EC Number   |
Recommended Name |
Application |
|---|
    3.2.1.1 | alpha-amylase |
synthesis |
industrial-scale starch liquefaction |
| 3.2.1.1 | alpha-amylase |
synthesis |
oligomer units are an intermediate in the high-fructose syrup production |
| 3.2.1.1 | alpha-amylase |
synthesis |
immobilization of enzyme in calcium alginate beads through entrapment technique. Activity of immobilized enzyme is 81% of free enzyme, its optimum acivity at pH 4.5-6.0 and 40°C, compared to pH 5.5 and 30°C for free enzyme. Immobilized enzyme retains its activity longer than free enzyme |
| 3.2.1.1 | alpha-amylase |
synthesis |
optimization of enzyme production parameters results in growth temperature 70°C, pH 7.75 and 84 h in nutrient medium |
| 3.2.1.1 | alpha-amylase |
synthesis |
use of probiotic Bacillus spores as a matrix for enzyme immobilization by covalent and adsorption methods. The maximum concentration of the alpha-amylase immobilized is 360 microg/1.2 10EE11spores. Maximum activity is achieved at an enzyme concentration of approximately 60 microg/0.4 10EE10 spores, corresponding to an estimated activity of 8000 IU per mg and 1.2 10EE11 spores for covalent immobilization and 85300 IU for the adsorption method. Enzyme immobilization yield is estimated to be 77% and 20.07% for the covalent and adsorption methods, respectively. The alpha-amylase immobilized by both methods, displays improved activity in the basic pH range. The optimum pH for the free enzyme is 5 while it shifts to 8 for the immobilized enzyme. The optimum temperatures for the free and immobilized enzymes are 0C and 0C, respectively. The covalently immobilized alpha-amylase retains 65% of its initial activity, even after 10 times of recycling |
| 3.2.1.B1 | extracellular agarase |
synthesis |
use of enzyme for preparation of neoagarooctaose and neoagarodecaose and separation of neoagaro-oligosaccharides by consecutive column chromatography |
| 3.2.1.3 | glucan 1,4-alpha-glucosidase |
synthesis |
the immobilized enzyme with high operational stability can be used for continuous production of glucose from soluble dextrin |
| 3.2.1.3 | glucan 1,4-alpha-glucosidase |
synthesis |
production of glucose, which is a feed stock for high fructose syrup |
| 3.2.1.3 | glucan 1,4-alpha-glucosidase |
synthesis |
the enzyme of the M115 mutant strain is useful for enhanced ethanol production by Saccharomyces cerevisiae, strain ATTC26602, using raw starch as substrate in solid state fermentation |
| 3.2.1.3 | glucan 1,4-alpha-glucosidase |
synthesis |
entrapment of amyloglucosidase into dipalmitoylphosphatidylcholine multilamellar vesicles and large unilamellar vesicles for biocatalysis inside liposomes and bioanalytical applications, overview |
| 3.2.1.3 | glucan 1,4-alpha-glucosidase |
synthesis |
enzyme immobilization on polyacrylamide gel results in an enzyme with increases thermostability for use in biocatalysis |
| 3.2.1.3 | glucan 1,4-alpha-glucosidase |
synthesis |
glycosylation of the phenolic hydroxyl group of the phenyl propanoid systems, eugenol and curcumin, using an amyloglucosidase from Rhizopus sp. and a beta-glucosidase from sweet almonds together with carbohydrates D-glucose, D-mannose, maltose, sucrose,and D-mannitol in di-isopropyl ether produce glycosides at 7-52% yields in 72 h, method optimization, overview, two compounds are glycosylated in order to enhance their water solubility and pharmacological activities |
| 3.2.1.3 | glucan 1,4-alpha-glucosidase |
synthesis |
preparations of glucoamylase are widely used in many branches of industry for hydrolyzing starch-containing raw materials |
| 3.2.1.3 | glucan 1,4-alpha-glucosidase |
synthesis |
the enzyme is industrially an important biocatalyst that decomposes starch into glucose by tearing-off alpha-1,4-linked glucose residue from the non-reduced end of the polysaccharide chain |
| 3.2.1.3 | glucan 1,4-alpha-glucosidase |
synthesis |
enzyme may be used for raw corn starch hydrolysis and subsequent bioethanol production using Saccharomyces cerevisiae. The yield in terms of grams of ethanol produced per gram of sugar consumed is 0.365 g/g, with 71.6% of theoretical yield from raw corn starch |
| 3.2.1.4 | cellulase |
synthesis |
synthesis of glyceroyl beta-N-acetyllactosaminide and derivatives, that could be used as starting material for the synthesis of neoglycolipid and new kinds of detergents and as acceptors for glycosidase and glycosyltransferase |
| 3.2.1.4 | cellulase |
synthesis |
when the enzyme is used in combination withbeta-glucosidase, cellulose is completely hydrolyzed to glucose at high temperature, suggesting great potential for EGPh in bioethanol industrial applications |
| 3.2.1.4 | cellulase |
synthesis |
glucose production from cellulose material using beta-glucosidase from Pyrococcus furioses and endocellulase from Pyrococcus horikoshii. The combination reaction can produce only glucose without the other oligosaccharides from phosphoric acid swollen Avicel |
| 3.2.1.4 | cellulase |
synthesis |
production of enzyme in parallel-operated shake flasks and, alternatively, in parallel-operated stirred-tank bioreactors on a 10-m. scale. Reaction conditions with 53.3 g/l microcrystalline cellulose in the initial medium, no lactose feeding and 3.3 g/l and day intermittent ammonium sulfate addition are optimal. The optimum substrate supply on a liter-scale results in the production of 4.88 filter paper units of enzyme per ml with after 96 h |
| 3.2.1.4 | cellulase |
synthesis |
use of a cellulase blend to evaluate its application in a simultaneous saccharification and fermentation process for second generation ethanol production from sugar cane bagasse. After enzyme production in a bioreactor and tangential ultrafiltration in hollow fiber membranes, the cellulolytic preparation is stable for at least 300 h at both 37°C and 50°C. The ethanol production is carried out by sugar cane bagasse partially delignified cellulignin fed-batch simultaneous saccharification and fermantation process, using the onsite cellulase blend. The method applied results in 100 g/l ethanol concentration at the end of the process, which corresponds to a fermentation efficiency of 78% of the maximum obtainable theoretically. The experimental results lead to the ratio of 380 l of ethanolper ton of sugar cane bagasse partially delignified cellulignin |
| 3.2.1.4 | cellulase |
synthesis |
40% higher cellulase activity on filter paper in 72 h is observed with the addition of 1 mM of nickel-cobaltite (NiCo2O4) nanoparticles in the growth medium. Maximum production of endoglucanase (211 IU/gds), beta-glucosidase (301 IU/gds), and xylanase (803 IU/gds) is achieved after 72 h without nanoparticles, while in the presence of 1 mM of nanoparticles, endoglucanase, beta-glucosidase, and xylanase activity increase by about 49, 53, and 19.8%, respectively, after 48 h of incubation |
| 3.2.1.4 | cellulase |
synthesis |
a medium based on starch casein minerals containing carboxymethyl cellulose and beef extract supports enhanced cellulase production. Carboxymethyl cellulose, beef extract , NaCl, temperature and pH are significant for cellulase production. Optimization of cellulase production results in an enhancement of endoglucanase activity to 27 IU per ml |
| 3.2.1.4 | cellulase |
synthesis |
expression of enzyme in Escherichia coli and Thermotoga sp. after fusion to the signal peptides of TM1840 (amyA) or TM0070 (xynB). Expressed in Escherichia coli and Thermotoga sp. renders the hosts with increased endo- and exoglucanase activities. In Escherichia coli, the recombinant enzymes are mainly bound to the bacterial cells, whereas in Thermotoga sp., about half of the enzyme activities are observed in the culture supernatants. However, the cellulase activities are lost in Thermotoga sp. after three consecutive transfers |
| 3.2.1.4 | cellulase |
synthesis |
expression of enzyme in Escherichia coli and Thermotoga sp. after fusion to the signal peptides of TM1840 (amyA) or TM0070 (xynB). Expressed in Escherichia coli and Thermotoga sp. renders the hosts with increased endoglucanase activities. In Escherichia coli, the recombinant enzymes are mainly bound to the bacterial cells, whereas in Thermotoga sp., about half of the enzyme activities are observed in the culture supernatants. However, the cellulase activities are lost in Thermotoga sp. after three consecutive transfers |
| 3.2.1.4 | cellulase |
synthesis |
heterologous expression in Bacillus subtilis combined with customized signal peptides for secretion from a random libraries with 173 different signal peptides originating from the Bacillus subtilis genome. The customized signal peptide does not affect enzyme performance when assayed on carboxymethyl cellulose, phosphoric acid swollen cellulose, and microcrystalline cellulose |
| 3.2.1.4 | cellulase |
synthesis |
in regulator cre1-silenced strain C88, the filter paper hydrolyzing activity and beta-1,4-endoglucanase activity are 3.76-, and 1.31fold higher, respectively, than those in the parental strain when the strains are cultured in inducing medium for 6 days. The activities of beta-1,4-exoglucanase and cellobiase are 2.64-, and 5.59fold higher, respectively, than those in the parental strain when the strains are cultured for 5 days |
| 3.2.1.4 | cellulase |
synthesis |
optimization of cultural conditions for enhanced cellulase production. Under solid-state fermentation, yields of carboxymethylcellulase are 463.9 U/g, filter paper cellulase 101.1 U/g and beta-glucosidase 99 U/g |
| 3.2.1.4 | cellulase |
synthesis |
alkali-pretreated roots of Taraxacum kok-saghyz (rubber dandelion), incubated with crude enzyme extracts from Thermomyces lanuginosus STm yield more natural rubber (90 mg/g dry root) than the protocols, Eskew process (24 mg/g) and commercial-enzyme-combination process (45 mg/g). The crude enzyme treatment at 91.6% rubber purity approaches the purity of the commercial-enzyme-combination process at 94.1% purity |
| 3.2.1.4 | cellulase |
synthesis |
scale-up systems for cellulase production and enzymatic hydrolysis of pretreated rice straw at highsolid loadings and by Aspergillus terreus. In a horizontal rotary drum reactor at 50°C with 25 % (w/v) solid loading and 9 FPU/g substrate enzyme load up to 20 % highly concentrated fermentable sugars are obtained at 40 h with an increased saccharification efficiency of 76 % compared to laboratory findings (69.2 %). Nearly 79-84% of the cellulases and more than 90% of the sugars are recovered from the saccharification mixture |
| 3.2.1.4 | cellulase |
synthesis |
under optimised conditions of growth on wheat bran, 420.8 and 22.73 units/g substrate of endo-beta-1,4-glucanase and filter paper cellulase are produced, respectively. Both endo-beta-1,4-glucanase and filter paper activity production show significant dependence on ammonium sulfate concentration and pH |
| 3.2.1.4 | cellulase |
synthesis |
enhanced production of enzyme in Escherichia coli. High-cell-density and optimal CenC expression are obtained in ZYBM9 medium induced either with 0.5 mM IPTG/150 mM lactose, after 6 h induction at 37°C. Before induction, bacterial cells are given heat shock (42°C) for 1 h when culture density (OD600 nm) reached at 0.6. Intracellular enzyme activity is enhanced by 6.67- and 3.20fold in ZYBM9 (yeast extract 0.5% (w/v), NaCl 0.5% (w/v), tryptone 1.0% (w/v), NH4Cl 0.1% (w/v), KH2PO4 0.3% (w/v), Na2HPO4 0.6% (w/v), MgSO4.7H2O 1 mM, and Glucose 0.4% (w/v)) and 3×ZYBM9 medium, respectively, under optimal conditions |
| 3.2.1.4 | cellulase |
synthesis |
the cold active butanol-tolerant endoglucanase is valuable for biobutanol production by a simultaneous saccharification and fermentation process |
| 3.2.1.6 | endo-1,3(4)-beta-glucanase |
synthesis |
the major products of water-soluble beta-glucan hydrolyzed by over-produced endo-beta-(1-3),(1-4)-glucanase are trioligosaccharides and tetrasaccharides, which can be developed as useful products such as antihypercholesterolemic, anti-hypertriglyceridemic, and anti-hyperglycemic agents |
| 3.2.1.7 | inulinase |
synthesis |
high-level expression in Pichia pastoris leads to production of enzyme at 286.8 U/ml and 8873 U/mg |
| 3.2.1.7 | inulinase |
synthesis |
isolation of mutant M-30 with enhanced inulinase production, mutant is stable after cultivation for 20 generations. Inulin, yeast extract, NaCl, temperature, pH for maximum inulinase production by the mutant M-30 are 20.0 g/l, 5.0 g/l, 20.0 g/l, at 28°C and pH 6.5, respectively. Under the optimized conditions, 127.7 U/ml of inulinase activity is reached in the liquid culture |
| 3.2.1.7 | inulinase |
synthesis |
proposed kinetic model for fructose production defined within temperature and substrate concentration ranges of industrial interest such as 40-60°C and 3-60 g/l, respectively. Model is based on a minimum number of parameters. The hypotheses are always specified and assumed only on the basis of convenience and rational consideration. The kinetic model was successfully validated by comparison with a vast set of experimental results |
| 3.2.1.7 | inulinase |
synthesis |
application of a bi-enzymatic system based on the combined use of levansucrase from Bacillus amyloliquefaciens and endo-inulinase from Aspergillus niger in a one-step reaction for the synthesis of fructooligosaccharides and oligolevans using sucrose as the sole substrate. The optimal conditions leading to a high yield of short chain fructooligosaccharides, i.e.1:1 ratio, 0.5 h, 0.6 M, are different from those resulting in a high yield of medium chain fructooligosaccharides and oligolevans, i.e. 1.85:1 ratio, 1.77 h, 0.6 M. The production of fructooligosaccharides and oligolevans at a large scale gives a yield of 57-65%, w/w and produces 65.8-266.8 g/l and h, and uses of low temperature of 35°C and low concentrations of sucrose |
| 3.2.1.7 | inulinase |
synthesis |
gene expression in Pichia pastoris using codon optimization results in the secretion of recombinant endoinulinase activity that reaches 1349 U/ml. Inulooligosaccharides production from inulin using the recombinant enzyme, after 8 h under optimal conditions, which include 400 g/l inulin, an enzyme concentration of 40 U/g substrate, 50°C and pH 6.0gives a yield of 91% |
| 3.2.1.7 | inulinase |
synthesis |
growth of Aspergillus niger AUMC 9375 on the mixture of a 6:1 w/w ratio of sun flower tuber:lettuce roots, yields the highest levels of inulinase at 50% moisture, 30°C, pH 5.0, with seven days of incubation, and with yeast extract as the best nitrogen source. Purified inulinase is successfully immobilized with an immobilization yield of 71.28%. After incubation for 2 h at 60°C, the free enzyme activity decreases markedly to 10%, whereas that of the immobilized form decreases only to 87%. The immobilized inulinase can be used for 10 cycles and in addition, can be stored for 32 days at 4°C |
| 3.2.1.7 | inulinase |
synthesis |
immobilization of endoinulinase results in higher stability than the free endoinulinase under various temperature levels. A residual activity of 81.2% can be still obtained after ten reaction cycles |
| 3.2.1.7 | inulinase |
synthesis |
optimal grwoth conditions for expression of enzyme are 1% inulin,1% yeast extract, and 0.05% KH2PO4. Under optimum conditions, endoinulinase production reaches 28.67 IU/ml and biomass yield 0.162 OD600/15, in excellence correlation with predicted values. Endoinulinase production from a simple and cost-effective medium using raw Dahlia inulin is comparable with pure inulin |
| 3.2.1.7 | inulinase |
synthesis |
endoinulinase is an inulolytic enzyme which is used for the production of fructooligosaccharides from inulin |
| 3.2.1.7 | inulinase |
synthesis |
endoinulinases are an industrial tool critical for the production of inulooligosaccharides (IOS) |
| 3.2.1.7 | inulinase |
synthesis |
enzymatic hydrolyzation of inulin by endo-inulinase to produce oligofructoses, a type of food additive and health product, a promising green and environmentally friendly technique |
| 3.2.1.7 | inulinase |
synthesis |
enzymatic synthesis of fructooligosaccharides (FOS) from sucrose by endo-inulinase-catalyzed transfructosylation reaction in biphasic systems, production of FOS from sucrose by commercial inulinase from Aspergillus niger |
| 3.2.1.7 | inulinase |
synthesis |
inulooligosaccharides (IOS) represent an important class of oligosaccharides at industrial scale. Efficient conversion of inulin to IOS through endoinulinase from Aspergillus niger |
| 3.2.1.8 | endo-1,4-beta-xylanase |
synthesis |
optimum levels of wheat bran (15-20 g/l), lactose (1.0-1.5 g/l), tryptone (2-2.5 g/l) and NaCl (7.0-8.0 g/l) support a 6.75fold increase in xylanase production |
| 3.2.1.8 | endo-1,4-beta-xylanase |
synthesis |
production of enzyme in Pichia pastoris with codon optimization. The activity of dual-copy enzyme is maximized at 15158 U/ml after 120 h of shaking |
| 3.2.1.8 | endo-1,4-beta-xylanase |
synthesis |
yield of enzyme is enhanced more than four fold in the presence of 1% corn husk and 0.5% peptone or feather hydrolysate at pH 11 and 37°C |
| 3.2.1.8 | endo-1,4-beta-xylanase |
synthesis |
recombinant expression of endo-beta-1,4-xylanase in Pichia pastoris. Codon optimization leads to 59% increase in activity. Coexpression of the Vitreoscilla hemoglobin (VHb) gene leads to higher biomass, cell viability, and xylanase activity. The maximum xylanase activity reaches 58792 U/ml when the induction temperature is 22°C |
| 3.2.1.8 | endo-1,4-beta-xylanase |
synthesis |
alkali-pretreated roots of Taraxacum kok-saghyz (rubber dandelion), incubated with crude enzyme extracts from Thermomyces lanuginosus STm yield more natural rubber (90 mg/g dry root) than the protocols, Eskew process (24 mg/g) and commercial-enzyme-combination process (45 mg/g). The crude enzyme treatment at 91.6% rubber purity approaches the purity of the commercial-enzyme-combination process at 94.1% purity |
| 3.2.1.8 | endo-1,4-beta-xylanase |
synthesis |
optimization of recombinant enzyme production in 1-liter flasks. Initial cell density is the most important parameter. Under optimized conditions, 1498 mg xylanase per liter can be achieved |
| 3.2.1.8 | endo-1,4-beta-xylanase |
synthesis |
Bacillus licheniformis strain DM5 is attributed for the production of prebiotic and anti-inflammatory XOS from agrowaste |
| 3.2.1.11 | dextranase |
synthesis |
- |
| 3.2.1.11 | dextranase |
synthesis |
manufacture of dentifrices |
| 3.2.1.11 | dextranase |
synthesis |
application in sugar cane mills |
| 3.2.1.11 | dextranase |
synthesis |
investigation on various adding times of dextranase to the dextransucrase system to reveal the synergistic processes of dextransucrase and dextranase. Dextranase added into the dextransucrase-sucrose system at different times gives rise to different main dextran products. Dextranase added into sucrose system at the same time with dextransucrase synthesizes low molecular weight dextran targeted to 5 kDa, while dextranase added during the reaction process of dextransucrase directionally prepares dextran with medium Mw of 10 kDa and 20 kDa. The synthesized oligodextrans are mainly composed of alpha-1,6-glycosidic linkages and low alpha-1,3-glycosidic branches |
| 3.2.1.11 | dextranase |
synthesis |
maximum enzyme production is obtained in a self designed medium (pH 6.0) containing 1% dextran 5000 Da, after 24 h culture incubation at 37°C.High dextranase production is achieved when medium is supplemented with dextran as only carbon source and no enzyme production is found in medium having glucose, sucrose or starch. Dextranase production is inversely proportional to dextran polymer length and extent of branching |
| 3.2.1.11 | dextranase |
synthesis |
optimal conditions for synthesis of enzyme are 28 h, 8.0, 30°C, and 25% volume of liquid in 100-ml Erlenmeyer flasks, respectively |
| 3.2.1.11 | dextranase |
synthesis |
optimized culture conditions for dextranase productions are 37°C, pH 10, 32 h, and 20% (v/w) moisture content. The addition of 0.175 mM CrCl3 increases the enzyme production by about 4.5fold |
| 3.2.1.11 | dextranase |
synthesis |
immobilization of enzyme in Fe3+-cross-linked alginate/carboxymethyl cellulose beads. The immobilization process improves the optimum temperature from 35°C to 45°C. The immobilized enzyme shows its optimum activity for synthesis of dextran in pH range 4.5-5.4 compared to pH 5.4 in case of free form. The immobilization process improve the thermal and pH enzyme stability to great extent. The enzyme retains 60% activity after 15 batch reactions |
| 3.2.1.11 | dextranase |
synthesis |
alpha-dextranase activity reaches 242.8 U/ml when fermentation conditions are 29°C, pH 6.0 and 220 rpm. Addition of glass beads to fermentation medium after 12 h improves enzyme activity by 135.5% |
| 3.2.1.11 | dextranase |
synthesis |
culturing Chaetomium gracile in medium containing crude dextran and use of high molecular weight of dextrans results in higher dextranase production. Cells incubated in medium containing glucose as sole carbon source exhibit a high growth rate but do not produce dextranase. Using fed-batch and two-step fermentation strategies, production of 159.5 and 187.0 U/ml, respectively, can be achieved |
| 3.2.1.14 | chitinase |
synthesis |
expression of chitinase in Bacillus thuringiensis under the control of a strong promoter and a 5'-mRNA stabilizing sequence leads to markedly elevated chinolytic activity and a diminution of 10-20% in size of the crystals produced. Strains overexpressing chitinase produce fewer viable spores. No change in protease activity is observed depsite teh overproduction of chitinase |
| 3.2.1.14 | chitinase |
synthesis |
recombinant enzyme produced in Escherichia coli can efficiently convert colloidal chitin to N-acetyl glucosamine and chitobiose at pH 4.0, 6.0 and 9.0 at 50°C and retains its activity up to 3 days under these conditions |
| 3.2.1.14 | chitinase |
synthesis |
the thermophilic chitinase may prove useful for industrial applications in chitooligosaccharide production from chitin |
| 3.2.1.17 | lysozyme |
synthesis |
the extracellular pH-sensitive glycosylation system can be used to obtain bioactive and surface functional neoglycoproteins |
| 3.2.1.17 | lysozyme |
synthesis |
production of secreted recombinant human lysozyme by use of overexpression vector pPIC3.5k, carrying the strong promoter AOX1 of aldehyde oxidase 1, the HSA signal peptide, the enterokinase recognition motif, and the lysozyme gene. Mature protein is identical with native human lysozyme. It exhibits in vitro bacteriolytic activity against the Gram-positive bacterium Micrococcus lysodeikticus and the Gram-negative bacterium Escherichia coli |
| 3.2.1.20 | alpha-glucosidase |
synthesis |
the enzyme can be potentially useful for starch hydrolysis as well for the novel synthesis of oligosaccharides in industry |
| 3.2.1.20 | alpha-glucosidase |
synthesis |
glucose production from maltodextrins employing a thermophilic immobilized cell biocatalyst in a packed-bed reactor, biotransformation of a commercial dextrin mixture at industrial concentrations (3040%, w/v) into glucose at 75°C, achieving up to 98% conversion |
| 3.2.1.20 | alpha-glucosidase |
synthesis |
immobilization of enzyme within agar-agar support via entrapment. The maximum immobilization efficiency of 82.77% is achieved using 4.0% agar-agar keeping the diameter of beads up to 3.0 mm. Km value of immobilized enzyme increases from 1.717 to 2.117 mM whereas Vmax decreases from 8,411 to 7,450 U/min as compared to free enzyme. The immobilization significantly increases the stability of maltase against various temperatures and immobilized maltase retains 100% of its original activity after 2 h at 50°C, whereas the free maltase only shows 60% residual activity under the same conditions. Entrapped maltase can be reused for up to 12 cycles and retains 50% of activity even after the 5th cycle. Agar entrapped maltase retains 73% of its initial activity even after 2 months when stored at 30°C |
| 3.2.1.20 | alpha-glucosidase |
synthesis |
the transglycosylation activity of the mutant glycosynthase produced from AglA can be used to synthesize arbutin alpha-glucosides. The glycosynthase reaction is very specific and produces a single transglycosylation compound. Therefore, it can be used to generate regiospecific glycosidic bonds |
| 3.2.1.20 | alpha-glucosidase |
synthesis |
the alpha-transglucosidase-producing Geobacillus stearothermophilus as a potential application technique can be successfully used to prepare industrial isomaltooligosaccharides (IMOs) |
| 3.2.1.21 | beta-glucosidase |
synthesis |
synthesis of glycoconjugates and oligosaccharides |
| 3.2.1.21 | beta-glucosidase |
synthesis |
increased hydrolysis of cellobiose by immobilized enzyme preparation |
| 3.2.1.21 | beta-glucosidase |
synthesis |
co-expression of beta-glucosidase and endoglucanase in Saccharomyces cerevisiae. Ethanol fermentation from 20 g per l barley beta-glucan with the co-displaying strain reaches 7.94 g per l ethanol after 24 h of fermentation. The conversion rate of ethanol is 69.6% of the theoretical ethanol concentration |
| 3.2.1.21 | beta-glucosidase |
synthesis |
construction of a lactic-acid producing Saccharomyces cerevisiae strain expressing isoform Bgl1 on cell surface by fusing the mature protein to the C-terminal half region of alpha-agglutinin. Strain is able to grow on cellobiose and glucose minimal medium at the same rate. The maximum rate of L-lactate production on cellobiose is 2.8 g per l and similar to that on glucose |
| 3.2.1.21 | beta-glucosidase |
synthesis |
enzyme is able to hydrolyze rice straw into simple sugars |
| 3.2.1.21 | beta-glucosidase |
synthesis |
optimization of culture condition for production of beta-glucosidase from Aspergillus niger and subsequent use for hydrolysis of ginsenosides. Presence of wheat bran and KH2PO4 and stirring speed have significant effect on enzyme activity |
| 3.2.1.21 | beta-glucosidase |
synthesis |
use of enzyme for syntheses of pyridoxine glycosides in di-isopropylether. Synthesis of 7-O-(alpha-D-glucopyranosyl)pyridoxine, 7-O-(beta-D-glucopyranosyl)pyridoxine, 6-O-(alpha-D-glucopyranosyl)pyridoxine, 7-O-(alpha-D-galactopyranosyl)pyridoxine, 7-O-(beta-D-galactopyranosyl)pyridoxine, 6-O-(alpha-D-galactopyranosyl)pyridoxine, 7-O-(alpha-D-mannopyranosyl)pyridoxine, 7-O-(beta-D-mannopyranosyl)pyridoxine, 6-O-(alpha-D-mannopyranosyl)pyridoxine in yields ranging from 23% to 40% |
| 3.2.1.21 | beta-glucosidase |
synthesis |
the enzyme is useful in synthetic biology to produce complex bioactive glycosides and to avoid chemical hazards |
| 3.2.1.21 | beta-glucosidase |
synthesis |
glucose production from cellulose material using beta-glucosidase from Pyrococcus furioses and endocellulase from Pyrococcus horikoshii. The combination reaction can produce only glucose without the other oligosaccharides from phosphoric acid swollen Avicel |
| 3.2.1.21 | beta-glucosidase |
synthesis |
preparation of lactose-free pasteurized milk with a recombinant thermostable beta-glucosidase |
| 3.2.1.21 | beta-glucosidase |
synthesis |
immobilization of enzyme on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde. The optimal conditions of immobilized enzyme are the same as that of the free enzyme, the highest activity with cellobiose as the substrate approaches 1.7 U/g. Immobilization improves the thermostability, pH stability and glucose tolerance, the residual activity is 68% of the initial activity at the end of 10 repeated cycles. 2 mM Zn2+ increases the relative activity of the immobilized enzyme to 192% and 199% with cellobiose and 4-nitrophenyl-beta-D-glucopyranoside as substrates, respectively and improves the reusability, high-temperature stability, and glucose tolerance |
| 3.2.1.21 | beta-glucosidase |
synthesis |
optimized medium composition for beta-glucosidase expression is corn cob (51.8 g/l), beef extract (23.8 g/l), salicin (0.5 g/l), MnSO4·H2O (0.363 g/l), MgSO4·7H2O (0.4 g/l), and NaCl (5 g/l). Under the optimal conditions, the activity of beta-glucosidase is up to 4.71 U/ml |
| 3.2.1.21 | beta-glucosidase |
synthesis |
the optimal medium composition for beta-glucosidase production is 2.99% (w/v) bagasse, 0.33% (w/v) yeast extract, 0.38% (w/v) Triton X-100, 0.39% (w/v) NaNO3, and pH 8.0 at 30°C. Large-scale production in 7-l stirred tank bioreactor results in beta-glucosidase production of up to 23.29 IU/g within 80 h of incubation |
| 3.2.1.21 | beta-glucosidase |
synthesis |
the enzyme can constitute a valuable biocatalyst for the synthesis of disaccharides involving beta(1-3) linked disaccharide structures as, for example, Bifidus factors |
| 3.2.1.22 | alpha-galactosidase |
synthesis |
production of extracellular alpha-galactosidase by solid-state fermentation. Soybean flour is the best solid substrate, and packed-bed bioreactors perform well giving a yield of 197 U/gds, with a forced aeration of 2 vvm. Highest yield is obtained after 96 h of incubation |
| 3.2.1.22 | alpha-galactosidase |
synthesis |
the mutant is an efficient alpha-galactosynthase producing different galactosylated disaccharides from beta-galactosyl-azide donors and 4-nitrophenyl-alpha-and beta-glycosides as acceptors |
| 3.2.1.23 | beta-galactosidase |
synthesis |
simple and inexpensive method for synthesizing (2R)-glycerol-O-D-beta-galactopyranoside by utilization of the transgalalactosylating properties of beta-galactosidase and the chloroform solubility of a derivative of (2R)-glycerol-O-D-beta-galactopyranoside that is formed by the transfer of galactose onto isopropylidene glycerol |
| 3.2.1.23 | beta-galactosidase |
synthesis |
enzyme mutant E184A is a valuable catalyst for the synthesis of metabolically stable analogues of the important glycosidic linkages to the 3 and 4 positions of glucosides and galactosides |
| 3.2.1.23 | beta-galactosidase |
synthesis |
expression in Escherichia coli under control of araBD promoter. The addition of D-fucose causes an improvement in specific beta-galactosidase production, although beta-galactosidase is produced as an inclusion body. The addition of D-fucose after induction leads to an increase in the specific activity of beta-galactosidase inclusion bodies and causes a changes in the structure of beta-galactosidase inclusion bodies, with higher enzyme activity |
| 3.2.1.23 | beta-galactosidase |
synthesis |
production of beta-galactosidase by expression of the genes encoding the large and the small subunit in Lactobacillus plantarum WCFS1. Cultivations yield about 23000 U of enzyme per l |
| 3.2.1.23 | beta-galactosidase |
synthesis |
the enzyme catalyzes the production of the synthetic disaccharide lactulose (4-O-beta-D-galactopyranosyl-D-fructose) via a transgalactosylation using lactose as a galactose donor and fructose as an acceptor. Lactulose is used in treatment of hyperammonemia and as a gentle laxative. It is also applied to commercial infant formulas and various milk products because it specifically promotes the intestinal proliferation of Bifidobacterium, which creates an acid medium that inhibits the growth of undesirable bacteria |
| 3.2.1.23 | beta-galactosidase |
synthesis |
the F441Y mutant enzyme has potential application in the industrial preparation of galactooligosaccharides |
| 3.2.1.23 | beta-galactosidase |
synthesis |
immobilization by covalent attachment onto Eupergit C with a binding efficiency of 95%. Immobilization increases both activity and stability at higher pH values and temperature but does not significantly change kinetic parameters for the substrate lactose. The immobilized enzyme shows a strong transgalactosylation reaction, resulting in the formation of galactooligosaccharides. The maximum yield of 34% galactooligosaccharides is obtained when the degree of lactose conversion is roughly 80% |
| 3.2.1.23 | beta-galactosidase |
synthesis |
fermentation parameters for the maximum production of cold active beta-galactosidase are pH 7.3, 82% (v/v) cheese whey, 3.84% tryptone. An overall 3.6fold increase in cold active beta-galactosidase production (34.37 U/ml) is achieved in optimized medium |
| 3.2.1.23 | beta-galactosidase |
synthesis |
immobilization and stabilization of beta-galactosidase on Duolite A568 using a combination of physical adsorption, incubation at pH 9.0 and cross-linking with glutaraldehyde leads to a 44% increase in enzymatic activity as compared with a two-step immobilization process (adsorption and cross-linking). The immobilized enzyme presents a good thermal stability at temperatures around 50°C, and very good pH stability in the range from 1.5 to 9.0 |
| 3.2.1.23 | beta-galactosidase |
synthesis |
immobilization of enzyme on aminovinylsulfone. The enzyme is immobilized at moderate ion strength at pH values from 5.0 to 9.0 via ion exchange on aminovinylsulfone support. 50-80% of the initial activity and a stabilization factor of around 8-15 can be obtained |
| 3.2.1.23 | beta-galactosidase |
synthesis |
immobilization of enzyme on functionalized multi-walled carbon nanotubes. Acid functionalization using H2SO4/HNO3 is the most effivcient method. Enzyme maintains 51% of initial activity after 90 days at 4°C and more than 90% of initial activity up to the 4th recycle |
