EC Number   |
Recommended Name  |
Application |
|---|
   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 |
| 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 |
| 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 |
| 4.2.3.16 | (4S)-limonene synthase |
industry |
limonene is an aromatic component in numerous products like beverages and cosmetics |
| 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 |
| 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 |
 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 |
| 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 |
| 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) |
| 2.5.1.32 | 15-cis-phytoene synthase |
food industry |
developement nutritional plants enriched with carotenoids |
| 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 |
| 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 |
| 1.1.1.312 | 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 |
| 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 |
| 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 |
| 1.1.1.102 | 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 3.5.1.117 | 6-aminohexanoate-oligomer endohydrolase |
industry |
the partial enzymatic hydrolysis of nylon surfaces by NylC can be used to change the smoothness of nylon fibers |
| 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 |
| 2.7.2.1 | acetate kinase |
industry |
enzyme involved in the wasteful production of acetate during conversion of cellulose to ethanol |
| 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 |
| 3.4.22.14 | 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 |
| 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 |
| 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 |
| 3.5.3.12 | 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 |
| 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 |
| 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 |
| 4.8.1.2 | aliphatic aldoxime dehydratase |
industry |
production of nitriles |
| 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 |
| 3.1.3.1 | 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 |
| 1.1.99.20 | alkan-1-ol dehydrogenase (acceptor) |
industry |
microbiological degradation appears to be the only means to decompose this group of polymers |
| 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 |
| 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 |
| 3.2.1.51 | alpha-L-fucosidase |
food industry |
the enzyme catalyse the transglycosylation reaction leading to production of fucosylated human milk oligosaccharides |
| 3.2.1.40 | 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 |
| 3.5.1.4 | 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 |
| 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 |
| 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 |
| 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 |
| 2.4.1.4 | 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 |
