EC Number   |
Recommended Name |
Application |
|---|
    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 |
