EC Number   |
Recommended Name  |
Application |
|---|
    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 |
| 3.2.1.23 | beta-galactosidase |
synthesis |
Optimal extracellular beta-galactosidase activity in recombinant Escherichia coli is observed when induction is initiated when the optical density at 600 nm reaches 40, when expression is induced at 37°C; and lactose is added at a constant feeding rate of 1.0 g/l/h. The extracellular activity reaches 220.0 U/ml, which represents 65.0% of the total beta-galactosidase activity expressed |
| 3.2.1.23 | beta-galactosidase |
synthesis |
synthesis of propyl-beta-galactoside using immobilized beta-galactosidase in glyoxyl-agarose. Reaction yield increases twofold with the glyoxyl-agarose derivative, and after ten sequential batches, the efficiency is 115% higher than obtained with the free enzyme. Enzyme immobilization favors product recovery, and avoids browning reactions. Propyl-beta-galactoside can be recovered with a purity above 99% |
| 3.2.1.26 | beta-fructofuranosidase |
synthesis |
immobilization using anion-exchange resin WA-30 and cross-linking with glutaraldehyde depresses the hydrolysis reaction of isoform F2 |
| 3.2.1.26 | beta-fructofuranosidase |
synthesis |
improved enzyme production by exposure of cells to 0.06 mg/ml N-methyl-N-nitro-N-nitrosoguanidine 0.06 mg/ml for 20 min. The resulting strain NG-5 offers improved extracellular beta-fructofuranidose production of 34 U/ml/min compared to the wild-type strain's 1.15 U/ml/min. A 40fold increase of beta-fructofuranidose activity can be achieved with the process parameters incubation period 48 h, sucrose concentration 5.0 g/l, initial pH of 6.0, inoculum size 2.0% v/v, 16 h old, and urea concentration of 0.2%, w/v |
| 3.2.1.26 | beta-fructofuranosidase |
synthesis |
immobilization by sodium alginate increases enzyme stability |
| 3.2.1.26 | beta-fructofuranosidase |
synthesis |
immobilization of invertase on a hydrogel comprised of methacrylic acid and N-vinyl pyrrolidone and ethyleneglycol dimethacrylate, converted to nanogel by an emulsification method and further functionalized by Curtius azide reaction. The values of Vmax, maximum reaction rate, of 0.123 unit/mg, Michaelis constant of 7.429 mol/L and energy of activation of 3.511 kJ/mol for the immobilized invertase are comparable with those of the free invertase at optimum conditions. The covalent immobilization enhances the pH and thermal stability of invertase |
| 3.2.1.26 | beta-fructofuranosidase |
synthesis |
immobilization of invertase on a porous silicon layer with appropriate catalytic behavior for the sucrose hydrolysis. The procedure is based on support surface chemical oxidation, silanization, activation with glutaraldehyde and finally covalent bonding of the free enzyme to the functionalized surface. Vmax undergoes a substantial increase of about 30% upon immobilization. The value of Km increases by a factor of 1.53 upon immobilization. The initial activity is still preserved up to 28 days while the free enzyme undergoes a 26% loss of activity after the same period |
| 3.2.1.26 | beta-fructofuranosidase |
synthesis |
immobilization of invertase on polyurethane rigid adhesive foam for application in an enzymatic bioreactor. The kinetic parameters are Km 46.5 mM for immobilized invertase versus 61.2 mM for free invertase. The immobilized invertase derivative maintains 50.1% of initial activity, i.e. 69.17 U/g support, for 8 months. The bioreactor shows the best production of inverted sugar syrup using up-flow rate of 0.48 l/h with average conversion of 10.64%/h at a feeding rate of 104 /h |
| 3.2.1.26 | beta-fructofuranosidase |
synthesis |
production of high levels of cell extract and extracellular invertases when grown under submerged fermentation and solid-state fermentation, using agroindustrial products or residues as substrates, mainly soy bran and wheat bran, at 40°C for 72 h and 96 h, respectively. Addition of glucose or fructose in submerged fermentation inhibits enzyme production, while the addition of 1% (w/v) peptone as organic nitrogen source enhances the production by 3.7fold. 1% (w/v) (NH4)2HPO4 inhibits enzyme production around 80% |
| 3.2.1.28 | alpha,alpha-trehalase |
synthesis |
expression as a fusion protein with an N-terminal or C-terminal hexahistidine tag in a baculovirus-silkworm expression system. Only N-terminally tagged trehalase shows a high activity |
| 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 |
| 3.2.1.31 | beta-glucuronidase |
synthesis |
the enzyme appears suitable for use in enzymatic oligosaccharide synthesis in either the transglycosylation mode or by use of glycosynthase and thioglycoligase approaches |
| 3.2.1.31 | beta-glucuronidase |
synthesis |
mutant enzyme A365H/R563E has great potential in the industrial production of glycyrrhetinic acid 3-O-mono-beta-D-glucuronide |
| 3.2.1.32 | endo-1,3-beta-xylanase |
synthesis |
the enzyme may be an essential component for the preparation of protoplasts from some groups of seaweed |
| 3.2.1.32 | endo-1,3-beta-xylanase |
synthesis |
preparation of a large number of protoplasts are isolated from Porphyra yezoensis, Phorphyra tenera, and Bangia atropurpurea |
| 3.2.1.32 | endo-1,3-beta-xylanase |
synthesis |
production of D-ylulose from beta-1,3-xylan, of the killer alga Caulerpa taxifolia. The synergistic action of beta-1,3-xylanase TxyA and beta-1,3-xylosidase XloA from Vibrio sp. strain XY-214 enables efficient saccharification of beta-1,3-xylan to D-xylose. D-Xylose is then converted to D-xylulose by using XylA |
| 3.2.1.33 | amylo-alpha-1,6-glucosidase |
synthesis |
use of enzyme for industrial production of cycloamylose |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
synthesis |
synthesis of a group of uncommon xylosides via the transxylosylation activity |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
synthesis |
immobilization of enzyme on chitosan as best support material gives immobilization and activity yields of 94% and 87%, respectively, of initial activity, and also provides the highest stability, retaining 94% of its initial activity even after being recycled 25times. Maximal activity of immobilized enzyme is achieved at pH 8.0 and 53°C, whereas that for the free enzyme is obtained at pH 7.0 and 50°C. The immobilized enzyme is more thermostable than the free beta-xylosidase. Km values of the free enzyme increases from 2.37 mM to 3.42 mM at the immobilized state. Immobilized enzyme catalyzes the reverse hydrolysis reaction, forming xylooligosaccharides in the presence of a high concentration of xylose. Co-immobilized of beta-xylosidase and xylanase on chitosan leads to a continuous hydrolysis of 3% oat spelt xylan at 50°C and better hydrolysis yields and higher amount of xylose are obtained |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
synthesis |
the enzyme immobilized by entrapment into alginate can be used for a continuous production of xylose from xylooligosaccharides at high temperature |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
synthesis |
formation of xylooligosaccharides from alpha-D-xylopyranosyl fluoride in a conjugated reaction between beta-xylosidase E335G mutant enzyme and endo-1,4-beta-xylanase E265G mutant enzyme |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
synthesis |
upon codon optimization for expression in Pichia pastoris, the expression level increases to 5.7 g/l in a fermenter system |
| 3.2.1.38 | beta-D-fucosidase |
synthesis |
synthesis of fucosylsugars using the transglycosylation activity |
| 3.2.1.39 | glucan endo-1,3-beta-D-glucosidase |
synthesis |
heterologous 1,3-beta-glucanase production in Escherichia coli is favoured with moderate culture aeration (0.7-0.9 vvm) and moderate stirring (125150 rev/min) |
| 3.2.1.39 | glucan endo-1,3-beta-D-glucosidase |
synthesis |
the enzyme in Schizophyllum commune strain GIM5-43 is used for partial schizophyllan cleavage to achieve a moderate molecular weight and better solubility of schizophyllan |
| 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 |
| 3.2.1.40 | alpha-L-rhamnosidase |
synthesis |
synthesis of aglycones from glycosides |
| 3.2.1.40 | alpha-L-rhamnosidase |
synthesis |
immobilization of recombinant enzyme on Ca2+ alginate beads. Immobilization enables its reutilization up to 9 hydrolysis batches without an appreciable loss in activity |
| 3.2.1.40 | alpha-L-rhamnosidase |
synthesis |
a wild-type alpha-L-rhamnosidase from Alternaria sp. L1 can synthesize rhamnose-containing chemicals through reverse hydrolysis reaction with inexpensive rhamnose as glycosyl donor |
| 3.2.1.40 | alpha-L-rhamnosidase |
synthesis |
adding sorbitol has great potential to promote enzymatic conversion of rutin to isoquercitrin production. Isoquercitrin has several biological activities, including anti-mutagenesis, anti-virus, anti-hypertensive, anti-proliferative effects, lipid peroxidation, oxidative-stress protection as well as other pharmacological effects |
| 3.2.1.41 | pullulanase |
synthesis |
use of enzyme for synthesis of novel heterobranche beta-cyclodextrins |
| 3.2.1.41 | pullulanase |
synthesis |
preparation of maltotriose by hydrolyzing of pullulan with pullulanase, optimum conditions are: time 6 h, pH 5.0, temperature 45°C, amount of pullulanase 10 ASPU/g, concentration of pullulan 3% w/v, method, overview |
| 3.2.1.41 | pullulanase |
synthesis |
recombinant expression of PulB in Bacillus subtilis is increased by stronger constitutive promoter P43 and use of strain WB600 instread of WB800. Extracellular pullulanase activity reaches up to 24.5 U/ml |
| 3.2.1.51 | alpha-L-fucosidase |
synthesis |
the transfucosylation ability of one of the fucosidase isoform might be of interest for the synthesis of fucosides |
| 3.2.1.54 | cyclomaltodextrinase |
synthesis |
CDase I-5 is applied to modify the starch structure to produce low-amylose starch products by incubating rice starch with this enzyme. The amylose content of rice starch decreases from 28.5 to 9% while the amylopectin content remains almost constant with no significant change in side chain length distribution |
| 3.2.1.54 | cyclomaltodextrinase |
synthesis |
the G415E mutant is an excellent candidate for the industrial production of specific-length maltooligosaccharides from cyclodextrins |
| 3.2.1.55 | non-reducing end alpha-L-arabinofuranosidase |
synthesis |
application of the recombinant enzyme in the production of xylobiose |
| 3.2.1.55 | non-reducing end alpha-L-arabinofuranosidase |
synthesis |
alpha-L-arabinanases are essential glycosyl hydrolases participating in the complete hydrolysis of hemicellulose, a natural resource for various industrial processes, such as bioethanol or pharmaceuticals production |
| 3.2.1.55 | non-reducing end alpha-L-arabinofuranosidase |
synthesis |
the enzyme might be useful for enzymatic synthesis of galactosylfuranoside-containing pharmacophores to be used in mammals |
| 3.2.1.55 | non-reducing end alpha-L-arabinofuranosidase |
synthesis |
the thermostable enzyme is used for production of ginsenoside Rd from ginsenoside Rc, optimal reaction conditions are pH 5.5, 80°C, 227 U enzyme/ml, and 8.0 g/l ginsenoside Rc in the presence of 30% v/v n-hexane |
| 3.2.1.55 | non-reducing end alpha-L-arabinofuranosidase |
synthesis |
use of alpha-L-arabinofuranosidase from Caldicellulosiruptor saccharolyticus along with beta-glycosidase from Sulfolobus solfataricus to produce ginsenoside compound K from the protopanaxadiol-type ginsenosides in red-ginseng extract. The optimal reaction conditions are as follows: pH 6.0, 80°C, 2 U/ml Sulfolobus solfataricus enzyme, 3 U/ml Caldicellulosiruptor saccharolyticus enzyme, and 7.5 g/l protopanaxadiol-type ginsenosides. The enzymes produce 4.2 g/l ginsenoside compound K from 7.5 g/l ginsenosides in 12 h without other ginsenosides, with a molar yield of 100% and a productivity of 348 mg/l/h |
| 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 |
| 3.2.1.61 | mycodextranase |
synthesis |
the enzyme seems to be a useful tool for the preparation of expensive nigerose and nigerooligosaccharides |
| 3.2.1.65 | levanase |
synthesis |
protection from aging |
| 3.2.1.65 | levanase |
synthesis |
paper industry |
| 3.2.1.65 | levanase |
synthesis |
synthesis of various products such as ethanol or aceton-butanol |
| 3.2.1.65 | levanase |
synthesis |
commercial production of ultra-high-fructose syrups |
| 3.2.1.65 | levanase |
synthesis |
the enzyme is used for simultaneous saccharification and fermentation of inulin to 2,3-butanediol. A fed-batch simultaneous saccharification and fermentation yields 103.0 g/liter 2,3-butanediol in 30 h, with a high productivity of 3.4 g/liter/h |
| 3.2.1.65 | levanase |
synthesis |
the enzyme is uzilized for production of beta2-6 fructose oligosaccharides (levan-type FOS) through a sequential reactionwith levan produced from sucrose by bacterial levansucrases, method development, overview |
| 3.2.1.67 | galacturonan 1,4-alpha-galacturonidase |
synthesis |
pectic enzymes used to generate protoplasts in cell cultures |
| 3.2.1.67 | galacturonan 1,4-alpha-galacturonidase |
synthesis |
pectic enzymes industrially important in processing of agricultural products, production of pectinolytic enzymes, specifical enzyme for modification of pectins |
| 3.2.1.67 | galacturonan 1,4-alpha-galacturonidase |
synthesis |
preparing methylated pectins |
| 3.2.1.67 | galacturonan 1,4-alpha-galacturonidase |
synthesis |
as adjunct to cellulases and hemicellulases in cellulosic biomass treatment |
| 3.2.1.67 | galacturonan 1,4-alpha-galacturonidase |
synthesis |
mutant strain M3 can be used for production of exopolygalacturonase |
| 3.2.1.68 | isoamylase |
synthesis |
the enzyme is used for debranching of amylomaize in the production of cycloamylose, natural amylopectin containing starch with enhanced conversion yield after debranching, use of Thermus aquaticus 4-alpha-glucanotransferase for conversion of debranched amylomaize amylose and amylomaize amylopectin into cycloamylose, overview |
| 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 |
| 3.2.1.73 | licheninase |
synthesis |
the unusually resistance against inactivation by heat, ethanol or ionic detergents makes the enzyme highly suitable for industrial application in the mashing process of beer brewing |
| 3.2.1.73 | licheninase |
synthesis |
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30% |
| 3.2.1.73 | licheninase |
synthesis |
over-expression in Pichia pastoris, with a yield of about 1000 U/ml in a 3.7 l fermentor |
