EC Number   |
Recommended Name |
Application |
|---|
    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.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 |
| 3.2.1.11 | dextranase |
food industry |
the use of the dextranase enzyme is the most efficient method for hydrolyzing the dextrans at sugar mills |
| 3.2.1.11 | dextranase |
food industry |
alpha-dextranase removes dextran by 46.6% in mixed sugarcane juice and 14.1% in clarified sugarcane juice |
| 3.2.1.11 | dextranase |
food industry |
the enzyme is used for dextran elimination in sugar production process |
| 3.2.1.15 | endo-polygalacturonase |
food industry |
agro-industrial wastes are suitable for polygalacturonase production |
| 3.2.1.15 | endo-polygalacturonase |
food industry |
high pressure processing can be used for selective inactivation of PG in tomato processing while keeping pectinmethylesterase intact |
| 3.2.1.15 | endo-polygalacturonase |
food industry |
properties of the enzyme may be highly beneficial during fruit processing |
| 3.2.1.15 | endo-polygalacturonase |
food industry |
the enzyme has a considerable potential for commercial application, primarily in the food and animal feedstock industries, due to features such as its optimum activity in acid medium, which remains at a high level at neutral pH, and good pH and temperature stability. The utilization of orange waste in PG production leads to an increase in yield with a reduction in process cost. Moreover, it adds value to the waste from the orange juice industry |
| 3.2.1.15 | endo-polygalacturonase |
food industry |
the polygalacturonase has a remarkable heat-tolerance, which makes it very attractive for industrial applications |
| 3.2.1.15 | endo-polygalacturonase |
food industry |
to preserve or improve rheological properties of tomato based products, the combination of 40°C and 400MPa represents an optimal condition to reduce tomato PG activity while maintaining sufficient pectinmethylesterase activity |
| 3.2.1.15 | endo-polygalacturonase |
food industry |
endo-PG I showed higher efficiency in juice clarification than the pectin lyase alone or the commercial pectinase widely used. Addition of endo-PG I at 3.4 U/ml reduces the intrinsic viscosity of apple juice by 4.5%, and increases the light transmittance by 71.8%. Endo-PG I is an interesting biocatalyst for juice clarification |
| 3.2.1.15 | endo-polygalacturonase |
food industry |
polygalacturonases are pectin substances degrading enzymes, that are widely used in juice and fruit beverages for quality improvement |
| 3.2.1.15 | endo-polygalacturonase |
food industry |
the enzyme improves the elimination of coffee mucilage |
| 3.2.1.15 | endo-polygalacturonase |
food industry |
the enzyme is used for guava juice extraction and clarification. The recovery of juice of enzymatically treated pulp increases from 6% to 23%. Addition of purified enzyme increases the%T650 from 2.5 to 20.4 and °Brix from 1.9 to 4.8. The pH of the enzyme treated juice decreases from 4.5 to 3.02 |
| 3.2.1.15 | endo-polygalacturonase |
food industry |
the enzyme reduces the viscosity of papaya juice by 17.6% and increases its transmittance by 59.1%. Its favourable enzymatic properties make the enzyme attractive for potential applications in the juice industry |
| 3.2.1.15 | endo-polygalacturonase |
food industry |
the enzyme is able to enhance the clarification of citrus juice |
| 3.2.1.15 | endo-polygalacturonase |
food industry |
the enzyme is used for grape juice clarification |
| 3.2.1.15 | endo-polygalacturonase |
food industry |
the enzyme is used for juice clarification of pear, banana and citrus |
| 3.2.1.15 | endo-polygalacturonase |
food industry |
the enzyme significantly reduces the viscosities and improves the yields of fruit juices from banana, plantain, papaya, pitaya and mango |
| 3.2.1.15 | endo-polygalacturonase |
food industry |
the enzyme significantly reduces the viscosity and increases the light transmittance of papaya pulp, and increases the recovery of the papaya extraction |
| 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 |
| 3.2.1.21 | beta-glucosidase |
food industry |
beta-glucosidases play an important role in the flavor formation of fruits, wine and sweet potato by the production of monoterpene alcohols such as linalool, alpha-terpeneol, citronellol, nerol, and geranol, supplementation with beta-glucosidases from external sources may enhance aroma release thus benefiting the winemaking process |
| 3.2.1.21 | beta-glucosidase |
food industry |
the enzyme is used for fermentation of Sicilian table olives |
| 3.2.1.23 | beta-galactosidase |
food industry |
enzyme immobilization onto Amberlite MB-150 beads greatly stabilizes the enzyme preparation, with no loss of activity for 12 months at room temperature. Immobilized enzyme hydrolyzes 64.5% and 69.2% of lactose present in milk and milk whey, respectively, within 10 h at room temperature. Enzyme has a reusability of 10 batchwise uses, with almost no loss in activity |
| 3.2.1.23 | beta-galactosidase |
food industry |
immobilization of recombinant enzyme onto chitosan and use for hydrolyzation of lactose in milk in a packed bed reactor. Immobilized beta-galactosidase is stable at 4°C for six weeks, shows greater relative activity in presence of Ca2+, and hydrolyzes more than 80% of lactose in milk after 2 h of operation in the reactor |
| 3.2.1.23 | beta-galactosidase |
food industry |
the enzyme is used for hydrolysis of lactose extracted from whey or milk |
| 3.2.1.23 | beta-galactosidase |
food industry |
the recombinant thermostable beta-galactosidase may be suitable for the hydrolysis of lactose in milk processing |
| 3.2.1.26 | beta-fructofuranosidase |
food industry |
producing short-chain fructooligosaccarides as functional food ingredients |
| 3.2.1.26 | beta-fructofuranosidase |
food industry |
production of invert sugar |
| 3.2.1.26 | beta-fructofuranosidase |
food industry |
invertase 2 has potential to be applied in food industry since its product, inverted sugar, is used in candies and syrup production, while fructooligosacharides are prebiotics, low calorie and noncariogenic sweeteners |
| 3.2.1.26 | beta-fructofuranosidase |
food industry |
production of invert sugars and prebiotic compounds |
| 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 |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
food industry |
the pretreatment of rice straw with ammonia followed by beta-xylosidase hydrolysis by Weisella cibaria FB069 seems to be a promising method for xylooligosaccharide (prebiotic) production from rice straw |
| 3.2.1.39 | glucan endo-1,3-beta-D-glucosidase |
food industry |
BglS27 is a good candidate for utilization in biotechnological applications such as plant protection, feed, and food preservation |
| 3.2.1.39 | glucan endo-1,3-beta-D-glucosidase |
food industry |
enzyme is able to hydrolyze both polymers, the beta-1,3-glucan from wine-related lactic acid bacterium Pediococcus parvus and that from yeast cell walls, which can make wine filtration difficult or impossible. Enzyme is still active under wine-relevant parameters such as elevated ethanol, sulfite, and phenol concentrations as well as at low pH values. Enzyme seems to be a useful tool to prevent slime production and undesirable yeast growth during vinification |
| 3.2.1.40 | alpha-L-rhamnosidase |
food industry |
alpha-L-rhamnosidase is an important enzyme with applications in the food industries because it can release terminal L-rhamnose residues from various natural products. The D594Q and G827K/D594Q mutant enzymes are more suitable for the industrial processes of isoquercitrin preparation than the wild-type enzyme |
| 3.2.1.40 | alpha-L-rhamnosidase |
food industry |
Aspergillus terreus alpha-L-rhamnosidase specifically hydrolyses the glycosidic linkage of dulcoside A (the bitterest compounds in steviol glycoside mixtures), and converts it to rubusoside. During a 12 h biotransformation, the dulcoside A from crude leaf extracts is completely converted by recombinant alpha-L-rhamnosidase from Aspergillus terreus into rubusoside. This process offers a promising approach for reducing the bitterness of steviol glycoside mixtures |
| 3.2.1.40 | alpha-L-rhamnosidase |
food industry |
efficient and cost-effective enzymatic production method for preparation of the high-valued natural sweetener trilobatin is developed by the combination of hydrogenation and enzymatic hydrolysis reactions with alpha-L-rhamnosidase as the catalyst in aqueous medium. This technology is adopting the cheap and largely available citrus flavanone naringin as the starting material for trilobatin synthesis, and the present enzymatic technology is possibly utilised by commercial for scale-up production. The production is a straightforward two-step process, in which naringin is hydrogenated into naringin dihydrochalcone and followed by removal of the rhamnosyl group of naringin dihydrochalcone by enzymatic hydrolysis using immobilised alpha-L-rhamnosidase as the catalyst. Under optimised conditions, an overall yield of 96% is achieved with a very low loading of alpha-L-rhamnosidase catalyst at 60 °C in a neutral aqueous buffer solution within 2 h. The immobilised alpha-L-rhamnosidase catalyst can be recycled for 10 reactions (90% yield retained) |
| 3.2.1.40 | alpha-L-rhamnosidase |
food industry |
the characteristics (good thermostability, wide range of pH-stability with the optimum pH of 5.0 and temperature of 60°C, not greatly affected by representative metal ions, excellent tolerance abilities against glucose and ethanol) of the enzyme suggest that it should be considered a potential new biocatalyst for food and drug industrial applications |
| 3.2.1.40 | alpha-L-rhamnosidase |
food industry |
the enzyme can efficiently remove naringin from pomelo juice without changing its aroma. It is desirable for debittering citrus juice thereby improving the quality of juice |
| 3.2.1.40 | alpha-L-rhamnosidase |
food industry |
the enzyme can remove the bitter taste of naringin from citrus juices. Improvement of thermostabilty can promote the practical value of the enzyme in citrus juice processing |
| 3.2.1.40 | alpha-L-rhamnosidase |
food industry |
the enzyme exhibits transglycosylating activity, which can synthesise rhamnosyl mannitol through the reactions of transglycosylation with inexpensive rhamnose as the glycosyl donor. The enzyme has potential value for glycoside synthesis in the food industry |
| 3.2.1.40 | alpha-L-rhamnosidase |
food industry |
the enzyme is used to enhance wine aromas or to debitter citrus juices by releasing L-rhamnose |
| 3.2.1.40 | alpha-L-rhamnosidase |
food industry |
the purified enzyme has potential for enhancement of wine aroma |
| 3.2.1.40 | alpha-L-rhamnosidase |
food industry |
with the enhanced thermostability, the mutant enzyme, K406R/K573R, has potentially broadened the applications of alpha-L-rhamnosidase in food processing industry |
| 3.2.1.41 | pullulanase |
food industry |
debranching of guar galactomannan by pullulanase as an alternative and inexpensive route to produce modified guar galactomannan with enhanced functional properties |
| 3.2.1.41 | pullulanase |
food industry |
maltotriose syrup preparation from pullulan using pullulanase, overview. In a batch system, pullulanase hydrolyzes 94.25% of purified pullulan and the resultant syrup contains 3.8 mg/ml of maltotriose |
| 3.2.1.41 | pullulanase |
food industry |
break down of starch for the production of high-glucose syrup. The L627R mutant enzyme may be suitable for industrial application because its shortened reaction time translates to reduced energy consumption |
| 3.2.1.41 | pullulanase |
food industry |
the enzyme can be used directly for maize starch saccharification without adjusting the pH, which reduces cost and improves efficiency |
| 3.2.1.41 | pullulanase |
food industry |
useful in starch industries. The addition of the enzyme in gelatinized rice and maize starches significantly increases the resistant starch type 3 yields (RS3). RS3 is of great importance for nutritionists and food industry, due to its reduced levels of plasma glucose and insulin, increased faecal bulk, and short-chain fatty acid production through fermentation in the large intestine |
| 3.2.1.51 | alpha-L-fucosidase |
food industry |
the enzyme catalyse the transglycosylation reaction leading to production of fucosylated human milk oligosaccharides |
| 3.2.1.52 | beta-N-acetylhexosaminidase |
food industry |
silencing of alpha-mannosidase and beta-D-N-acetylhexosaminidase enhances fruit shelf life due to the reduced degradation of N-glycoproteins which result in delayed softening |
| 3.2.1.54 | cyclomaltodextrinase |
food industry |
the extremely thermostable enzyme might be of potential value in the production of isomaltooligosaccharides in the food industry |
| 3.2.1.55 | non-reducing end alpha-L-arabinofuranosidase |
food industry |
clarification of fruit juices for wine industry |
| 3.2.1.58 | glucan 1,3-beta-glucosidase |
food industry |
use of enzyme as antifungal agent against green and blue mold diseases, in citrus fruits. All tested isolates of Penicillium digitatum and Penicillium italicum are susceptible to panomycocin in vitro. Effective panomycocin concentrations for 50% growth inhibition for Penicillium digitatum and Penicillium italicum are 2 and 1 microg/ml, respectively. In tests on fruit, panomycocin at concentrations equal to the concentration required for complete inhibition in vitro protects lemon fruit from decay |
| 3.2.1.58 | glucan 1,3-beta-glucosidase |
food industry |
Exg2 is active under typical wine-related conditions, such as low pH (3.54.0), high sugar concentrations (up to 20% w/v), high ethanol concentrations (1015% v/v), presence of sulfites (up to 2 mM) and various cations and may have multiple uses in wine making |
| 3.2.1.60 | glucan 1,4-alpha-maltotetraohydrolase |
food industry |
utilization of a maltotetraose-producing amylase as a whole wheat bread improver of the baking performance of whole-grain wheat flour, overview. Whole-grain bread dough prepared with the enzyme shows reduced water absorption and increased development time, while the dough stability is not affected. Also, the enzyme-treated samples exhibit lower Mixolab torque values than the control upon heating and cooling. The viscous characteristics of whole-grain bread dough become dominant with increasing levels of the enzyme. The enzyme delays the crumb firming of whole-grain wheat bread during a 7-d storage period and can function as an antiretrogradation agent to enhance the quality attributes of whole-grain wheat bread |
| 3.2.1.65 | levanase |
food industry |
the enzyme is used for enzymatic analysis of levan produced by lactic acid bacteria in fermented doughs |
| 3.2.1.67 | galacturonan 1,4-alpha-galacturonidase |
food industry |
properties of PGI may be suitable for food processing |
| 3.2.1.67 | galacturonan 1,4-alpha-galacturonidase |
food industry |
polygalacturonases are widely used in the food industry for juice extraction and clarification |
| 3.2.1.67 | galacturonan 1,4-alpha-galacturonidase |
food industry |
exo-polygalacturonase has a wide range of applications in food processing, i.e. juice extraction, clarification of wine, bakery and distillery industries |
| 3.2.1.67 | galacturonan 1,4-alpha-galacturonidase |
food industry |
the enzyme is used for guava juice extraction and clarification. The recovery of juice of enzymatically treated pulp increases from 6% to 23%. Addition of purified enzyme increases the%T650 from 2.5 to 20.4 and °Brix from 1.9 to 4.8. The pH of the enzyme treated juice decreases from 4.5 to 3.02 |
| 3.2.1.67 | galacturonan 1,4-alpha-galacturonidase |
food industry |
the enzyme is applied in the juice clarification of tangerine, orange, grapefruit, and apple |
| 3.2.1.67 | galacturonan 1,4-alpha-galacturonidase |
food industry |
the enzyme is suitable for clarification of orange juice |
| 3.2.1.67 | galacturonan 1,4-alpha-galacturonidase |
food industry |
the enzyme may be used for clarification of different fruit juices |
| 3.2.1.68 | isoamylase |
food industry |
saccharification potential of isoamylases is employed in food industry for preparation of high glucose syrup, maltose, maltitol, trehalose, cyclodextrin and resistant starch from starch |
| 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 |
| 3.2.1.78 | 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 |
| 3.2.1.80 | 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 |
