EC Number   |
Recommended Name  |
Application |
|---|
   1.10.3.2 | laccase |
food industry |
potential for bioconversion of lignin rich agricultural byproducts into animal feed and cellulosic ethanol. The enzyme effectively improves in vitro digestibility of maize straw |
| 3.2.1.108 | lactase |
food industry |
the enzyme is used for the production of dairy 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 |
| 3.4.11.1 | leucyl aminopeptidase |
food industry |
application of recombinant leucine aminopeptidase rLap1 from Aspergillus sojae in debittering |
| 3.2.1.65 | levanase |
food industry |
the enzyme is used for enzymatic analysis of levan produced by lactic acid bacteria in fermented doughs |
| 2.4.1.10 | levansucrase |
food industry |
lactosucrose, a rare trisaccharide formed from sucrose and lactose by enzymatic transglycosylation, is a type of indigestible carbohydrate with a good prebiotic effect. Lactosucrose biosynthesis is efficiently carried out by a purified levansucrase from Leuconostoc mesenteroides B-512 |
| 2.4.1.10 | levansucrase |
food industry |
the enzyme is interesting in food and pharmaceutical industries for synthesis of diverse sucrose analogues, hetero-oligosaccharides (especially lactosucrose), and interesting fructosides from a wide range of substrates, i.e. monosaccharides, disaccharides, and aromatic and alkyl alcohols |
| 3.2.1.73 | licheninase |
food industry |
the enzyme is a good candidate in the malting and brewing industry reducing the filtration time and viscosity of mash from barley grains, overview |
| 3.2.1.73 | licheninase |
food industry |
the enzyme is considered as a candidate for application particularly in the animal feed industry |
| 3.2.1.73 | licheninase |
food industry |
the secretively produced beta-1,3-1,4-glucanase shows excellent thermostability up to 80°C and a wide pH range from pH 4 to pH 11 and has a potential in the food and animal feed applications |
| 3.2.1.73 | licheninase |
food industry |
the thermostable enzyme can be useful in mashing at 72°C of brewing processes |
| 3.2.1.73 | licheninase |
food industry |
enzyme can promote mashing with a reduced filtration time (14.0%) and viscosity (3.4%) |
| 3.2.1.73 | licheninase |
food industry |
exogenous 1,3-1,4-beta-glucanases but not 1,4-beta-glucanases (EC 3.2.1.4) are obligatory enzymes to improve the nutritive value of barley-based diets for broilers. Enzyme is completely resistant to proteolytic inactivation after a 30 min incubation with pancreatic proteases |
| 3.2.1.73 | licheninase |
food industry |
the addition of mutant K20S/N31c/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P in congress mashing decreases the filtration time and viscosity by 21.3 and 9.6 %, respectively |
| 3.2.1.73 | licheninase |
food industry |
the enzyme is used for production and processing of alcoholic beverages |
| 3.2.1.73 | licheninase |
food industry |
the enzyme is used for production of oligomers as prebiotics |
| 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 |
| 2.4.1.210 | limonoid glucosyltransferase |
food industry |
Limonoid glucosyltransferase is an enzyme that catalyzes the conversion of bitter limonoid into non-bitter limonoid glucoside while retaining the health benefit of limonoids in the juice. The immobilization of this enzyme in a column can solve the juice bitterness problem |
| 2.4.1.210 | limonoid glucosyltransferase |
food industry |
Citxadrus limonoid glucosyltransferase which is a key playxader for natural debitterness and anticancerous potenxadtial, can be utilized for metabolic engineering of Citxadrus limonoids to get rid of delayed bitterness problem along with enhanced limonoid glucoside molecules. The presence or absence of LGT can serve as a molecxadular indicator for determining the level of accumulaxadtion of limonoid glucoside and may reflect ultimately the possibility of delayed bitterness in available Citrus germplasm. Enhanced activity of LGT in citrus fruits may increase the glucoside level, which in turn will reduce the bitterness problem |
| 2.4.1.210 | limonoid glucosyltransferase |
food industry |
major problem in the orange industry is delayed bitterness, which is caused by limonin, a bitter compound developing from its non-bitter precursor limonoate A-ring lactone (LARL) during and after extraction of orange juice. The glucosidation of LARL by limonoid UDP-glucosyltransferase (LGT) to form non-bitter glycosyl-limonin during orange maturation has been demonstrated as a natural way to debitter by preventing the formation of limonin. Enzyme LGT activity can be used to develop biotechnology-based approaches for producing orange juice from varietals that traditionally have a delayed bitterness |
| 2.4.1.210 | limonoid glucosyltransferase |
food industry |
overexpression of the LGT gene can reduce the delayed bitterness problem in citrus juice |
| 1.13.11.12 | linoleate 13S-lipoxygenase |
food industry |
lipoxygenase is widely used in food industry to improve aroma, rheological, or baking properties of foods |
| 1.13.11.12 | linoleate 13S-lipoxygenase |
food industry |
addition of LOX1 and LOX2 altered the elasticity as well as viscosity of dough prepared from bleached wheat flour, LOX improves the dough rheology |
| 3.4.24.75 | lysostaphin |
food industry |
antistaphylococcal agent |
| 3.2.1.17 | lysozyme |
food industry |
the LD50 value of lysozyme is 4530 mg/kg body weight. 90 days of marine low-temperature lysozyme treatment at three doses shows no significant difference on blood biochemistry and organ index in drug treatment groups compared to saline treatment group. Marine low-temperature lysozyme can be safely used at the dose of experiment applied in food industry and further clinical studies |
| 3.2.1.17 | lysozyme |
food industry |
dry-heated hen egg white lysozyme simultaneously exhibits enhanced foaming properties and aggregation capacity. It may self-associate at the air/water interface, stabilizing air bubbles |
| 3.2.1.17 | lysozyme |
food industry |
due to increasing demands for natural food preservatives, lysozyme is increasingly important in food processing |
| 3.2.1.17 | lysozyme |
food industry |
possible use of lysozyme as an anti-microbial agent during the winemaking process, the enzyme is covalently immobilized on two different micro-size magnetic particles, the tosyl-activated particles are more stable, overview. The insoluble lysozyme provides advantages over the soluble form, such as enabling reutilization of enzyme and an increase in stability, immobilization may impart stable antimicrobial capability to the surface of food packaging polymers and create a more suitable microenvironment for the enzyme. Treated food can be claimed additive-free following removal of immobilized lysozyme |
| 3.2.1.17 | lysozyme |
food industry |
potential for the use of immobilized lysozyme as an antimicrobial component for antimicrobial packaging |
| 3.2.1.17 | lysozyme |
food industry |
the enzyme is used as antimicrobial substance or indicator in fish, meat, dairy, fruits, vegetables and wines or serving as the active component integrated into food packaging systems as well as other active functions in the food matrix |
| 4.1.1.101 | malolactic enzyme |
food industry |
cell surface display of malolactic enzyme on the cell surface of Sacchaormyces cerevisiae to conduct malolactic fermentation in wine. The malolactic activity of the genetically engineered yeast strain can turn 21.11% L-malate into lactic acid after 12 h reaction with L-malate |
| 4.1.1.101 | malolactic enzyme |
food industry |
expression of malolactic enzyme from Oenococcus oeni in the host strain Lactobacillus plantarum WCFS1. Under conditions with L-malic acid as the only energy source and in presence of Mn2+ and NAD+, the recombinant Lactobacillus plantarum and the wild-type strain convert 85% (2.5 g/l) and 51% (1.5 g/l), respectively, of L-malic acid in 3.5 days. The recombinant Lactobacillus plantarum cells convert in a modified wine 15% (0.4 g/l) of initial L-malic acid concentration in 2 days |
| 4.1.1.101 | malolactic enzyme |
food industry |
the bacterial mleS gene introduced into yeast Sacchaormyces cereuisiae induces transformation of L-malate in L-lactate. In spite of a high in vitro malolactic specific activity, malate degradation via malolactic enzyme is very low |
 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 |
| 3.2.1.78 | 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 |
| 3.2.1.96 | mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase |
food industry |
the enzyme can be used in dairy industry to efficiently release N-glycans from milk proteins |
| 4.2.2.3 | mannuronate-specific alginate lyase |
food industry |
the KJ-2 polyMG-specific alginate lyase can be used in combination with other alginate lyases for a synergistic saccharification of alginate |
| 2.4.1.242 | NDP-glucose-starch glucosyltransferase |
food industry |
because waxy wheat starch has greater water absorbance and resistance to retrogradation than normal starch, its inclusion in flour blends has been suggested as a means of improving the texture and appearance of bakery products and noodles. The results indicate that wheat encoding functional homeologs of GBSS1 produces starch that has potential in the production of certain food items, such as Asian noodles |
| 3.2.1.55 | non-reducing end alpha-L-arabinofuranosidase |
food industry |
clarification of fruit juices for wine industry |
| 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 |
| 4.1.1.17 | ornithine decarboxylase |
food industry |
the enzyme is used in the wine making process |
| 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 |
| 3.7.1.1 | oxaloacetase |
food industry |
oxalate toxicity is a concern for the commercial application of fungi in the food and drug industries |
| 3.1.1.B10 | p-coumaroyl esterase |
food industry |
the enzyme is used to decrease 5-O-chlorogenic acid content in coffee powder. As chlorogenic acids are suspected to cause stomach irritating effects in sensitive people, the enzyme treatment offers a technically feasible approach to improve the quality of coffee beverages by reducing 5-O-chlorogenic acid concentration without significantly affecting the aroma and taste profile |
| 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 |
| 4.2.2.2 | pectate lyase |
food industry |
effects of pectate lyase-silencing in tissue integrity increases the content of large particles in juice, its viscoelastic properties being modified and its viscosity increased |
| 4.2.2.2 | pectate lyase |
food industry |
firmness of full ripen strawberry fruits from Pel lines is significantly higher than control fruits, while color and soluble solids are not affected. The increase of firmness in Pel lines is maintained when ripe fruits are stored for 3 days at 25°C |
| 4.2.2.2 | pectate lyase |
food industry |
inhibition of the pectate lyase gene improves postharvest behavior of strawberries |
| 4.2.2.10 | pectin lyase |
food industry |
enzyme is used for maceration and clarification in the process of fruit juice production. The recombinant strain 105 has a high potential to produce pectin lyase for application in industrial processes, such as textile and plant fiber processing, coffee and tea fermentation, oil extraction, industrial wastewater treatment, and paper making. It offers the advantage of producing great amounts of PL using sugar cane juice as the sole carbon source, which would lower production costs |
| 4.2.2.10 | pectin lyase |
food industry |
homogeneous pectin lyase from Penicillium canescens exhibits the ability to clarify apple juice. Efficient treatment of juice requires 0.2 mg of homogeneous enzyme |
| 4.2.2.10 | pectin lyase |
food industry |
successfully applied to production and clarification of juice |
| 4.2.2.10 | pectin lyase |
food industry |
commercial pectic enzyme plays an important role in the process of winemaking for extraction, clarification, and filtration of fruit juice and wine puree to increase the yield and quality, such as pigment, flavor, transmittance, and viscosity |
| 4.2.2.10 | pectin lyase |
food industry |
used for apple juice clarification |
| 4.2.2.10 | pectin lyase |
food industry |
application for clarification of fruit juice. For apple, orange, pomegranate juices treated with the partially purified enzyme, the clarity values are 219.74, 206.38 and 203.48%, respectively |
| 4.2.2.10 | pectin lyase |
food industry |
pectin lyase PNL-ZJ5A can effectively decrease the viscosity and improve the yield of apple juice and light transmittance |
| 3.1.1.11 | pectinesterase |
food industry |
added as exogenous enzyme in fruit and vegetable processing, used to increase the yield during extraction, to clarify and concentrate fruit juices, for gelation of fruit, and to modify texture and rheology of fruit and vegetable based products |
| 3.1.1.11 | pectinesterase |
food industry |
destabilizes pectinaceous materials in fruit juices and concentrates and modifies the texture of fruit and vegetable products |
| 3.1.1.11 | pectinesterase |
food industry |
enzyme is known to be responsible for cloud loss in juice processing and storage |
| 3.1.1.11 | pectinesterase |
food industry |
one of the most important enzymes in the industrialization and preservation of fruits, juices or other industrial products that involve the presence or absence of intact pectin |
| 3.1.1.11 | pectinesterase |
food industry |
responsible for phase separation and cloud loss in fruit juice manufacturing |
| 3.1.1.11 | pectinesterase |
food industry |
used for juice clarification and gelation of frozen concentrates, destabilizing agent for pectin material in fruit juices and concentrates |
| 3.1.1.11 | pectinesterase |
food industry |
used for various applications in fruit processing e.g. texture improvement of fruit pieces, juice extraction, concentration and clarification of fruit juices |
| 3.1.1.11 | pectinesterase |
food industry |
PME has a higher thermal resistance than the bacteria and yeasts existing in orange juice, therefore its inactivation is used as a parameter to define the time/temperature combination of the thermal process of pasteurisation of orange juice, which is necessary to prevent spoilage, overview |
| 3.1.1.11 | pectinesterase |
food industry |
inhibition of pectin methylesterase directly after juice extraction is crucial in the production of storable citrus juice products |
| 3.1.1.11 | pectinesterase |
food industry |
PME (0.12% (v/v)) and Ca2+ (0.5% (w/w)) in osmotic sugar solutions positively affect the relative hardness of dehydrated strawberry fruits, which is ascribed to the effect of PME and Ca2+ on the cell wall strength of the tissue (no cell wall damage and tissue particle alterations are observed upon dehydration) |
| 3.1.1.11 | pectinesterase |
food industry |
exogenous pectin methylesterase is applied in texture engineering of thermally processed intact fruits and vegetables, for example, via enzyme infusion |
| 3.1.1.11 | pectinesterase |
food industry |
pectin methylesterase can positively or negatively affect structural quality of plant-based foods (cloud stability, viscosity, texture) |
| 3.1.1.11 | pectinesterase |
food industry |
total pectin methylesterase activity is an indicator of freshness that is universally applicable to Citrus juices derived from orange, mandarin, and lemon or blends thereof |
| 3.1.1.11 | pectinesterase |
food industry |
due to very high de-esterification activity, easy denaturation and significant efficacy in incrementing clarification of fruit juice makes the enzyme useful for industrial application |
| 3.1.1.11 | pectinesterase |
food industry |
the enzyme enhances the pectin degradation process in apple juice clarification |
| 3.1.1.11 | pectinesterase |
food industry |
pectin methylesterase (PME) is a ubiquitous cell wall enzyme, which de-esterifies and modifies pectins for food applications. The papaya PME can be potentially utilized to modify pectin functionality at elevated temperature |
| 3.1.1.11 | pectinesterase |
food industry |
the enzyme is suitable for both acidic and alkaline processing, such as coffee and tea fermentation |
| 3.1.1.11 | pectinesterase |
food industry |
study of kinetic characterization, thermal stability and synergistic effect of temperature and pH for peroxidase (POD) and pectin methylesterase (PME) in tomato puree. Inactivation of both enzymes is very important, since these enzymes can have very negative effects on the color, odor, flavor and texture of juices and vegetable beverages during storage. The browning and loss of stability in juices and vegetable beverages, such as tomato puree, can be controlled by applying temperature and pH combinations capable of inactivating these enzymes in a total or partial way, but while respecting the limits organoleptic and legal for juices and vegetable beverages |
| 3.4.23.20 | Penicillopepsin |
food industry |
the enzyme is used in the dairy industry such as in accelerated cheese ripening |
| 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 |
| 1.11.1.7 | peroxidase |
food industry |
preservation of raw milk, yoghurt, and cheese |
| 1.11.1.7 | peroxidase |
food industry |
study of kinetic characterization, thermal stability and synergistic effect of temperature and pH for peroxidase (POD) and pectin methylesterase (PME) in tomato puree. Inactivation of both enzymes is very important, since these enzymes can have very negative effects on the color, odor, flavor and texture of juices and vegetable beverages during storage. The browning and loss of stability in juices and vegetable beverages, such as tomato puree, can be controlled by applying temperature and pH combinations capable of inactivating these enzymes in a total or partial way, but while respecting the limits organoleptic and legal for juices and vegetable beverages |
| 4.3.1.24 | phenylalanine ammonia-lyase |
food industry |
the enzyme can be used for the development of dietary foods and biotechnological products for patients with phenylketonuria |
| 4.3.1.24 | phenylalanine ammonia-lyase |
food industry |
the enzyme from Cyathobasis fruticulosa is a potential candidate for serial production of dietary food and biotechnological products |
| 4.3.1.25 | phenylalanine/tyrosine ammonia-lyase |
food industry |
the enzyme is a useful biocatalyst for removal of L-phenylalanine from protein hydrolysates, which can be evaluated as potential ingredients in foodstuffs for phenylketonuria patients. The enzyme is also capable to catalyze the deamination of L-tyrosine to p-coumaric acid but at a substantially low reaction rate. Therefore, the final content of L-Tyr in samples treated with L-phenylalanine ammonia-lyase should be analyzed in each case and taken in consideration to avoid its deficiency in phenylketonuria patients |
| 5.4.2.2 | phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) |
food industry |
the enzyme is involved in production of sphingans, extracellular polysaccharides used as thickeners, emulsifiers and gelling agents, its overexpression increases the sphingan production of the transformed cell |
| 3.1.4.11 | phosphoinositide phospholipase C |
food industry |
the enzyme is used in industrial soybean oil degumming |
| 3.1.1.32 | phospholipase A1 |
food industry |
the enzyme improves foaming stability and properties of skim milk and whey, implying that phospholipases can be useful tools for modifying the functionality of dairy products and ingredients |
| 3.1.1.4 | phospholipase A2 |
food industry |
PLA2 stability in the presence of organic solvents, as well as in acidic and alkaline pH and at high temperature makes it a good candidate for its application in food industry |
| 3.1.4.3 | phospholipase C |
food industry |
the enzyme is used in vegetable oil refining by enzymatic phospholipid removal (degumming ) |
| 5.4.2.8 | phosphomannomutase |
food industry |
the enzyme is involved in production of sphingans, extracellular polysaccharides used as thickeners, emulsifiers and gelling agents, its overexpression increases the sphingan production of the transformed cell |
| 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 |
| 3.4.21.7 | 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 |
