EC Number   |
Recommended Name  |
Application |
|---|
   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 |
| 3.4.24.27 | 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 |
| 3.4.24.28 | 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 |
| 3.5.1.24 | 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 |
| 3.5.1.5 | 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 |
| 3.5.1.75 | 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 |
| 3.5.3.1 | 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 |
| 3.7.1.1 | oxaloacetase |
food industry |
oxalate toxicity is a concern for the commercial application of fungi in the food and drug industries |
| 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 |
| 4.1.1.15 | 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 |
| 4.1.2.13 | 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 |
| 4.1.99.1 | tryptophanase |
food industry |
expression of enzyme in wine yeast results in a strong increase of passion fruit aroma in wine |
| 4.2.1.92 | hydroperoxide dehydratase |
food industry |
the enzyme produces aldehydes that are used as flavours in foods and beverages |
| 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 |
| 4.2.2.11 | 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 |
| 4.2.2.2 | 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 |
| 4.2.2.23 | 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 |
| 4.2.2.3 | 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 |
| 4.3.1.1 | 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 |
| 4.3.1.24 | 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 |
| 4.4.1.13 | 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 |
| 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 |
| 5.3.1.14 | L-rhamnose isomerase |
food industry |
L-rhamnose isomerase is used in rare sugar production |
| 5.3.1.15 | D-lyxose ketol-isomerase |
food industry |
the enzyme is an industrial producer of D-lyxose |
| 5.3.1.4 | 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 |
| 5.3.1.5 | 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 |
| 5.4.2.2 | 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 |
