EC Number   |
Recommended Name  |
Application |
|---|
   3.2.1.73 | licheninase |
food industry |
the enzyme is used for production of oligomers as prebiotics |
| 3.2.1.78 | mannan endo-1,4-beta-mannosidase |
food industry |
the enzyme is involved in the degradation of plant cell wall, resulting in an increase in feed conversion efficiency of animal feed and improvement in the growth performance of broilers. The enzyme can also be used for hydrolyzing galactomannans present in coffee extract to inhibit gel formation during freezed-drying of the instant coffee |
| 3.2.1.78 | mannan endo-1,4-beta-mannosidase |
food industry |
the enzyme is used for clarification of fruit juices such as grape, peach, orange and pomegranate juices |
| 3.2.1.78 | mannan endo-1,4-beta-mannosidase |
food industry |
the purified enzyme can be used in clarifying kiwi juice |
| 3.2.1.78 | mannan endo-1,4-beta-mannosidase |
food industry |
the purified enzyme is used to clarify some fruit juices like orange, grape fruit and apple juices |
 3.2.1.8 | endo-1,4-beta-xylanase |
food industry |
changes in arabinoxylan during the breadmaking process are to a large extent caused by endogenous endoxylanases, whereas the contribution of microbial endoxylanases to these changes are very low. Endogenous endoxylanases affect the arabinoxylan population only during the fermentation phase and not during the mixing phase of breadmaking. Endoxylanases can, on the one hand, positively affect bread volume by solubilization of water unextractable arabinoxylan, but they can, on the other hand, also lead to unwanted stickiness |
| 3.2.1.8 | endo-1,4-beta-xylanase |
food industry |
contribution of microbial endoxylanases to changes in arabinoxylan during the breadmaking process are very low. Microbial endoxylanases end up in flour as contaminant and affect its functional properties |
| 3.2.1.8 | endo-1,4-beta-xylanase |
food industry |
high levels of endoxylanase activity in wheat flour should be avoided as they can cause uncontrolled degradation of arabinoxylan during bread dough processing, glutenstarch separation, or refrigerated dough storage |
| 3.2.1.8 | endo-1,4-beta-xylanase |
food industry |
improvement of cereal-based industrial processing by endoxylanase enzymes insensitive towards inhibitors |
| 3.2.1.8 | endo-1,4-beta-xylanase |
food industry |
wheat flour-associated endoxylanases are not active during dough mixing but exert their main effect during the fermentation phase of bread making. Wheat flour-associated endoxylanases can alter part of the arabinoxylan in dough, thereby changing their functionality in bread making and potentially affecting dough and end product properties |
| 3.2.1.8 | endo-1,4-beta-xylanase |
food industry |
endogenous endoxylanase activity during fermentation and storing can have negative effects on dough, the enzyme effect depends on the wheat variety's enzyme content and inhibitor content |
| 3.2.1.8 | endo-1,4-beta-xylanase |
food industry |
extraction of pectins from apple pomace with monoactive preparation of endoxylanase and endocellulase. Endoxylanase application results in the highest extraction efficiency of pectins (19.8%). The obtained polymer was characterised by a very high molecular mass, high level of neutral sugars (mainly arabinose, galactose and glucose), and very high degree of pectin methylation (73.4). The simultaneous application of both enzymatic preparations results in their cooperation, leading to a decrease of both the extraction efficiency and the molecular mass of pectin. This pectin is distinguished by the highest GalA (74.7%) and rhamnose contents |
| 3.2.1.8 | endo-1,4-beta-xylanase |
food industry |
extraction of pectins from apple pomace with monoactive preparation of endoxylanase and endcellulase. Pectin extracted with endocellulase has 1.5fold lower molecular mass but contains significantly more galacturonic acid (70.5%) of a high degree of methylation (66.3%). The simultaneous application of both enzymatic preparations results in their cooperation, leading to a decrease of both the extraction efficiency and the molecular mass of pectin. This pectin displays the highest galacturonic acid (74.7%) and rhamnose contents |
| 3.2.1.8 | endo-1,4-beta-xylanase |
food industry |
use of enzyme as an additive in the bread making process leads to a decrease in firmness, stiffness and consistency, and improvements in specific volume and reducing sugar content |
| 3.2.1.8 | endo-1,4-beta-xylanase |
food industry |
application of the extremely thermo- and alkali-stable enzyme for preparation of prebiotic xylooligosaccharides |
| 3.2.1.8 | endo-1,4-beta-xylanase |
food industry |
fruit juice clarification potential of GC25 xylanase at mild conditions. Pediococcus acidilactici strain GC25 xylanase causes a high increase in reducing sugar content after 30 min incubation at 40°C |
| 3.2.1.8 | endo-1,4-beta-xylanase |
food industry |
the ability of the enzym to produce xylobiose from agricultural and forestry residues proves that it is an excellent candidate enzyme in prebiotic and alternative sweetener industries |
| 3.2.1.8 | endo-1,4-beta-xylanase |
food industry |
the enzyme is important for industrial applications such as pretreatment of poultry cereals, bio-bleaching of wood pulp and degradation of plant biomass |
| 3.2.1.8 | endo-1,4-beta-xylanase |
food industry |
xylooligosaccharide derived from enzymatic hydrolysis of biopolymers is of considerable importance in preparing nutritional health oligosaccharides useful in food and pharmaceutical industries. To create added value products from hardwood xylan, xylanase (XynB) and alpha-glucuronidase (AguA) from Thermotoga maritima were co-produced in Escherichia coli through dual-promoter and bicistronic constructs |
| 3.2.1.80 | fructan beta-fructosidase |
food industry |
a typical solution product consists of a mixture of fructose (155 g/l), glucose (155 g/l), sucrose (132 g/l) and fructooligosaccharides (50 g/l). The concentrations are suitable for applications in most food industries, in products such as sweets, candies, chocolates and yogurts. Besides, the prebiotic function of fructooligosaccharides as stimulants of the beneficial intestinal flora will give the product a functional and differentiated feature |
| 3.2.1.80 | fructan beta-fructosidase |
food industry |
diabetics |
| 3.2.1.80 | fructan beta-fructosidase |
food industry |
production of fuel ethanol and ultra-high fructose syrup |
| 3.2.1.82 | exo-poly-alpha-digalacturonosidase |
food industry |
properties of PGI may be suitable for food processing |
| 3.2.1.96 | mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase |
food industry |
the enzyme can be used in dairy industry to efficiently release N-glycans from milk proteins |
| 3.2.1.98 | glucan 1,4-alpha-maltohexaosidase |
food industry |
production of maltohexaose with low sweetness, low viscosity, and high efficiency for the uptake of energy by humans |
| 3.2.1.98 | glucan 1,4-alpha-maltohexaosidase |
food industry |
the enzyme can be applied to manufacture high maltose syrup |
| 3.2.1.98 | glucan 1,4-alpha-maltohexaosidase |
food industry |
the enzyme preparation is effective in removing starch based stains |
| 3.2.1.B26 | Sulfolobus solfataricus beta-glycosidase |
food industry |
the enzyme suitable for hydrolysis of lactose at temperatures at 70-80°C |
| 3.2.1.B26 | Sulfolobus solfataricus beta-glycosidase |
food industry |
the immobilized enzyme is useful for the hydrolysis of lactose in whey or milk by using a packed-bed enzyme reactor operated at 70°C |
| 3.2.1.B28 | Pyrococcus furiosus beta-glycosidase |
food industry |
the hyperthermostable beta-glycosidase may be useful for food and pharmaceutical applications |
| 3.2.1.B28 | Pyrococcus furiosus beta-glycosidase |
food industry |
the enzyme suitable for hydrolysis of lactose at temperatures at 70-80°C |
| 3.2.1.B28 | Pyrococcus furiosus beta-glycosidase |
food industry |
the immobilized enzyme is useful for the hydrolysis of lactose in whey or milk by using a packed-bed enzyme reactor operated at 70°C |
| 3.2.1.B33 | Sulfolobus shibatae beta-glycosidase |
food industry |
processing of lactose-containing products |
| 3.2.1.B8 | malto-alpha-amylase (reducing end) |
food industry |
the enzyme might be of potential value in the food and starch industries due to its extreme thermostability |
| 3.4.11.1 | leucyl aminopeptidase |
food industry |
application of recombinant leucine aminopeptidase rLap1 from Aspergillus sojae in debittering |
| 3.4.11.5 | prolyl aminopeptidase |
food industry |
Aspergillus oryzae enzyme PAP together with alkaline protease and leucine aminopeptidase is used to hydrolyze rice protein. The amount of hydrophobic amino acids is significantly increased, which contributes to a reduction in the bitterness |
| 3.4.11.9 | Xaa-Pro aminopeptidase |
food industry |
PepX aminopeptidase from Streptococcus thermophilus ACA DC 0022 is used in Greek Feta cheese manufacturing |
| 3.4.13.9 | Xaa-Pro dipeptidase |
food industry |
prolidase can be used in dietary industry as bitterness reducing agent |
| 3.4.13.9 | Xaa-Pro dipeptidase |
food industry |
prolidases are employed in the cheese-ripening process to improve cheese taste and texture |
| 3.4.14.11 | Xaa-Pro dipeptidyl-peptidase |
food industry |
X-prolyl dipeptidyl aminopeptidase PepX, EC 3.4.14.11, and the general aminopeptidase N, EC 3.4.11.2, exhibit a clear synergistic effect in casein hydrolysis studies. Here, the relative degree of hydrolysis is increased by approx. 132% |
| 3.4.14.11 | Xaa-Pro dipeptidyl-peptidase |
food industry |
activation of the enzyme is observed after processing at 100-200 MPa and 20-30°C. More intense processing conditions lead to enzyme inactivation. Pressures up to 200 MPa result in a structurally molten globule-like state where PepX maintains its secondary structure but the tertiary structure is substantially affected and enzyme activity increased. Both secondary and tertiary structures are affected severely by higher pressures (450 MPa), which reduce enzyme activity |
| 3.4.14.11 | Xaa-Pro dipeptidyl-peptidase |
food industry |
during casein hydrolysis, the sequential application of PepX or PepN after prehydrolysis with Alcalase results in an relative degree of hydrolysis (rDH) increase of 1.12- or 2.00fold, respectively, compared to only using Alcalase. The simultaneous application of Alcalase, PepX and PepN from the beginning shows similar results as the sequential application, but only three remaining peptides are observed and the hydrolysis time is reduced from 16 h (sequential approach) to 6.5 h (simultaneous approach) |
| 3.4.14.11 | Xaa-Pro dipeptidyl-peptidase |
food industry |
immobilization of enzyme as cross-linked enzyme aggregate CLEA results in 66% residual activity at 50°C after 4 d (compared to 50% for the free enzyme), and the optimum temperature increases from 30°C for wild-type to 40°C for PepN-CLEAs. With combined CLEAs of PepX/PepN the highest activity yield is about 18% and 9% for PepX and PepN activity, respectively. The combined CLEAs are suitable for application in protein hydrolysis. The relative degree of hydrolysis is increased by approximately 52% compared to an alcalase pre-hydrolyzed casein solution |
| 3.4.14.11 | Xaa-Pro dipeptidyl-peptidase |
food industry |
production, characterization and use of cross-linked enzyme aggregates (CLEAs) from a fusion protein of PepN and PepX (FUS-PepN_PepX CLEA). The FUS-PepN_PepX CLEAs produced have activity for both specific enzymes. pH and temperature optima, environmental conditions show that the CLEAs are suitable for application in a complex matrix, such as food protein hydrolysates. The relative degree of hydrolysis of a prehydrolyzed casein solution is increased by 100% and the hydrolysate obtained shows a strong antioxidative capacity (ABTS-IC50 value: 7.85 microg/ml) |
| 3.4.14.5 | dipeptidyl-peptidase IV |
food industry |
use of enzyme for degradation of food-derived opiods from milk, soybean, wheat |
| 3.4.15.6 | cyanophycinase |
food industry |
the production of beta-dipeptides from cyanophycin by cyanophycinase is economically important, because di- and tripeptides are more efficiently utilized than intact proteins or free amino acids, have a greater nutritional value, and are better absorbed |
| 3.4.17.1 | carboxypeptidase A |
food industry |
Brassica carinata protein hydrolysates could be used for developing functional foods for the treatment of heart and related diseases |
| 3.4.17.1 | carboxypeptidase A |
food industry |
hydrolyzates could be used for preparing special diets when there is a need to increase the supply of branched amino acids and/or reduce the intake of aromatic amino acids |
| 3.4.17.1 | carboxypeptidase A |
food industry |
the application of the novel ochratoxin A hydrolytic enzyme to reduce the ochratoxin A contents on some food or feed products is under evaluation |
| 3.4.17.1 | carboxypeptidase A |
food industry |
application of enzyme to wheat flour contaminated by ochratoxin A leads to 16.8-78.5% reduction of ochratoxin A and production of ochratoxin alpha |
| 3.4.21.111 | aqualysin 1 |
food industry |
presence of aqualysin 1 in bread dough has no impact on the specific bread volume and only limited impact on hardness, cohesiveness, springiness, resilience and chewiness, but impacts bread crumb coherence. Aualysin in dough is inhibited by wheat endogenous serine peptidase inhibitors during dough mixing and fermentation and starts hydrolyzing gluten proteins during baking above 80°C |
| 3.4.21.111 | aqualysin 1 |
food industry |
the level of protein extractable in sodium dodecyl sulfate containing medium under non-reducing conditions from wheat dough decreases upon heating to a lesser extent when aqualysin is used than in control experiments. The higher level is caused by the release by Aq1 of peptides from the repetitive gluten protein domains during baking. The resultant thermoset gluten network in bread crumb is mainly made up by protein from non-repetitive gluten domains |
| 3.4.21.25 | cucumisin |
food industry |
the high milk-clotting ability of religiosin C supports its use in the food industry |
| 3.4.21.25 | cucumisin |
food industry |
milk-clotting enzyme for cheese-making |
| 3.4.21.26 | prolyl oligopeptidase |
food industry |
the enzyme can be used during mashing to produce gluten free beer |
| 3.4.21.4 | trypsin |
food industry |
the enzyme can be used as a possible biotechnological tool in the fish processing and food industries |
| 3.4.21.62 | Subtilisin |
food industry |
alcalase-hydrolyzed potato protein has both antioxidant and emulsifying properties which may be of potential use in meat emulsion manufacturing |
| 3.4.21.63 | Oryzin |
food industry |
the enzyme is efficient in producing antihypertensive peptide IPP from beta-casein and a potential debittering agent. The high degree of hydrolysis of the enzyme to soybean protein (8.8%) and peanut protein (11.1%) compared to papain and alcalase makes it a good candidate in the processing of oil industry byproducts |
| 3.4.21.63 | Oryzin |
food industry |
the salt tolerance of proteases secreted by Aspergillus oryzae 3.042 closely relates to the utilization of raw materials and the quality of soy sauce |
| 3.4.21.7 | plasmin |
food industry |
milk retentate with increased plasmin activity is an interesting starting material for cheese-making. Increased plasmin activity increases cheese flavour and decreases ripening time |
| 3.4.21.7 | plasmin |
food industry |
the enzyme is responsible for spoilage of directly heated ultra-high temperature milk products |
| 3.4.21.96 | Lactocepin |
food industry |
CEP isolated from Mongolian fermented mare's milk strain SBT11087 is distinct from those from previously reported Lactobacillus helveticus strains in terms of its optimal temperature and its degradation of beta-casein |
| 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 |
| 3.4.22.14 | 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 |
| 3.4.22.2 | papain |
food industry |
combination of ultrasound and papain is more beneficial for improving functional properties of meat compared with the individual treatment |
| 3.4.22.3 | 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 |
| 3.4.22.30 | Caricain |
food industry |
the enzyme detoxifies gliadin in wheat dough |
| 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%) |
| 3.4.22.7 | asclepain |
food industry |
asclepain f is less adequate as coagulant in cheesemaking |
| 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.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 |
| 3.4.23.1 | 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 |
| 3.4.23.20 | 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 |
| 3.4.23.4 | 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 |
| 3.4.23.40 | 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 |
