EC Number   |
Recommended Name |
Application  |
|---|
    2.4.1.18 | 1,4-alpha-glucan branching enzyme |
food industry |
enzyme treatment reduces the rate of starch retrogradation |
| 2.4.1.19 | cyclomaltodextrin glucanotransferase |
food industry |
the enzyme can be used in the bread-baking process since its addition in the dough mix improved significantly the loaf volume and decreased the firmness of bread during storage |
| 2.4.1.19 | cyclomaltodextrin glucanotransferase |
food industry |
the enzyme improves the sweetness and edulcorant quality of stevioside |
| 2.4.1.19 | cyclomaltodextrin glucanotransferase |
food industry |
the enzyme leads to an improvement in the technological quality of gluten-free laminated baked products |
| 2.4.1.19 | cyclomaltodextrin glucanotransferase |
food industry |
cyclodextrins are frequently utilized chemical substances in the food, pharmaceutical, cosmetics, and chemical industries. An enzymatic process for cyclodextrin production is developed by utilizing sucrose as raw material instead of corn starch. Cyclodextrin glucanotransferase from Paenibacillus macerans is applied to produce the cyclodextrins from linear alpha-(1,4)-glucans, which are obtained by Neisseria polysaccharea amylosucrase treatment on sucrose. The greatest cyclodextrin yield (21.1%, w/w) is achieved from a one-pot dual enzyme reaction at 40°C for 24 h. The maximum level of cyclodextrin production (15.1 mg/ml) is achieved with 0.5 M sucrose in a simultaneous mode of dual enzyme reaction, whereas the reaction with 0.1 M sucrose is the most efficient with regard to conversion yield. Dual enzyme synthesis of cyclodextrins is successfully carried out with no need of starch material. Efficient bioconversion process that does not require the high temperature necessary for starch liquefaction by thermostable alpha-amylase in conventional industrial processing |
| 2.4.1.21 | starch synthase (glycosyl-transferring) |
food industry |
resistant starch (RS) has the potential to protect against diabetes and reduce the incidence of diarrhea, inflammatory bowel disease, colon cancer, and chronic renal and hepatic diseases. Soluble starch synthase SSIIIa has a critical role in synthesizing resistant starch in rice |
| 2.4.1.25 | 4-alpha-glucanotransferase |
food industry |
thermostable 4-alpha-glucanotransferase from Thermus scotoductus is used for rice cake production |
| 2.4.1.25 | 4-alpha-glucanotransferase |
food industry |
TmalphaGT can be used to produce granular corn starch, which contains amylose and amylopectin having lower molecular weights and a thermoreversible gelation property |
| 2.4.1.25 | 4-alpha-glucanotransferase |
food industry |
the disproportionating enzyme 4alphaGTase, is used to modify the structural properties of rice starch to produce a suitable fat substitute in reduced-fat mayonnaise. The mayonnaise fat is partially substituted with the 4alphaGTase-treated starch paste at levels up to 50% in combination with xanthan gum. All mayonnaises exhibit shear thinning behavior and yield stress. Viscoelastic properties of mayonnaise are altered, and the mayonnaises exhibited weak gel-like properties. The magnitude of elastic and loss moduli is also affected by 4alphaGTase-treated starch concentration and presence of xanthan gum, microstructure, method, overview |
| 2.4.1.B34 | 4,6-alpha-glucanotransferase |
food industry |
during the process of cooking wheat, semicrystallized chains of raw starch are hydrated into an amorphous form. After they have cooled for a sufficiently long period, linear molecules, amylose, and linear parts of amylopectin molecules expel water and rearrange into a more crystalline structure. This recrystallization, called retrogradation, often leads to the formation of hard and digestive enzyme-inaccessible textures in some wheat-based foods, resulting in poor sensory quality, short shelf life, and low consumer acceptance. After the GtfB-modified wheat starches are gelatinized and stored at 4°C for 1-2 weeks, their endothermic enthalpies are significantly lower than that of the control sample, indicating low retrogradation rates |
| 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 |
| 2.4.1.236 | flavanone 7-O-glucoside 2''-O-beta-L-rhamnosyltransferase |
food industry |
the study provides the basis for potentially improving the taste in citrus fruit through manipulation of the network by knocking-out 1,2-rhamnosyltransferase or by enhancing the expression of flavonoid-7-O-di-glucosyltransferases using genetic transformation |
| 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 |
| 2.5.1.29 | geranylgeranyl diphosphate synthase |
food industry |
the enzyme in Xanthophyllomyces is used for production of astaxanthin, i.e. 3,3'-hydroxy-4,4'-diketo-beta-carotene, which is an industrially important carotenoid used for feeding salmon or trout in farming |
| 2.5.1.32 | 15-cis-phytoene synthase |
food industry |
developement nutritional plants enriched with carotenoids |
| 2.5.1.62 | chlorophyll synthase |
food industry |
changes of chlorophyll and its derivatives in postharvest tea leaves under different low-temperature treatments. At the initial stage of withering, a significant increase is observed in the chlorophyll content, expression of chlorophyll-synthesis-related enzymes and chlorophyll synthase activity in newly picked tea leaves. CHLG expression exhibits a steady decrease during the withering process. An obvious decrease is found in the content of L-glutamate as the foremost precursor substance of chlorophyll synthesis |
| 2.6.1.B3 | aminopentol:pyruvate aminotransferase FumI |
food industry |
enzymatic detoxification of fumonisins in animal feed and potentially also in foodstuffs intended for human consumption, improvement of food and feed safety |
| 2.7.2.4 | aspartate kinase |
food industry |
L-lysine, one of the essential amino acids required for nutrition in animals and humans, is widely used in the food industry, medical industry, etc. L-lysine has been mainly produced by microbial fermentation employing mutant strains of bacteria. An L-lysine high-yielding strain is developed by modification of aspartokinase III and dihydrodipicolinate synthetase |
| 2.7.4.33 | AMP-polyphosphate phosphotransferase |
food industry |
AMP is known to have potential for use as a reliable indicator in hygiene monitoring, the development of a sensitive method for detecting AMP, by using polyphosphate-AMP phosphotransferase and adenylate kinase in conjugation with firefly luciferase, is useful to detect food samples with high sensitivity |
| 2.7.8.8 | CDP-diacylglycerol-serine O-phosphatidyltransferase |
food industry |
phospholipids, especially phosphatidylserine, have many applications in functional food and pharmaceutical industries |
| 2.7.9.4 | alpha-glucan, water dikinase |
food industry |
rice starch contains only low concentrations of starch bound phosphate monoesters, which limits its usage in various industrial processes. Six stable individual transgenic lines with hyper-phosphorylated starch are produced by the overexpression of the StGWD1 in rice (Oryza sativa japonica cv. Zhonghua 11). The transgenic lines have 9fold and double higher Glc-6-P and Glc-3-P, respectively and increased amylose content. The starch granules display only minor morphological alterations, notably the presence of surface pores and moderately distorted edges and surfaces. The novel starch introduces unique combinations of functionality for rice starch, such as reduced gelatinization temperature, decreased pasting viscosity, increased gel formation capacity and increased gel hardness |
| 3.1.1.3 | triacylglycerol lipase |
food industry |
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats |
| 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 |
| 3.1.1.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 |
| 3.1.1.11 | 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 |
| 3.1.1.20 | tannase |
food industry |
the enzyme could be used in the food processing industry |
| 3.1.1.20 | tannase |
food industry |
the enzyme could find potential use in the food-processing industry |
| 3.1.1.20 | tannase |
food industry |
the enzyme is a food processing enzyme used in food, brewing, and feed industry |
| 3.1.1.20 | tannase |
food industry |
the enzyme is found to be useful in the manufacture of instant tea, acron wine, coffee-flavoured soft drinks, clarification of beer and fruit juices |
| 3.1.1.20 | tannase |
food industry |
the enzyme is useful in the food-processing industry |
| 3.1.1.20 | tannase |
food industry |
fruit juice debittering |
| 3.1.1.20 | tannase |
food industry |
the enzyme is used in food and beverage processing, and some of the major commercial applications are the preparation of instant tea, acorn liquor and production of gallic acid |
| 3.1.1.20 | tannase |
food industry |
the use of Lactobacillus plantarum tannase is an adequate alternative to the fungal tannases currently used in the food industry. Use of tannase may provide an efficient means for obtaining molecules with valuable activities from the degradation of complex tannins present in food and agricultural wastes |
| 3.1.1.20 | tannase |
food industry |
tannase is a potential agent for the manufacture of instant tea (tea cream solubilisation) |
| 3.1.1.20 | tannase |
food industry |
the enzyme is used in the manufacture of instant tea, beer, fruit juices, some wines and gallic acid |
| 3.1.1.20 | tannase |
food industry |
tannin acyl hydrolase catalyzes the hydrolysis of hydrolyzable tannins. It is used in the manufacture of instant tea and in the production of gallic acid |
| 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 |
| 3.1.1.42 | chlorogenate hydrolase |
food industry |
the treatment of the wheat dough with the recombinant enzyme causes a softening. The enzyme does not increase the specific bread volume, but improves dough handling. The enzyme may be effective to improve the taste and digestibility of coffee beverages |
| 3.1.1.73 | feruloyl esterase |
food industry |
Aspergillus awamori is applicable to food production and Awamori production. |
| 3.1.1.73 | feruloyl esterase |
food industry |
ferulic acid released from plant cell wall by the action of FAEs is an effective natural antioxidant with potential applications in the pharmaceutical and food industries |
| 3.1.1.73 | feruloyl esterase |
food industry |
industrial production of ferulic acid for use in the food industry |
| 3.1.1.73 | feruloyl esterase |
food industry |
release of phenolic acids |
| 3.1.1.73 | feruloyl esterase |
food industry |
The production of low-cost cell-wall-deconstructing enzymes on agro-industrial by-products could lead to the production of low-cost enzymes for use in the valorisation of food processing wastes. |
| 3.1.1.73 | feruloyl esterase |
food industry |
the enzyme shows stable activity at pH 3 and 50°C, thus the enzyme is acid tolerant, but not heat tolerant, making this enzyme useful for food production |
| 3.1.1.73 | feruloyl esterase |
food industry |
potential for the application of Aspergillus tubingensis enzyme extract in coffee processing. Crude enzyme extracts, containing feruloyl esterase and polygalacturonase, removes the mucilage of coffee cherries within 3 h, which is substantially more efficient than traditional fermentation, the viscosity of coffee mucilage is reduced to 80% by a 3-h treatment with the crudeenzyme extract at 50°C. Total chlorogenic acid in the green beans decreases to 67.3%, while a decline of only 14.3% is observed in the traditionally fermented group. On the other hand, chlorogenic acid lactones in the roasted beans are reduced to 63.9%, and a 37.2% decline in the chlorogenic acid content is detected |
| 3.1.1.81 | quorum-quenching N-acyl-homoserine lactonase |
food industry |
infectious diseases caused by Aeromonas hydrophila is the major problem in aquaculture production. Effects of dietary Lactobacillus plantarum or/and N-acylated homoserine lactonase (AHL lactonase) on controlling Aeromonas hydrophila infection in juvenile hybrid tilapia. Dietary Lactobacillus plantarum or/and AHL lactonase reduce the extent of intestine damage, to a level similar as control fed fish (tilapia), not exposed to Aeromonas hydrophila |
| 3.1.1.87 | fumonisin B1 esterase |
food industry |
enzymatic detoxification of fumonisins in animal feed and potentially also in foodstuffs intended for human consumption, improvement of food and feed safety |
| 3.1.1.87 | fumonisin B1 esterase |
food industry |
feed additive combining two specific biotransformation processes is able to partially or totally neutralize the toxic effects induced by deoxynivalenol and fumonsins |
| 3.1.1.88 | pyrethroid hydrolase |
food industry |
high potential for bioremediation of pyrethroid-contaminated vegetables |
| 3.1.1.112 | isoamyl acetate esteras |
food industry |
balance of enzyme activities of alcohol acetyltransferase AATFase and isoamyl acetate esterase Iah1 is important for optimum production of isoamyl acetate in sake brewing. The amount of isoamyl acetate in the sake increases with an increasing ratio of AATFase/Iah1 esterase activity |
| 3.1.3.1 | alkaline phosphatase |
food industry |
quantification of alkaline phosphatase by using a monoclonal antibody-based immunoassay immunoassay is appropriate for determining mild time/temperature treatment of milk and for the control of milk pasteurization |
| 3.1.3.1 | alkaline phosphatase |
food industry |
marker for milk pasteurization |
| 3.1.3.8 | 3-phytase |
food industry |
Pediococcus pentosaceus strains KTU05-9 and KTU05-8 are recommended to use as a starter for sourdough preparation for increasing of mineral bioavailability from wholemeal wheat bread |
| 3.1.3.8 | 3-phytase |
food industry |
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes |
| 3.1.3.8 | 3-phytase |
food industry |
the enzyme can be applied in dephytinizing animal feeds, and the baking industry. Effect of phytase supplementation in different doses on bread characteristics, overview |
| 3.1.3.8 | 3-phytase |
food industry |
the phytase from Wickerhamomyces anomalus has adequate thermostability for its applicability as a food and feed additive, applicability of recombinant PPHY in dephytinization of wheat bread, overview |
| 3.1.3.8 | 3-phytase |
food industry |
the recombinant enzyme rSt-Phy is useful in dephytinization of tandoori and naan (unleavened flat Indian breads), and bread, liberating soluble inorganic phosphate that mitigates anti-nutrient effects of phytic acid |
| 3.1.3.26 | 4-phytase |
food industry |
Pediococcus pentosaceus strains KTU05-9 and KTU05-8 are recommended to use as a starter for sourdough preparation for increasing of mineral bioavailability from wholemeal wheat bread |
| 3.1.3.26 | 4-phytase |
food industry |
the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes |
| 3.1.3.26 | 4-phytase |
food industry |
the enzyme can be applied in dephytinizing animal feeds, and the baking industry. Effect of phytase supplementation in different doses on bread characteristics, overview |
| 3.1.4.3 | phospholipase C |
food industry |
the enzyme is used in vegetable oil refining by enzymatic phospholipid removal (degumming ) |
| 3.1.4.11 | phosphoinositide phospholipase C |
food industry |
the enzyme is used in industrial soybean oil degumming |
| 3.2.1.1 | alpha-amylase |
food industry |
starch has a protective effect on thermal stability of honey amylase. Therefore, it might be critical to process or control the amylase in honey before incorporation into starch-containing foods to aid in the preservation of starch functionality |
| 3.2.1.1 | alpha-amylase |
food industry |
the maltooligosaccharide forming endo-alpha-amylase is useful in bread making as an antistaling agent and it can be produced economically using low-cost sugarcane bagasse |
| 3.2.1.1 | alpha-amylase |
food industry |
important industrial enzyme in brewing and alcohol production |
| 3.2.1.3 | glucan 1,4-alpha-glucosidase |
food industry |
key enzyme in ripening and production of good taste in fermented tofu production, overview |
| 3.2.1.3 | glucan 1,4-alpha-glucosidase |
food industry |
ethanol production, production of sugars |
| 3.2.1.3 | glucan 1,4-alpha-glucosidase |
food industry |
glucoamylase is an important group of enzymes in starch processing in the food industries, as it is used for the production of glucose and fructose syrup from liquefied starch |
| 3.2.1.3 | glucan 1,4-alpha-glucosidase |
food industry |
the enzyme performs highly efficient hydrolysis of raw starches and direct conversion of raw corn and cassava flours via simultaneous saccharification and fermentation to ethanol suggesting that the enzyme has a number of potential applications in industrial starch processing and starch-based ethanol production. Effective hydrolysis of raw starch flour by the recombinant rPoGA15A preparation and alpha-amylase |
| 3.2.1.4 | cellulase |
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 enzymaticpreparations 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 |
| 3.2.1.4 | cellulase |
food industry |
the capacity of Cel8A to cleave 1,3-1,4-beta-glucans is significantly affected by the presence of the barley-based feed for broilers. Exogenous 1,3-1,4-beta-glucanases (EC 3.2.1.73) but not 1,4-beta-glucanases 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 |
| 3.2.1.6 | endo-1,3(4)-beta-glucanase |
food industry |
construction of a transgenic yeast, Saccharomyces cerevisiae, expressing the enzyme, results in a food-grade yeast that has the potential to improve the brewing properties of beer |
| 3.2.1.6 | endo-1,3(4)-beta-glucanase |
food industry |
application in malting and brewing industry. Under simulated mashing conditions, addition of Agl9A at 20 U/ml or a commercial xylanase at 200 U/ml reduce the filtration rate by 26.71% and 20.21%, respectively, and viscosity by 6.12% and 4.78%, respectively. Combined use of Agl9A at 10 U/ml and the xylanase at 100 U/ml even more effectively reduces the filtration rate by 31.73% and viscosity by 8.79% |
| 3.2.1.6 | endo-1,3(4)-beta-glucanase |
food industry |
the enzyme reduces viscosity of mash during brewing peocesses |
| 3.2.1.7 | inulinase |
food industry |
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps |
| 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 |
