EC Number   |
Recommended Name |
Application |
|---|
   3.2.1.99 | arabinan endo-1,5-alpha-L-arabinanase |
nutrition |
commercial applications in fruit and vegetable processing, particularly in apple juice manufacture where their use prevents haze formation in pectinase-treated apple pulp by depolymerizing debranched arabinan, linear alpha-1,5-arabinan, formed by the action of alpha-L-arabinofuranosidases during this process |
| 3.2.1.99 | arabinan endo-1,5-alpha-L-arabinanase |
nutrition |
useful for pectin production from sugar beet pulp |
| 3.2.1.99 | arabinan endo-1,5-alpha-L-arabinanase |
nutrition |
useful for pectin extraction from citrus peel from fruit-juice industries and sugar-beet pulp from sugar factories |
| 3.2.1.99 | arabinan endo-1,5-alpha-L-arabinanase |
nutrition |
production of L-arabinose from plant arabinan at high temperatures |
 3.2.1.116 | glucan 1,4-alpha-maltotriohydrolase |
nutrition |
enzyme produced on the industrial scale for the production of high maltotriose-containing syrup |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
nutrition |
utilization of starch from corn, cereals, potatoes, sorghum and other plants as valuable raw material for the production of glucose, fructose, oligosaccharides, and alcohol |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
nutrition |
production of isomaltosaccharides with various compositions and useful properties is in great demand in the starch industry, efficient process with cooperative action of maltogenic amylase and alpha-glucanotransferase from Thermotoga maritima |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
nutrition |
transglycosylation activity of BbmA can be applied for the preparation of branched oligosaccharide mixtures, which are used as low calorie sweeteners or humectants |
| 3.2.1.147 | thioglucosidase |
nutrition |
in intact vegetable tissues, the enzyme is present in compartments separated from its substrate, the glucosinolates. The enzymatic hydrolysis can merely occur after cellular disruption. In this respect, processes such as cutting, cooking, freezing, or pressurizing of the vegetables will have large effect on the glucosinolate hydrolysis by myrosinase |
| 3.2.1.147 | thioglucosidase |
nutrition |
study on kinetics of thermal enzyme inactivation in broccoli juice at elevated pressure for optimization of health effects. Pressure has an antagonistic effect on thermal inactivation at 50°C and above. Isothiocyanates formed by enzyme are relatively thermolabile and pressure stable |
| 3.2.1.149 | beta-primeverosidase |
nutrition |
beta-primeverosidase is a key enzyme in tea aroma formation |
| 3.2.2.22 | rRNA N-glycosylase |
nutrition |
study on the effects of heat treatment on the detection and toxicity of ricin added to milk- and soy-based infant formulas. Half-lives of ricin cytotoxicactivity in a milk-based infant formula at 70°C, 75°C, 80°C, 85°C, and 90°C are 9.8, 5.8, 5.1, 3.1, and 1.8 min, respectively, the comparable values for a soy-based infant formula are 16, 8.7, 6.9, 3.0, and 2.0 min |
| 3.4.11.2 | membrane alanyl aminopeptidase |
nutrition |
total degradation of the bitter peptide beta-CN f193-209 by aminopeptidase PepN does not occur without endopeptidases activities PepO and PepO3 |
| 3.4.11.5 | prolyl aminopeptidase |
nutrition |
cheese ripening, debittering, milk processing |
| 3.4.11.5 | prolyl aminopeptidase |
nutrition |
collagen degradation |
| 3.4.11.10 | bacterial leucyl aminopeptidase |
nutrition |
debittering of casein- and soyprotein-derived peptide solutions |
| 3.4.11.22 | aminopeptidase I |
nutrition |
the enzyme is useful to reduce bitterness of food products by hydrolysis of peptides with hydrophobic amino acids causing the bitter taste |
| 3.4.13.19 | membrane dipeptidase |
nutrition |
cadmium given in drinking water compromises protein digestion and absorption of nutrients particularly in the proximal region of small intestine |
| 3.4.14.1 | dipeptidyl-peptidase I |
nutrition |
muscle DPP I may be a key enzyme responsible for the generation of dipeptides in Jinhua ham processing |
| 3.4.15.6 | cyanophycinase |
nutrition |
Nicotiana benthamiana-expressed cyanophycin fed in combination with Nicotiana benthamiana-expressed CGPase is hydrolysed in the intestine of mice, and high levels of beta-Asp-Arg dipeptides are found in plasma. However, there is no increase in Asp and Arg or its metabolite ornithine in plasma. Intestinal degradation of cyanophycin by CGPase leads to low intestinal cyanophycin content 4 h after consumption, but after ingestion of cyanophycin alone, high cyanophycin concentrations remain in the large intestine |
| 3.4.16.5 | carboxypeptidase C |
nutrition |
MpiCP-1 suppresses and reverses the development of the bitterness taste that results from the pepsin hydrolysis of soybean protein by releasing mainly hydrophobic amino acids from the C-termini of the bitter components |
| 3.4.19.6 | pyroglutamyl-peptidase II |
nutrition |
animals drinking a 2.5% NaCl solution for 7 d present body weight reduction. Despite their negative energy balance, they avoid food and have increased hypothalamic paraventricular nucleus thyrotropin releasing hormone expression and thyroid-stimulating hormone serum levels. Increased medial basal hypothalamic pyroglutamyl-aminopeptidase II activity in dehydration-induced anorexia rats might counteract their high thyrotropin releasing hormone release |
| 3.4.21.5 | thrombin |
nutrition |
comparison of anticoagulation response to thrombin inhibitors ximelagatran and warfarin in rats on a normal diet to those on a vitamin K deficient diet. Ximelagatran and warfarin increase prothrombin time, activated partial thromboplastin time and ecarin clotting time in rats on normal diet. Vitamin K deficient diet alone causes modest increases in prothrombin time, activated partial thromboplastin time and ecarin clotting time. The anticoagulant activity of both ximelagatran and warfarin is significantly greater in rats on vitamin K deficient diet compared to those on normal diet. Thrombin activity is reduced by both ximelagatran and warfarin to 58% and 44%, respectively, in rats on normal diet. Thrombin activity is virtually abolished by both drugs in rats on vitamin K deficient diet |
| 3.4.21.7 | plasmin |
nutrition |
hydrolysis of milk proteins alphaS-casein, beta-casein, kappa-casein, alpha-lactalbumin, beta-lactoglobulin, and lactoferrin is highly dependent on photooxidation state of substrate. Changes in the formation of potential angiotensin I-converting enzyme-inhibitory peptides as well as peptides proposed to have anti-bactericidal activities are observed after oxidation of substrates before plasmin hydrolysis |
| 3.4.21.25 | cucumisin |
nutrition |
fruit development |
| 3.4.21.25 | cucumisin |
nutrition |
meat tenderizer |
| 3.4.21.26 | prolyl oligopeptidase |
nutrition |
oral supplementation of celiac patients with postproline cutting enzymes could be a valuable method to eradicate the proline-rich T cell stimulatory epitopes from gluten proteins, the Aspergillus niger enzyme is a good candidate because it is highly resistant to acidic conditions and degradation by pepsin, found in the stomach, in contrast to other POPs |
| 3.4.21.63 | Oryzin |
nutrition |
used in food processing, strain U1521 assumes industrial and economic importance |
| 3.4.21.96 | Lactocepin |
nutrition |
cheese making, cheese starter organism, dairy industry |
| 3.4.22.2 | papain |
nutrition |
papain is used in the preparation of fish protein concentrates from fish waste |
| 3.4.22.2 | papain |
nutrition |
chill-proofing ability in beer |
| 3.4.22.2 | papain |
nutrition |
used in the tenderisation of meat by its action on connective tissue and muscle protein. Beef is the only meat that is routinely subjected to papain tenderisation and the application of this technology is almost exclusively restricted to the USA |
| 3.4.22.2 | papain |
nutrition |
the enzyme is used for the development of roast beef-like flavours by partial hydrolysis of proteins |
| 3.4.22.2 | papain |
nutrition |
production of dehydrated pulses and beans |
| 3.4.22.2 | papain |
nutrition |
papain is used in the brewing process for two main purposes: use in chillproofing and use in the mash tun to uncrease the yield of extract and therefore decrease malt consumption. The enzyme can be used in the production of specialized fish protein concentrate for use as a milk replacer when feeding calves and piglets. The enzyme is used to improve the protein dispersibility index of soya flour. Treatment of oil seed cake to incrase the nitrogen solubility index and/or the protein dispersibility index |
| 3.4.22.2 | papain |
nutrition |
used extensively in food processing especially in tenderization of meat |
| 3.4.22.6 | chymopapain |
nutrition |
at low pH, enzyme undergoes conformational transition leading to instability and rapid degradation by pepsin. To be effective in gut after oral administration, enzyme needs to be protected against acid denaturation and degradation |
| 3.4.22.14 | actinidain |
nutrition |
actinidin induces protease-dependent morphology changes of T84 human colorectal adenocarcinoma cells leading to cell rounding and desquamation of the epithelial monolayer, without affecting cell viability |
| 3.4.22.25 | glycyl endopeptidase |
nutrition |
the enzyme needs to be protected from acid denaturation and proteolysis in the gut after oral administration to be effective as cysteine protease |
| 3.4.22.30 | Caricain |
nutrition |
at low pH, enzyme undergoes conformational transition leading to instability and rapid degradation by pepsin. To be effective in gut after oral administration, enzyme needs to be protected against acid denaturation and degradation |
| 3.4.22.67 | zingipain |
nutrition |
meat tenderizing agent, stability of the enzyme can be greatly improved, increasing its attractiveness as a commercial product |
| 3.4.23.1 | pepsin A |
nutrition |
modification of the substrate specificity of porcine pepsin for the enzymatic production of bovine hide gelatin, The mutant enzyme F111T/L112F can potentially enhance the rate of solubilization of bovine hide collagen under conditions mild enough to maintain the triple helix structure and hence minimize the rate of subsequent denaturation and proteolytic cleavage |
| 3.4.23.1 | pepsin A |
nutrition |
role for proteolysis in killing of bacteria. Addition of enzyme alone or in gastric juice at pH 3.5 reduces viability of suspensions of Escherichia coli 690 and K-12 by 100% after 100 min incubation. With Helicobacter pylori, viable counts decrease by 50% after 20 min |
| 3.4.23.1 | pepsin A |
nutrition |
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 |
| 3.4.23.18 | Aspergillopepsin I |
nutrition |
Aspergillus awamori and the extracellular protease play important roles in japanese food production, overview |
| 3.4.23.18 | Aspergillopepsin I |
nutrition |
Aspergillus oryzae and the extracellular protease play important roles in japanese food production, overview |
| 3.4.23.18 | Aspergillopepsin I |
nutrition |
Aspergillus saitoi and the extracellular protease play important roles in japanese food production, overview |
| 3.4.23.18 | Aspergillopepsin I |
nutrition |
Aspergillus sojae and the extracellular protease play important roles in japanese food production, overview |
| 3.4.23.18 | Aspergillopepsin I |
nutrition |
Aspergillus species and the extracellular protease play important roles in japanese food production, overview |
| 3.4.23.22 | Endothiapepsin |
nutrition |
the enzyme can be used as a fungal rennet in cheese production |
| 3.4.23.23 | Mucorpepsin |
nutrition |
Mucor rennin can be used as a substituting enzyme for calf chymosin in the cheese industry |
| 3.4.23.23 | Mucorpepsin |
nutrition |
used as a substitute for calf chymosin, making use of its milk-clotting activity |
| 3.4.23.23 | Mucorpepsin |
nutrition |
wide industrial appplication as calf rennet substitutes in cheese manufacture |
| 3.4.24.26 | pseudolysin |
nutrition |
pseudolysin is an enzyme cleaving gluten effectively at extremely low as well as near neutral pH values. The potential to degrade gluten during gastric transport opens possibilities for its application as a therapeutic agent for the treatment of celiac disease |
| 3.4.24.27 | thermolysin |
nutrition |
the enzyme is used for synthesis of N-carbobenzyloxy L-Asp-L-Phe methyl ester, a precursor of the artificial sweetener aspartam |
| 3.4.24.30 | coccolysin |
nutrition |
wide utilization in the production of dairy products like yoghurt, hard cooked cheese, and soft cheese |
| 3.5.1.2 | glutaminase |
nutrition |
the enzyme from Aspergillus oryzae is important in soy sauce fermentation |
| 3.5.1.2 | glutaminase |
nutrition |
the enzyme is applicated in Japanese soy sauce fermentation |
| 3.5.1.5 | urease |
nutrition |
elimination of the urea in alcoholic beverages |
| 3.5.1.15 | aspartoacylase |
nutrition |
development of a general and simple procedure for the resolution of racemic amino acids |
| 3.5.1.22 | pantothenase |
nutrition |
vitamin determination, extremely sensitive assay of pantothenic acid in various dietary sources, as low as 5 nM concentration |
| 3.5.1.24 | choloylglycine hydrolase |
nutrition |
BSH is a key mechanistic microbiome target for the development of non-antibiotic food additives to improve animal feed production and for the design of measures to control obesity in humans |
| 3.5.1.44 | protein-glutamine glutaminase |
nutrition |
the enzyme might be useful to improve solubility and susceptibility of zeins from maize, which have high antioxidant potential and important functional properties in nutrition |
| 3.5.1.61 | mimosinase |
nutrition |
implication for reducing the toxicity of Leucaena used for stock feed, the product 3-hydroxy-4(1H)-pyrid-4-one, DHP, is goitrogenic in animals but is less toxic than mimosine, conversion of mimosine to DHP is therefore beneficial for the use of Leucaena as animal feed |
| 3.5.1.75 | urethanase |
nutrition |
practically ineffective for the elimination of urethane from alcoholic beverages, because the enzyme is inactive in high concentrations of alcohol, ethanol, and at acidic pH |
| 3.5.1.75 | urethanase |
nutrition |
enzyme may be practically applicable in removal of urethane from alcoholic beverages, because very high ethanol resistance, high activity at acidic condition, pH 5.0 and very low Km value for urethane |
| 3.5.1.75 | urethanase |
nutrition |
great advantage for industrial removal of urethane, potentially carcinogenic, mutagenic and teratogenic to human, from alcoholic beverages |
| 3.5.1.75 | urethanase |
nutrition |
strain IFO 12107, enzyme may be a practical means of removing urethane from alcoholic beverages, because its higher activity under acidic conditions, pH 4.5, its high ethanol resistance and its low Km value for urethane |
| 3.5.2.2 | dihydropyrimidinase |
nutrition |
- |
| 3.5.2.2 | dihydropyrimidinase |
nutrition |
useful for production of D-amino acids, microbial hydantoinases used industrially to produce N-carbamoyl-D-hydroxyphenylglycine |
| 3.5.2.2 | dihydropyrimidinase |
nutrition |
no degradative activity for L-tryptophan, method for L-tryptophan production is very promising as a commercial process |
| 3.5.3.1 | arginase |
nutrition |
oopherectomized animals treated with 0.5% cholesterol-enriched diet. Diet results in increase in plasma lipids, atheromatous lesions as well as expression of enzyme isoforms arginase I and II and an increase in cellular proliferation. Diet plus supplementation of 17beta-estradiol results in a decrease of atheromatous lesions and reduced expression of both enzyme isoforms and inducible NO synthase |
| 3.5.3.12 | agmatine deiminase |
nutrition |
developing of an analytic method for agmatine, being an important reagent for food research |
| 3.5.4.16 | GTP cyclohydrolase I |
nutrition |
construction of transgenic tomato plants expressing GCHI for engineering of the peteridine branch of folate synthesis in Lycopersicon esculentum by folate biofortification, overview |
| 3.13.2.2 | S-adenosyl-L-methionine hydrolase (L-homoserine-forming) |
nutrition |
dimethylsulfide is volatile and serves as quality marker for cabbage |
| 4.1.1.5 | acetolactate decarboxylase |
nutrition |
ADC has a practical application in brewing, used to speed maturation |
| 4.1.1.5 | acetolactate decarboxylase |
nutrition |
use of enzyme allows the acceleration of beer fermentation/maturation because it shunts diacetyl formation, new process involving recoverable encapsulated enzyme |
| 4.1.1.15 | glutamate decarboxylase |
nutrition |
use of Bacillus subtilis strain expressing L-glutamate decarboxylase from Lactobacillus brevis for preparation of Korean fermented soybean product Chungkukjang results in significantly higher levels of gamma-aminobutanoate in products |
| 4.1.1.20 | diaminopimelate decarboxylase |
nutrition |
lysine complementation of calf nutrition by lysine-overproducing rumen bacteria, considered |
| 4.1.1.22 | histidine decarboxylase |
nutrition |
dairy products must be dedicated to a thorough risk analysis and development of strategies to contrast the presence of histaminogenic Streptococcus thermophilus strains in products from raw or mildly heat-treated milk. The HdcA enzyme in crude cell-free extracts is mostly active at acidic pH values common in dairy products. NaCl concentrations lower than 5% do not affect its activity. The enzyme is quite resistant to heat treatments resembling low pasteurization, but is inactivated at 75°C for 2 min |
| 4.1.1.25 | tyrosine decarboxylase |
nutrition |
information about enzyme may contribute to the prevention of tyramine formation during wine production and storage |
| 4.1.1.25 | tyrosine decarboxylase |
nutrition |
production of plant secondary metabolites |
| 4.1.1.29 | sulfinoalanine decarboxylase |
nutrition |
mice supplemented with dietary cholate exhibit reduced hepatic cysteine sulfinic acid decarboxylase mRNA while those receiving cholestyramine exhibit increased mRNA. Activation of farnesoid X receptor suppresses cysteine sulfinic acid decarboxylase mRNA expression whereas cysteine sulfinic acid decarboxylase expression is increased in mice lacking farnesoid X receptor small heterodimer partner Shp. Hepatic hypotaurine concentration, the product of cysteine sulfinic acid decarboxylase, is higher in Shp-/- mice with a corresponding increase in serum taurine conjugated bile acids. Fibroblast growth factor 19 administration suppresses hepatic cholesterol 7-alpha-hydroxylase CYP7A1 mRNA but does not change cysteine sulfinic acid decarboxylase mRNA expression |
| 4.2.2.10 | pectin lyase |
nutrition |
post harvest spoilage of citrus products |
| 4.2.2.10 | pectin lyase |
nutrition |
macerin can be used in the production of fruit and vegetable purees and homogeneized pulp juices |
| 4.2.2.10 | pectin lyase |
nutrition |
potential for use in fruit juice processing |
| 4.2.2.17 | inulin fructotransferase (DFA-I-forming) |
nutrition |
di-D-fructofuranose-1,2':2,1'-dianhydride is expected to be useful as a low-calorie sweetener |
| 4.2.3.1 | threonine synthase |
nutrition |
interesting with respect to attempts to obtain transgenic plants with elevated levels of essential amino acids Met, Lys, Thr |
| 4.2.3.25 | S-linalool synthase |
nutrition |
the enzyme can be used to modify the flavor/nuritional value of vegetables, e.g. tomato fruits, by enzyme expression in transgenic plants |
| 4.2.3.118 | 2-methylisoborneol synthase |
nutrition |
2-methylisoborneol produced by cyanobacteria,, causes an unpleasant taste and odor in tap water. Bacterial cultures show higher accumulation of 2-methylisoborneol at 30°C than at 4°C or 20°C after 24 h of culture |
| 4.2.3.133 | alpha-copaene synthase |
nutrition |
tuber-specific over-expression of potato alpha-copaene synthase gene results in up to 15fold enhanced levels of alpha-copaene with a positive correlation between transgene expression level and alpha-copaene abundance. No aroma differences in the transgenic samples compared with controls and no significant differences in taste attributes are found. Sensory analysis suggests that alpha-copaene is not a major component of potato flavour |
| 4.3.1.24 | phenylalanine ammonia-lyase |
nutrition |
the enzyme can be used for the development of dietary foods and biotechnological products for patients with phenylketonuria |
| 4.3.1.25 | phenylalanine/tyrosine ammonia-lyase |
nutrition |
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 |
| 4.4.1.1 | cystathionine gamma-lyase |
nutrition |
Lactobacillus fermentum is contained in the natural starter used for producing Parmesan cheese and as adventitious non-starter lactic acid bacteria. It also populates several Italian and Swiss cheeses. EC 4.4.1.1 is stable in the conditions of cheese ripening and may contribute to the biosynthesis of sulfur-containing compounds |
| 4.4.1.4 | alliin lyase |
nutrition |
dense phase carbon dioxide has a significant effect on the greening of intact garlic (Allium sativum L.) cloves. The formation of the green colour is a comprehensive result of dense phase carbon dioxide on changing cellular structure, alliin consumption and alliinase activity. DPCD treatment at 10 MPa and 55°C is the optimum condition for the greening of Laba garlic |
| 4.4.1.11 | methionine gamma-lyase |
nutrition |
the enzymatic degradation of L-methionine and subsequent formation of volatile sulfur compounds is believed to be essential for flavour development in cheese. Overproduction of Brevibacterium linens methionine-gamma-lyase in bacteria such as lactic acid bacteria can be a more efficient way to increase cheese flavour of some cheeses, among others, cheddar, than the addition of Brevibacterium linens cells or extracts, which is not successful in enhancing cheese flavour |
| 4.4.1.11 | methionine gamma-lyase |
nutrition |
importance in flavor formation during cheese ripening |
| 4.4.1.13 | cysteine-S-conjugate beta-lyase |
nutrition |
possible essential role of the enzyme in flavor development in cheese is suggested |
| 5.1.3.11 | cellobiose epimerase |
nutrition |
cellobiose 2-epimerase is an attractive enzyme to produce epilactose (4-O-beta-Dgalactosyl-D-mannose) from lactose. Epilactose is a non-digestible oligosaccharide, and enhances proliferation of bifidobacilli and lactobacilli in the human gut |
| 5.1.3.11 | cellobiose epimerase |
nutrition |
cellobiose 2-epimerases can be used for the production of epilactose from milk ultrafiltrate containing lactose |
