EC Number   |
Recommended Name |
Application |
|---|
   3.4.22.1 | cathepsin B |
food industry |
the gel strength of modori gel is increased by suppression of cathepsin B activity using CA-074. Cathepsin B may cause modori phenomenon. Therefore, our results suggest that natural cysteine protease inhibitor, such as oryzacystatin derived from rice may apply to surimi-based product processing of horse mackerel to improve the quality of thermal gels |
| 3.4.22.2 | papain |
food industry |
combination of ultrasound and papain is more beneficial for improving functional properties of meat compared with the individual treatment |
| 3.4.22.2 | papain |
industry |
papain has many uses and functions in a variety of industries: clarifying beer, meat tenderization, preservation of spices, contact lens cleaners, detergents, pet food palatability, digestive aids, blood stain remover, blood coagulant and cosmetics |
| 3.4.22.2 | papain |
industry |
the cotton fabric immobilized modified papain has potential applicationsin the functional textiles field |
| 3.4.22.2 | papain |
industry |
the enzyme with high biological activity and the decomposing ability is widely used in the lines of medical application, cell isolation, food, detergents, leather, textile, cosmetic and pharmaceutical industry |
| 3.4.22.2 | papain |
industry |
catalytic properties of papain immobilized on hybrid nanoflowers are enhanced compared with that of free papain. The hybrid nanoflowers exhibit excellent reusability, high thermostability, long storage life and great potential in industrial applications |
| 3.4.22.2 | papain |
industry |
immobilization on multi-walled carbon nanotubes is beneficial to the industrial applications because of its potential to be easily separated from the end product at the end of the reaction, reuse for multiple times and allow the development of multiple enzyme reaction system |
| 3.4.22.2 | papain |
industry |
papain combined with chitosan-sodium alginate pretreated with the appropriate ultrasound can be effective technique for improving the activity of immobilized enzymes as a result of changes in its structure and intermolecular interactions. It is important to extend the application of chitosan-sodium alginate gel in the immobilized enzyme industry |
| 3.4.22.3 | ficain |
food industry |
prolonged stability of ficin at low pH values in comparison to papain can be of importance for industrial processes that run in low pH conditions such as chill haze prevention during winemaking which prompted us to check long term stability of ficin and papain at low pH and in the presence of ethanol |
| 3.4.22.3 | ficain |
industry |
enzyme is used in the food, pharmaceutical, and detergent industries |
| 3.4.22.7 | asclepain |
food industry |
asclepain f is less adequate as coagulant in cheesemaking |
| 3.4.22.14 | actinidain |
food industry |
actinidin is used as a beef tenderizer, use of actinidin-tenderized beef significantly improves emulsion stability, texture, and organoleptic properties of the sausage product |
| 3.4.22.14 | actinidain |
food industry |
actinidin, particularly at level 20 unit/g of skin, can be used to improve the yield and properties of gelatin from bovine skin |
| 3.4.22.14 | actinidain |
food industry |
the enzyme can be used in meat tenderisation |
| 3.4.22.B29 | calpain 9 |
food industry |
single nucleotide polymorphisms G7518A and C7542G are associated with carcass weight, evisceration weight, abdominal fat weight, abdominal fat percentage, and breast muscle percentage. The AA(7518)/GG(7542) genotype has the highest intramuscular fat content, highest breast muscle weight, and lower abdominal fat weight and abdominal fat percentage |
| 3.4.22.30 | Caricain |
food industry |
the enzyme detoxifies gliadin in wheat dough |
| 3.4.22.B31 | calpain 11 |
food industry |
in muscle 3 h postmortem, the decrease in unautolyzed and total activities of calpain-11, desmin content and shear force are more rapid in CaCl2-incubated samples than in control, NaCl- and EDTA-incubated samples. In the absence of calpain-1, calpain-11 with an extensive activation by adding exogenous Ca2+ could enhance the postmortem proteolysis and tenderization of ostrich muscle |
| 3.4.22.32 | Stem bromelain |
food industry |
stem bromelain immobilized on chitosan beads without glutaraldehyde yields a food-safe biocatalyst for unstable real wine future application |
| 3.4.22.32 | Stem bromelain |
food industry |
the immobilized stem bromelain has productive biotechnological applications in wine-making |
| 3.4.22.41 | cathepsin F |
food industry |
CTSF gene (encoding cathepsin F) is a suitable marker for screening pigs to improve cured weight and yield for country ham production |
| 3.4.22.41 | cathepsin F |
food industry |
CTSF gene is a suita marker for screening pigs to leimprove meat quality. CTSF gene is associated with estimated breeding values: average daily gain, lean cuts, and backfat thickness |
| 3.4.22.41 | cathepsin F |
food industry |
CTSF gene is a suitable marker for screening pigs to improve meat quality. CTSF gene is associated with estimated breeding values: average daily gain, lean cuts, and backfat thickness |
| 3.4.22.52 | calpain-1 |
food industry |
markers developed at the CAST and CAPN1 genes are suitable for use in identifying animals with the genetic potential to produce meat that is more tender |
| 3.4.22.67 | zingipain |
food industry |
application of enzyme in food industry for cheese-making or meat tenderization. Optimization of purification protocol via three-phase partitioning system |
| 3.4.22.67 | zingipain |
food industry |
zingipain can hydrolyze the gelatin from fish skin to peptides with low average molecular weights (below 690 Da) more efficiently than that from pig skin, pig bone and bovine skin. All gelatin hydrolysates show higher antioxidative activities than non-hydrolysed gelatins. Fish skin gelatin hydrolysate obtained using ginger protease exhibits the highest degree of hydrolysis (13.08%) and antioxidant activity towards 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical (97.21%) and lipid peroxidation (48.46%) |
| 3.4.23.1 | pepsin A |
food industry |
treatment with pepsin at pH 4.0 results in lowering the (pseudo)peroxidase activity of metmyoglobin both at physiological pH and at meat pH, leading to strongly enhanced prooxidative effect of mildly proteolyzed metmyoglobin on lipid oxidation |
| 3.4.23.1 | pepsin A |
food industry |
the porcine pepsin digests of cheese whey at a specific acidic pH have the potential to be used as natural food preservatives due to the presence of the three peptides with antibacterial activity against Bacillus subtilis (lactoferrin f(20-30) and beta-lactoglobulin f(14-22)) and Escherichia coli (beta-lactoglobulin f(82-103)) |
| 3.4.23.2 | pepsin B |
food industry |
the enzyme's milk-clotting activity is used for cheese making. Mutant enzyme T218S serves as a milk coagulant that contributes to an optimal flavor development in mature cheese |
| 3.4.23.4 | chymosin |
food industry |
used as milk coagulant in cheese preparation |
| 3.4.23.4 | chymosin |
food industry |
used for the production of dairy products |
| 3.4.23.4 | chymosin |
food industry |
coagulant for cheese making |
| 3.4.23.4 | chymosin |
food industry |
chymosin constitutes a traditional ingredient for enzymatic milk coagulation in cheese making |
| 3.4.23.4 | chymosin |
food industry |
the enzyme is used as milk coagulant in the cheese industry |
| 3.4.23.4 | chymosin |
food industry |
the enzyme is used for the production of Reggianito cooked cheese |
| 3.4.23.4 | chymosin |
food industry |
the enzyme is used industrially in cheese production |
| 3.4.23.4 | chymosin |
food industry |
the enzyme plays an essential role in the coagulation of milk in the cheese industry |
| 3.4.23.20 | Penicillopepsin |
food industry |
the enzyme is used in the dairy industry such as in accelerated cheese ripening |
| 3.4.23.21 | Rhizopuspepsin |
food industry |
the peptidase may function as an important alternative enzyme in milk clotting during the preparation of cheese |
| 3.4.23.25 | saccharopepsin |
food industry |
important for the nitrogen release during alcoholic fermentation in wine production which is required for subsequent malolactic fermentation by Oenococcus oeni |
| 3.4.23.25 | saccharopepsin |
food industry |
possibly involved in ripening processes of fermented meat products |
| 3.4.23.25 | saccharopepsin |
food industry |
the enzyme is detrimental to beer foam stability |
| 3.4.23.25 | saccharopepsin |
food industry |
the enzyme significantly affects the safety and quality of alcoholic drinks, especially the foam stability of beer |
| 3.4.23.40 | Phytepsin |
food industry |
cardosins from Cynara scolymus flower extract are suitable for Gouda-type cheese manufacturing. The type of coagulant has no significant effect upon the chemical parameters analyzed and pH values of the cheeses throughout ripening, and no significant differences are detected in the organoleptic properties between cheeses manufactured with Cynara scolymus brining for 40 h or animal rennet |
| 3.4.23.40 | Phytepsin |
food industry |
gene expression under postharvest chilling treatment in two pineapple varieties differing in their resistance to blackheart development reveals opposite trends. The resistant variety shows an up-regulation of AP1 precursor gene expression whereas the susceptible shows a down-regulation in response to postharvest chilling treatment. The same trend is observed regarding specific aspartic protease enzyme activity in both varieties |
| 3.4.23.40 | Phytepsin |
food industry |
use of recombinant enzyme for manufacturing sheep, goat, and cow cheeses result in a higher cheese yield for all three types of cheese when compared with synthetic chymosin |
| 3.4.23.49 | omptin |
food industry |
the peptidase shows maximal milk clotting activity at 60-65 °C and maintenance of enzymatic activity above 80% in the presence of 20 mM CaCl2 |
| 3.4.24.26 | pseudolysin |
industry |
A2 protease is usable for shrimp waste deproteinization in the process of chitin preparation, percent of protein removal after 3 h hydrolysis at 40°C with an enzyme/substrate ratio of 5 U/mg protein is about 75%. A2 proteolytic preparation also demonstrates powerful depilating capabilities of hair removal from bovine skin |
| 3.4.24.26 | pseudolysin |
industry |
pseudolysin is a biotechnologically important enzyme in the tanning industry |
| 3.4.24.26 | pseudolysin |
industry |
potential application in the leather industry and as a therapeutic agent |
| 3.4.24.27 | thermolysin |
food industry |
the enzyme can be used for production of caseicin A, an antimicrobial active peptide, from alpha-casein, for potential improvement of the safety of infant milk formula using milk-derived bioactive peptides |
| 3.4.24.27 | thermolysin |
industry |
the enzyme is used for synthesis of N-carbobenzyloxy L-Asp-L-Phe methyl ester, a precursor of the artificial sweetener aspartam |
| 3.4.24.28 | bacillolysin |
food industry |
in the beer brewing process, the neutral protease during mashing process can release more amino acids from wort such as aspartic acid, arginine, methione, and histidine, resulting in a better amino acid profile in wort |
| 3.4.24.28 | bacillolysin |
food industry |
the enzyme is an effective food additive for improving the quality of gluten-free rice bread. Bacillolysin together with subtilisin and papain increase the specific volume of gluten-free rice breads by 30-60% compared with untreated breads |
| 3.4.24.75 | lysostaphin |
food industry |
antistaphylococcal agent |
 3.5.1.1 | asparaginase |
food industry |
reduction of acrylamide level in biscuits and bread |
| 3.5.1.1 | asparaginase |
food industry |
the acrylamide contents in baked dough were reduced to sixty percent after treatment with recombinant enzyme as compared to the untreated control |
| 3.5.1.1 | asparaginase |
food industry |
the enzyme is used for reducing acrylamide formation during the potato frying process |
| 3.5.1.1 | asparaginase |
food industry |
the enzyme reduces acrylamide content in starchy fried food commodities |
| 3.5.1.1 | asparaginase |
food industry |
the final level of acrylamide in biscuits and bread is decreased by about 81.6% and 94.2%, respectively, upon treatment with 10 U asnase per mg flour |
| 3.5.1.1 | asparaginase |
food industry |
addition of partially purified L-asparaginase to potato products followed by incubation of the mixture at 37°C for 30 min leads to 92% reduction of acrylamide content |
| 3.5.1.1 | asparaginase |
food industry |
approximately 88.5% (0.978 mg/kg) acrylamide can be removed from fried potato chips by mutant V26A/E30G/D181G/V245G/G276D pre-treatment |
| 3.5.1.1 | asparaginase |
food industry |
pretreatment of potato chips and mooncakes with Asnase significantly decreases their acrylamide by 86% and 52%, respectively |
| 3.5.1.2 | glutaminase |
food industry |
microbial glutaminases are enzymes with emerging potential in both the food and the pharmaceutical industries, potential application for bioconversion of glutamine to flavor-enhancing glutamic acid |
| 3.5.1.2 | glutaminase |
food industry |
the enzyme is used in soy sauce fermentation |
| 3.5.1.4 | amidase |
industry |
the immobilized, cross-linked enzyme aggregate proves useful as a substitute for soluble amidase as a biocatalyst in the pharmaceutical and chemical industries |
| 3.5.1.5 | urease |
food industry |
the enzyme is applicable to elimination of urea in Chinese rice wine |
| 3.5.1.5 | urease |
food industry |
use of recombinant acid urease for enzymatic degradation of urea in rice wine. Ethylcarbamate, a carcinogenic compound, is formed from urea and ethanol in rice wine, therefore enzymatic elimination of urea is always attractive |
| 3.5.1.5 | urease |
industry |
enhancement of stability of immobilised urease by biocompatible polymer-conjugated magnetic beads for industrial application based on removal of urea |
| 3.5.1.11 | penicillin amidase |
industry |
PAC is used in industrial synthesis of semi-synthetic antibiotics |
| 3.5.1.11 | penicillin amidase |
industry |
penicillin acylase are industrially important enzymes that break down different penicillins to give 6-amino penicillanic acid, the precursor for synthesis of semi synthetic penicillins and cephalosporins antibiotics |
| 3.5.1.24 | choloylglycine hydrolase |
food industry |
enzyme inhibitors are promising feed additives to replace antibiotic growth promoters for enhancing the productivity and sustainability of food animals |
| 3.5.1.24 | choloylglycine hydrolase |
food industry |
inhibitors are a promising alternatives to antibiotic growth promoters for enhanced animal growth performance and food safety, required since antibiotic growth promoter usage is linked to the emergence of antibiotic resistant bacteria. Enzyme BSH inhibitors are promising feed additives to replace antibiotic growth promoters for enhanced host lipid metabolism and growth performance |
| 3.5.1.44 | protein-glutamine glutaminase |
food industry |
in food industry, protein deamination is regarded as a promising method to improve protein functionality (solubility, emulsion, foam and gelling properties) desired in food systems. The enzyme produced from Chryseobacterium proteolyticum is not toxigenic so that consumer safety is assured. The enzyme can be reproducibly produced and purified into a consistent enzyme product |
| 3.5.1.44 | protein-glutamine glutaminase |
food industry |
protein-glutaminase is contributes to improving the quality of various dairy products such as yoghurt, cheese, acid milk drinks, etc. Deamidation by protein-glutaminase improves the emulsion capacity of skim milk solution |
| 3.5.1.44 | protein-glutamine glutaminase |
food industry |
the commercial enzyme is used for enhancing food proteins solubilization. Optimization of coconut protein deamidation using protein-glutaminase and its effect on solubility, emulsification, and foaming properties of the proteins, overview |
| 3.5.1.75 | urethanase |
food industry |
urethanase is useful to reduce ethyl carbamate, i.e. urethane, in Chinese rice wine, strain CGMCC 5081 culture condition optimization for enzyme production in immobilized cells |
| 3.5.1.75 | urethanase |
food industry |
with good ethanol tolerance, the crude urethanase is able to reduce ethyl carbamate, i.e. urethane, in Chinese rice wine without the change of flavor substance in wine |
| 3.5.1.75 | urethanase |
food industry |
crosslinked enzyme aggregates of Providencia rettgeri urease (PRU-CLEAs) have great potential in the elimination of urethane (ethyl carbamate) from Chinese rice wine. Process flow diagram of PRU-CLEAs applied in membrane reactor, overview |
| 3.5.1.81 | N-Acyl-D-amino-acid deacylase |
industry |
industrial applications of D-amino acids, produced by several different enzymes on different pathways, including the N-acyl-D-amino acid amidohydrolase, are in the pharmaceutical industry for antibiotics production or as medicine, or in food industry for food sweeteners, or in cosmetics in skin protection products |
| 3.5.1.93 | glutaryl-7-aminocephalosporanic-acid acylase |
industry |
great potential for industrial application of the lysis genes-assisted cell disruption |
| 3.5.1.93 | glutaryl-7-aminocephalosporanic-acid acylase |
industry |
the huge production of engineered GLA produced in Escherichia coli under optimized conditions makes this enzyme an economic tool to be used in bioconversion processes at the industrial level, e.g., in 7-ACA production |
| 3.5.1.93 | glutaryl-7-aminocephalosporanic-acid acylase |
industry |
cephalosporin C acylase (CCA), a proton-forming enzyme, is an important industrial enzyme that can directly catalyze the substrate cephalosporin C (CPC) to 7-aminocephalosporanic acid (7-ACA), which is an intermediate in many types of synthetic cephalosporins. Immobilized CCA on porous carriers is applied in industry for the production of 7-ACA because of its high efficiency and environmentally friendly nature compared with the chemical process and two-step enzymatic process involving two enzymes. Mutational improvement of catalytic efficiency and operational stability |
| 3.5.1.117 | 6-aminohexanoate-oligomer endohydrolase |
industry |
the partial enzymatic hydrolysis of nylon surfaces by NylC can be used to change the smoothness of nylon fibers |
| 3.5.2.2 | dihydropyrimidinase |
industry |
production of optically pure D-amino acids that are key intermediates in the synthesis of commercial products such as beta-lactam semisynthetic antibiotics, peptides, hormones, pyretroids and pesticides |
| 3.5.2.B2 | (+)-gamma-lactamase |
industry |
the enzyme can be a promising candidate of biocatalyst for industrial applications of highly valuable chiral pharmaceutical chemicals |
| 3.5.3.1 | arginase |
food industry |
when milk casein is hydrolyzed at 37°C by using commercial digestive enzymes, pancreatin F and protease A, a significant accumulation of L-ornithine in the hydrolysate and the simultaneous disappearance of L-arginine is noted. Transient but distinct arginase activity, which is sufficiently high for L-ornithine production, is detected in the hydrolysate for a certain period during casein hydrolysis. Findings suggest that an inactive precursor of arginase is contaminated in pancreatin F and is proteolytically activated during the incubation |
| 3.5.3.12 | agmatine deiminase |
food industry |
development of a multiplex PCR method for the simultaneous detection of four genes involved in the production of histamine, i.e. histidine decarboxylase hdc, tyramine, i.e.tyrosine decarboxylase tyrdc, and putrescine, via either ornithine decarboxylase odc, or agmatine deiminase agdi. A collection of 810 lactic acid bacteria strains isolated from wine and cider was screened. The most frequent gene corresponds to the agdi gene detected in 112 strains, 14% of all lactic acid bacteria strains, of 10 different lactic acid bacteria species |
| 3.5.4.2 | adenine deaminase |
food industry |
in beer samples treated with adenine deaminase and guanine deaminase, the adenine concentration in beer drops 66-67% and guanine concentration in beer drops from 68.8 microM to a minimal amount |
| 3.5.4.3 | guanine deaminase |
food industry |
in beer samples treated with adenine deaminase and guanine deaminase, the adenine concentration in beer drops 66-67% and guanine concentration in beer drops from 68.8 microM to a minimal amount |
| 3.5.4.6 | AMP deaminase |
food industry |
noting the use of the enzyme from Aspergillus oryzae in food intended for human consumption and potential presence at trace levels in finished goods, a series of safety studies including an in vitro Ames test and chromosome aberration assay with Chinese hamster lung fibroblasts are conducted along with a 90-day oral toxicity study in rats. AMP deaminase shows no evidence of genotoxicity in the in vitro tests. Following gavage administration of Sprague-Dawley rats at dosages of 19.8, 198.4, or 1984 mg total organic solids (TOS)/kg body weight (bw)/day for 90 days, no adverse effects on body weight gain, food consumption, hematology, clinical chemistry, urinalysis, ophthalmological and histopathological examinations are observed. The no-observed-adverse-effect level is considered to be 1984 mg TOS/kg bw/day, the highest dose tested. Results of the genotoxicity studies and subchronic rat study support the safe use of AMP deaminase produced from Aspergillus oryzae in food production |
| 3.5.4.6 | AMP deaminase |
food industry |
production of 5'-IMP as food additives and pharmaceutical intermediate, important enzyme for the food industry |
| 3.5.5.1 | nitrilase |
industry |
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation |
| 3.5.5.1 | nitrilase |
industry |
spore surface display of nitrilases is an effective approach for enzyme immobilization in biochemical engineering on an industrial scale |
| 3.5.5.1 | nitrilase |
industry |
the high-level production of Arthrobacter aurescens CYC705 nitrilase will meet the need of industrial biosynthesis of iminodiacetic acid |
| 3.5.5.1 | nitrilase |
industry |
the purified enzyme reveales its selectivity towards dinitriles, which suggests a possible industrial application in the synthesis of cyanocarboxylic acids |
| 3.5.5.7 | Aliphatic nitrilase |
industry |
the enzyme is engineered for the commercial production of 3-hydroxyvaleric acid |
| 3.5.5.7 | Aliphatic nitrilase |
industry |
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation |
| 3.5.5.7 | Aliphatic nitrilase |
industry |
the enzyme is a potential candidate for industrial applications for biosynthesis of carboxylic acid |
| 3.5.5.7 | Aliphatic nitrilase |
industry |
the enzyme is a promising biocatalyst for mild nitrile hydrolysis |
| 3.5.5.7 | Aliphatic nitrilase |
industry |
under optimized conditions, using the fed-batch reaction mode, total of 1050 mM 3-cyanopyridine is hydrolyzed completely in 20.8 h with eight substrate feedings, yielding 129.2 g/l production of nicotinic acid and thus showing a potential for industrial application |
