.17 ornithine decarboxylase food industry the enzyme is used in the wine making process 4.1.1.25 tyrosine decarboxylase food industry tyrosine decarboxylase is expressed during wine fermentation 4.1.1.101 malolactic enzyme food industry cell surface display of malolactic enzyme on the cell surface of Sacchaormyces cerevisiae to conduct malolactic fermentation in wine. The malolactic activity of the genetically engineered yeast strain can turn 21.11% L-malate into lactic acid after 12 h reaction with L-malate 4.1.1.101 malolactic enzyme food industry expression of malolactic enzyme from Oenococcus oeni in the host strain Lactobacillus plantarum WCFS1. Under conditions with L-malic acid as the only energy source and in presence of Mn2+ and NAD+, the recombinant Lactobacillus plantarum and the wild-type strain convert 85% (2.5 g/l) and 51% (1.5 g/l), respectively, of L-malic acid in 3.5 days. The recombinant Lactobacillus plantarum cells convert in a modified wine 15% (0.4 g/l) of initial L-malic acid concentration in 2 days 4.1.1.101 malolactic enzyme food industry the bacterial mleS gene introduced into yeast Sacchaormyces cereuisiae induces transformation of L-malate in L-lactate. In spite of a high in vitro malolactic specific activity, malate degradation via malolactic enzyme is very low 4.1.2.4 deoxyribose-phosphate aldolase industry ultrathin enzymatically active films are useful for applications in which only small quantities of active material are needed and at the same time quick response and contact times without diffusion limitation are wanted. 2-Deoxy-D-ribose-5-phosphate aldolase can be immobilized in a thin polymer layer at the air-water interface and transferred to a suitable support by the Langmuir-Schaefer technique under full conservation of enzymatic activity. The polymer in use is a poly(N-isopropylacrylamide-co-N-2-thiolactone acrylamide) statistical copolymer in which the thiolactone units serve a multitude of purposes including hydrophobization of the polymer, covalent binding of the enzyme and the support and finally cross-linking of the polymer matrix. The application of this type of polymer keeps the whole approach simple as additional cocomponents such as cross-linkers are avoided 4.1.2.9 phosphoketolase industry the production of D-lactic acid as well as L-lactic acid is of significant importance for the practical application of polylactic acid, which is an important raw material for bioplastics that can be produced from biomass 4.1.2.9 phosphoketolase industry using the Lactobacillus plantarum NCIMB 8826 strain whose L-lactate dehydrogenase gene is deficient and whose phosphoketolase gene is substituted with a heterologous transketolase gene the fermentation of optically pure D-lactic acid from arabinose is achieved 4.1.2.9 phosphoketolase industry industrially important enzyme in the production of L-glutamic acid, mevalonate, isoprenoid precursors and isoprene 4.1.2.13 fructose-bisphosphate aldolase food industry fructose-1,6-bisphosphate aldolase is an immunogenic surface target useful for the detection of Listeria genus. Listeria monocytogenes is a major public health concern and a potential economic burden regarding food industry 4.1.2.47 (S)-hydroxynitrile lyase food industry root-specific expression of cassava HNL not only increases total root protein levels 3fold approaching the target values for a nutritionally balanced meal but accelerates cyanogenesis during food processing resulting in a safer and more nutritious food product 4.1.3.3 N-acetylneuraminate lyase industry the enzyme has potential in the industrial production of N-acetylneuraminic acid 4.1.99.1 tryptophanase food industry expression of enzyme in wine yeast results in a strong increase of passion fruit aroma in wine 4.2.1.2 fumarate hydratase industry use of purified enzyme in L-malic acid production is uneconomical because whole cells are cheaper. Use of one mg of purified fumarase in continuous production of L-malic acids, corresponds to the use of enzyme in 68 g (wet weight) cells of Saccharomyces bayanus or in 120 g (wet weight) cells of baker's yeast 4.2.1.51 prephenate dehydratase industry overexpression of pheAfbr and/or wild-type aroF is helpful for the enhancement of the key enzymes in L-phenylalanine biosynthesis, which is an important prerequisite for improved production of L-phenylalanine with engineered strains 4.2.1.84 nitrile hydratase industry biotransformation of nitrile. Nitrile hydratase from Rhodococcus rhodochrous J1 is used for industrial production of acrylamide and nicotinamide. Production of enzyme by recombinant Escherichia coli is superior to that in R. rhodochrous J1. Genetically engineered Escherichia coli can be used for industrial applications instead of Rhodococcus rhodochrous J1. High-molecular weight nitrile hydratase may be more suitable for industrial application than low-molecular weight nitrile hydratase because of its higher product tolerance, which would lead to a high product concentration 4.2.1.91 arogenate dehydratase industry fine tuning of the feedback sensitivity of ADT may be effective to establish a line that accumulate Phe at a high concentration 4.2.1.92 hydroperoxide dehydratase food industry the enzyme produces aldehydes that are used as flavours in foods and beverages 4.2.1.108 ectoine synthase industry the engineered Escherichia coli strain has potential industrial application since it produces ectoine at high rates and can avoid the complex down streaming process associated with the conventional bioprocess 4.2.2.2 pectate lyase food industry effects of pectate lyase-silencing in tissue integrity increases the content of large particles in juice, its viscoelastic properties being modified and its viscosity increased 4.2.2.2 pectate lyase food industry firmness of full ripen strawberry fruits from Pel lines is significantly higher than control fruits, while color and soluble solids are not affected. The increase of firmness in Pel lines is maintained when ripe fruits are stored for 3 days at 25°C 4.2.2.2 pectate lyase food industry inhibition of the pectate lyase gene improves postharvest behavior of strawberries 4.2.2.2 pectate lyase industry enzyme treatment in fibre degumming validated by weight loss in gampi and paper mulberry fibres 4.2.2.2 pectate lyase industry the thermoactive pectate lyase from strain DKS1 of Bacillus pumilus has a potential use for degumming ramie fiber, the purified pectate lyase causes a weight loss of the ramie fibre of 25%. Arg235 is an essential catalytic residue to degumming ramie fibre 4.2.2.2 pectate lyase industry biotechnological applications of microbial pectate lyases in plant fiber processing are considered as environmentally friendly. As such, they become promising substitutes for conventional chemical degumming process 4.2.2.2 pectate lyase industry pectate lyase (Bsp165PelA) from Bacillus sp. N16-5 has a great potential in industrial applications because it shows high specific activity under extremely alkaline conditions 4.2.2.2 pectate lyase industry the conventional degumming process of ramie with alkaline treatment at high temperature causes severe environmental pollution. Pectate lyases can be used to remove pectin from ramie in a degumming process with reduced environmental pollution and energy consumption 4.2.2.3 mannuronate-specific alginate lyase food industry the KJ-2 polyMG-specific alginate lyase can be used in combination with other alginate lyases for a synergistic saccharification of alginate 4.2.2.5 chondroitin AC lyase food industry in Flavobacterium columnare strains C, E, G and H isolated from disease outbreaks, chondroitinase activity is significantly higher in the virulent, rhizoid variants than in the rough variants of the same strain. Temperature significantly increases the adhesion of rhizoid variants up to 20°C. Both rhizoid colony morphology and high chondroitinase activity seem to be needed for virulence and temperature may promote the adhesion of the virulent variants to surfaces at fish farms 4.2.2.9 pectate disaccharide-lyase industry degumming and retting of fiber crops and pre-treatment of pectic waste water from fruit juice industries 4.2.2.10 pectin lyase food industry enzyme is used for maceration and clarification in the process of fruit juice production. The recombinant strain 105 has a high potential to produce pectin lyase for application in industrial processes, such as textile and plant fiber processing, coffee and tea fermentation, oil extraction, industrial wastewater treatment, and paper making. It offers the advantage of producing great amounts of PL using sugar cane juice as the sole carbon source, which would lower production costs 4.2.2.10 pectin lyase food industry homogeneous pectin lyase from Penicillium canescens exhibits the ability to clarify apple juice. Efficient treatment of juice requires 0.2 mg of homogeneous enzyme 4.2.2.10 pectin lyase food industry successfully applied to production and clarification of juice 4.2.2.10 pectin lyase food industry commercial pectic enzyme plays an important role in the process of winemaking for extraction, clarification, and filtration of fruit juice and wine puree to increase the yield and quality, such as pigment, flavor, transmittance, and viscosity 4.2.2.10 pectin lyase food industry used for apple juice clarification 4.2.2.10 pectin lyase food industry application for clarification of fruit juice. For apple, orange, pomegranate juices treated with the partially purified enzyme, the clarity values are 219.74, 206.38 and 203.48%, respectively 4.2.2.10 pectin lyase food industry pectin lyase PNL-ZJ5A can effectively decrease the viscosity and improve the yield of apple juice and light transmittance 4.2.2.10 pectin lyase industry enzyme shows retting of Crotalaria juncea fibre in the presence of EDTA 4.2.2.10 pectin lyase industry purified enzyme shows efficient retting of Crotolaria juncea fibres 4.2.2.11 guluronate-specific alginate lyase food industry the KJ-2 polyMG-specific alginate lyase can be used in combination with other alginate lyases for a synergistic saccharification of alginate 4.2.2.11 guluronate-specific alginate lyase industry alginate lyase is a promising biocatalyst because of its application in saccharification of alginate for the production of renewable biofuels 4.2.2.22 pectate trisaccharide-lyase industry food and textile industry 4.2.2.23 rhamnogalacturonan endolyase food industry rhamnogalacturonan lyase is useful in the processing of fruit, where it is important that the commercial pectolytic enzyme preparations solubilize and hydrolyze the branched RG structures, which otherwise remain as colloidally dissolved polymers in the juice and lead to problems during filtration and clarification 4.2.3.16 (4S)-limonene synthase industry limonene is an aromatic component in numerous products like beverages and cosmetics 4.2.3.124 2-deoxy-scyllo-inosose synthase industry the enzyme converts the sustainable source glucose 6-phosphate to the carbocycle 2-deoxy-scylla-inosose, which easily aromatizes to yield catechol 4.3.1.1 aspartate ammonia-lyase food industry propionic acid bacteria isolates originating from cheese show a wide range of aspartase activity. Aspartase activity is strain-dependent and each strain must be tested separately in order to be able to choose the most suitable starter culture for cheese production.70% of the 100 isolates tested, show very low levels of aspartate activity 4.3.1.1 aspartate ammonia-lyase industry aspartate synthesis 4.3.1.24 phenylalanine ammonia-lyase food industry the enzyme can be used for the development of dietary foods and biotechnological products for patients with phenylketonuria 4.3.1.24 phenylalanine ammonia-lyase food industry the enzyme from Cyathobasis fruticulosa is a potential candidate for serial production of dietary food and biotechnological products 4.3.1.25 phenylalanine/tyrosine ammonia-lyase food industry the enzyme is a useful biocatalyst for removal of L-phenylalanine from protein hydrolysates, which can be evaluated as potential ingredients in foodstuffs for phenylketonuria patients. The enzyme is also capable to catalyze the deamination of L-tyrosine to p-coumaric acid but at a substantially low reaction rate. Therefore, the final content of L-Tyr in samples treated with L-phenylalanine ammonia-lyase should be analyzed in each case and taken in consideration to avoid its deficiency in phenylketonuria patients 4.3.3.7 4-hydroxy-tetrahydrodipicolinate synthase food industry L-lysine, one of the essential amino acids required for nutrition in animals and humans, is widely used in the food industry, medical industry, etc. L-lysine has been mainly produced by microbial fermentation employing mutant strains of bacteria. An L-lysine high-yielding strain is developed by modification of aspartokinase III and dihydrodipicolinate synthetase 4.3.3.7 4-hydroxy-tetrahydrodipicolinate synthase industry considering the industrial application of this protein, such as its use for lysine biosynthesis, stable conformation via tight tetramerization interfaces may make this valuable protein to be more useful 4.4.1.13 cysteine-S-conjugate beta-lyase food industry transformed wine yeast strain has a 10fold higher activity of cysteine-S-conjugate beta-lyase 4.4.1.13 cysteine-S-conjugate beta-lyase food industry improvement of wine aroma during fermentation of a Vitis vinifera cultivar Sauvignon blanc juice 4.4.1.14 1-aminocyclopropane-1-carboxylate synthase food industry 1-aminocyclopropane-1-carboxylate synthase is the rate-limiting enzyme in ethylene biosynthesises, ethylene biosynthesis in ripening banana fruit is controlled differently in the pulp tissue and in the peel tissue, treatment with 1-methylcyclopropene, an ethylene action inhibitor, either induces or prevents 1-aminocyclopropane-1-carboxylate (ACC) synthase activity 4.4.1.14 1-aminocyclopropane-1-carboxylate synthase food industry chilling stress induces increased ethylene production, O2 – is involved in the chilling induced increases in ACS activity, but not H2O2 4.4.1.14 1-aminocyclopropane-1-carboxylate synthase food industry due to increased ACC synthesis treatment with 0.5 ml/l of ethylene for 12 h accelerates ripening of the fruits, fruits are edible 3 days after treatment, compared to 6-7 days for untreated mangoes 4.4.1.14 1-aminocyclopropane-1-carboxylate synthase food industry silencing of the ACACS2 gene using genetic engineering techniques can be used to control natural flowering in commercial situations 4.4.1.14 1-aminocyclopropane-1-carboxylate synthase food industry wounding and pre-treatment with 1-methylcyclopropene promotes ethylene production by inducing expression of the ACC synthase, which accelerates persimmon fruit softening 4.8.1.2 aliphatic aldoxime dehydratase industry production of nitriles 5.1.1.13 aspartate racemase food industry the enzyme from the lactic acid bacterium Lactobacillus sakei NBRC 15893 is considered to be involved in D-aspartate synthesis during the brewing process of Japanese sake at low temperatures 5.1.3.11 cellobiose epimerase food industry the enzyme can be used for production of the probiotic lactulose 5.1.3.11 cellobiose epimerase food industry the enzyme is of interest for the dairy industry due to their ability to convert lactose into epilactose and lactulose, rare disaccharides with prebiotic properties 5.1.3.11 cellobiose epimerase food industry the enzyme may introduce an added value for particular dairy products by in situ production of the prebiotic sugar epilactose 5.3.1.B3 L-ribulose isomerase industry a novel way of producing L-ribose from the readily available raw material L-arabinose is described 5.3.1.4 L-arabinose isomerase food industry production of D-tagatose 5.3.1.4 L-arabinose isomerase food industry production of D-tagatose as a low-calorie sugar-substituting sweetener 5.3.1.4 L-arabinose isomerase food industry production of D-tagatose as a low-calorie sugar-substituting sweetener lower pH is preferable for industrial production 5.3.1.4 L-arabinose isomerase food industry production of D-tagatose as a low-calorie sugar-substituting sweetener, reactor was run for 50 days 5.3.1.4 L-arabinose isomerase food industry production of D-tagatose as a low-calorie sugar-substituting sweetener, the D-tagatose yield from the mutated enzyme is higher than from the wild type 5.3.1.4 L-arabinose isomerase food industry hyperthermophilic L-arabinose isomerase is useful in the commercial production of D-tagatose as a low-calorie bulk sweetener 5.3.1.4 L-arabinose isomerase industry a novel way of producing L-ribose from the readily available raw material L-arabinose is described 5.3.1.5 xylose isomerase food industry thermophilic xylose isomerase from Opuntia vulgaris can serve as a good alternate source of enzyme for use in the production of high fructose corn syrup 5.3.1.5 xylose isomerase food industry xylose isomerase is widely used for production of glucose fructose syrup, a natural sweetener in dietary and preventive nutrition 5.3.1.5 xylose isomerase food industry xylose isomerase isozyme T80 serves as potential alternate catalytic converter of glucose in the production of high-fructose corn syrup for the sweetener industry and for ethanol production 5.3.1.5 xylose isomerase food industry industrial production of high fructose corn syrup 5.3.1.14 L-rhamnose isomerase food industry L-rhamnose isomerase is used in rare sugar production 5.3.1.14 L-rhamnose isomerase industry as D-allose and D-psicose are rare sugars, existing in small amounts in nature, Pseudomonas stutzeri L-rhamnose isomerase is exploited for industrial applications in rare sugar production 5.3.1.14 L-rhamnose isomerase industry industrial applications in rare sugar production 5.3.1.15 D-lyxose ketol-isomerase food industry the enzyme is an industrial producer of D-lyxose 5.3.3.2 isopentenyl-diphosphate DELTA-isomerase industry over-expression of isopentenyl diphosphate isomerase and 1-deoxy-D-xylulose 5-phosphate synthase in combination with heterologous expression of squalene/phytoene synthase and farnesyl diphosphate synthase of Streptomyces peucetius in Escherichia coli facilitates the synthesis of the industrially important compound squalene 5.3.4.1 protein disulfide-isomerase industry PDI assists incorporation of cysteine-containing compounds (CCCs) into hair and wool substrates in order to generate milder methods to dye hair with longer lasting colour by creating new disulfide bonds between hair and peptide. PDI-assists promotion of the migration of CCCs (dyes), previously attached to keratin, along hair fibres, to avoid repetitive hair dyeing procedures. PDI induces controlled release of a CCC protein (e.g. reduced form of RNase A) from wool matrices 5.4.2.2 phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) food industry the enzyme is involved in production of sphingans, extracellular polysaccharides used as thickeners, emulsifiers and gelling agents, its overexpression increases the sphingan production of the transformed cell 5.4.2.8 phosphomannomutase food industry the enzyme is involved in production of sphingans, extracellular polysaccharides used as thickeners, emulsifiers and gelling agents, its overexpression increases the sphingan production of the transformed cell 5.4.99.11 isomaltulose synthase food industry isomaltulose is widely used as sucrose substitute in diet and diabetes products 5.4.99.11 isomaltulose synthase food industry sucrose isomerase activity is used industrially for the conversion of sucrose into isomers, particularly isomaltulose or trehalulose, which have properties advantageous over sucrose for some food uses. The industrial potential may be further enhanced by selection for variants that do not catabolize the sucrose substrate 5.4.99.11 isomaltulose synthase food industry sucrose isomerase activity is used industrially for the conversion of sucrose into isomers, particularly isomaltulose or trehalulose, which have properties advantageous over sucrose for some food uses.The industrial potential may be further enhanced by selection for variants that do not catabolize the sucrose substrate