EC Number   |
Recommended Name |
Application  |
|---|
   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 |
| 3.2.1.108 | lactase |
food industry |
the enzyme is used for the production of dairy products |
 3.2.1.116 | glucan 1,4-alpha-maltotriohydrolase |
food industry |
formation of type III resistant starch is affected by branch chain lengths, especially medium-length chains (DP 30-130), and it can be improved when hydrolysis by glucan 1,4 alpha-maltotriohydrolase precedes debranching. Type III resistant starch (RS3) is of particular interest as a food ingredient, because of its nutritional functionality and thermal stability in most normal cooking operations |
| 3.2.1.116 | glucan 1,4-alpha-maltotriohydrolase |
food industry |
the enzyme may be effective in retarding starch retrogradation in baked products |
| 3.2.1.118 | prunasin beta-glucosidase |
food industry |
beta-glucosidase as a tool in marker-assisted selection against bitter almonds |
| 3.2.1.131 | xylan alpha-1,2-glucuronosidase |
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 are co-produced in Escherichia coli through dual-promoter and bicistronic constructs |
| 3.2.1.132 | chitosanase |
food industry |
has potential in the production of functional foods |
| 3.2.1.132 | chitosanase |
food industry |
usage of strain TKU011 on the microbial reclamation of food processing wastes such as shrimp shell wastes for the production of chitosanase |
| 3.2.1.132 | chitosanase |
food industry |
seafood processing industries use chitosanase for bioconversion/valorisation of marine crustacean biomaterials |
| 3.2.1.132 | chitosanase |
food industry |
chitosanase from Paenibacillus mucilaginosus TKU032 may have potential applications in production of bioactive chitosan oligosaccharides for the food and pharmaceutical industries |
| 3.2.1.132 | chitosanase |
food industry |
partially acetylated chitosan oligosaccharides have various potential applications in agriculture, biomedicine, and pharmaceutics due to their suitable bioactivities. A more promising approach is enzymatic depolymerization of chitosan using chitinases or chitosanases, as the substrate specificity of the enzyme determines the composition of the oligomeric products |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
food industry |
Novamyl is currently used in the baking industry as an anti-staling agent in breads at neutral or near neutral pH. It is rapidly inactivated during the baking process. Relative to the Novamyl wild-type the variants exhibit more than 10°C increase in thermal stability at pH 4.5, improving the anti-staling effect |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
food industry |
impact on crumb texture, and amylopectin recrystallization: reduction of bread firmness increase during storage compared to control or other amylases, bread firmness is slightly increased at day 0, firmness at day 6 is 9.00, 7.15, and 4.40 N (compared to 16.85 N in control) for BStA dosages of 5.05, 10.1, and 20.2 enzyme units/g flour, respectively, though highest dosage leads to sticky dough and low resilience. Enzyme unit = amount of enzyme releasing 1 micromol maltose/minute at 40°C, pH 6.0, 100 mM sodium maleate buffer with 5.0 mM CaCl2. BStA almost completely suppresses amylopectin recrystallization. Hot water extractable dextrin content is increased largely by BStA |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
food industry |
wild-type enzyme is not thermostable at low pH as encountered in recipes such as sourdough and rye dough, recombined variants increase thermal stability more than 10°C at pH 4.0-4.5, application test is performed with wheat flour dough at pH 5.5-5.9 and sourdough at pH 4.0-4.3 baked at 230°C for 22 min, firmness and elasticity tested at days 1, 3, and 7 after baking and vacuum packing |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
food industry |
the enzyme is used for the production of maltose syrup from starch |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
food industry |
the enzyme is used in baking and brewing industry |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
food industry |
maltogenic amylases are used to decrease the maltotriose content of high maltose syrups. However, due to the interplay between the hydrolysis and transglycosylation activities of maltogenic amylases, the maltotriose contents of these syrups are still greater than that necessary for pure maltose preparation. Mutant enzyme W177S, shows decreased transglycosylation activity and enhanced maltose production. It will deliver performance superior to that of the wild-type under industrial conditions |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
food industry |
potentially applied in bakery industries |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
food industry |
the enzyme has many potential applications in food processing |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
food industry |
transglucosidase (TGAN) in combination with maltogenic alpha-amylase and beta-amylase appears to be advantageous to modulate sweet potato starch properties. The treatment increases the alpha-1, 6 glycosidic linkage ratio and short chain proportions. Decrease in chain length, molecular weight and long chain proportions is noticed. The initial C-type starch polymorphic structure transforms to B-type structure along with decreased crystallinity. Solubility increases substantially with concomitant decrease in viscosity, gelatinization temperature and melting enthalpy. The outcome is believed to open new pathways for regulating the physicochemical properties of sweet potato starch especially by enzyme modification to the design and development of novel sweet potato starch based products |
| 3.2.1.136 | glucuronoarabinoxylan 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 |
| 3.2.1.141 | 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase |
food industry |
trehalose has many potential applications in biotechnology and the food industry due to its protective effect against environmental stress. Raising trehalose productivity can be achieved through homologous overexpression of maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase. Overexpression of the treY gene and the treY/treZ synthetic operon significantly increases maltooligosyltrehalose synthase activity, the rate-limiting step, and improves the specific productivity and the final titer of trehalose. Furthermore, a strong decrease is noted in glycogen accumulation. Expression of galU/treY and galU/treYZ synthetic operons show a partial recovery in the intracellular glycogen levels and a significant improvement in both intra- and extracellular trehalose content |
| 3.2.1.142 | limit dextrinase |
food industry |
the prediction of malt fermentability is achieved by both forward step-wise multi-linear regression and the partial least squares multivariate model development methods. Both methods produce similar identifications of the parameters predicting wort fermentability at similar levels of predictive power. Both models are substantially better at predicting fermentability than the traditional use of diastatic power on its own. Limit dextrinase thermostability is not a substantial predictor of fermentability, presumably due to its negative correlation with total limit dextrinase activity. The application of these insights in the malting and brewing industries is expected to result in substantial improvements in brewing consistency and enable more specific quality targets for barley breeders progeny selection cut-off limits to be more precisely defined |
| 3.2.1.142 | limit dextrinase |
food industry |
limit dextrinase activity is of particular importance for the brewing industry as the branched dextrins produced after the action of alpha-amylase on starch are not fermentable and represent a loss of potential ethanol production |
| 3.2.1.142 | limit dextrinase |
food industry |
limit dextrinase is a unique debranching enzyme involved in starch mobilization of barley grains during malting, and closely related to malt quality |
| 3.2.1.142 | limit dextrinase |
food industry |
the enzyme is important for malting, influence of kilning on the enzyme activity, process optimization overview |
| 3.2.1.142 | limit dextrinase |
food industry |
the enzyme is used in brewing and malting, the enzyme is limited for starch degradation due to its thermolability during kilning at 70°C, overview |
| 3.2.1.168 | hesperidin 6-O-alpha-L-rhamnosyl-beta-D-glucosidase |
food industry |
herperidin occurs in lemons and oranges in high concentrations and contributes to juice clouding. Enzymatic hydrolysis via the diglycosidase is useful to remove the unpleasant taste or for juice clarification, a deglycosylation (hydrolysis and transglycosylation) in a single step |
| 3.2.1.168 | hesperidin 6-O-alpha-L-rhamnosyl-beta-D-glucosidase |
food industry |
potential use of the enzyme for biotechnoligical applications, e.g. in aroma modulation of fermented foods |
| 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 |
| 3.4.14.5 | dipeptidyl-peptidase IV |
food industry |
use of enzyme for degradation of food-derived opiods from milk, soybean, wheat |
| 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) |
| 3.4.15.6 | 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 |
| 3.4.21.4 | trypsin |
food industry |
the enzyme can be used as a possible biotechnological tool in the fish processing and food industries |
| 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 |
| 3.4.21.25 | 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 |
| 3.4.21.62 | 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 |
| 3.4.21.96 | 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 |
| 3.4.21.111 | 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 |
| 3.4.22.1 | 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 |
| 3.4.22.3 | 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 |
| 3.4.22.7 | 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 |
