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Search term: synthesis

<< < Results 2001 - 2100 of 3221 > >>
EC Number Recommended Name Application Commentary
Show all pathways known for 3.2.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.23beta-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
Show all pathways known for 3.2.1.23Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.23beta-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%
Show all pathways known for 3.2.1.26Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.26beta-fructofuranosidase synthesis immobilization using anion-exchange resin WA-30 and cross-linking with glutaraldehyde depresses the hydrolysis reaction of isoform F2
Show all pathways known for 3.2.1.26Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.26beta-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
Show all pathways known for 3.2.1.26Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.26beta-fructofuranosidase synthesis immobilization by sodium alginate increases enzyme stability
Show all pathways known for 3.2.1.26Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.26beta-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
Show all pathways known for 3.2.1.26Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.26beta-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
Show all pathways known for 3.2.1.26Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.26beta-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
Show all pathways known for 3.2.1.26Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.26beta-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%
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26Sulfolobus solfataricus beta-glycosidase synthesis a continuous stirred-tank reactor charged with the enzyme and operated at steady-state conditions could be a useful reaction system for the production of galacto-oligosaccharides in which composition is narrower and more easily programmable, in terms of the individual components contained, as compared to the batchwise reaction
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26Sulfolobus solfataricus beta-glycosidase synthesis development of a continuous cellobiose hydrolysis system for glucose production with a high degree of conversion by the enzyme immobilized on chitosan activated with glutaraldehyde
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26Sulfolobus solfataricus beta-glycosidase synthesis enzymatic synthesis of 2-beta-D-galactopyranosyloxyethyl methacrylate starting from 2-hydroxyethyl methacrylate and 4-nitrophenyl-beta-D-galactopyranoside
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26Sulfolobus solfataricus beta-glycosidase synthesis enzymatic synthesis of polyol- and masked polyol-glycosides. The enzyme performs the synthesis of glycosides in a competitive high yield compared with that obtained with mesophilic enzymes. It permits the use of a wide variety of acceptors including tetritol compounds and their masked or protected derivatives. The synthesis of glucosides of 2,3-isopropylidene protected pure enantiomers of threitol shows the possibility of obtaining reasonable yields of products in the presence of a scarce amount of the acceptor by adding aliquots of donor at time intervals, in such a way that a molar excess of acceptor was maintained, thus avoiding undesirable formation of glycosides of the donor or enzymatic hydrolysis of the product
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26Sulfolobus solfataricus beta-glycosidase synthesis formation of mannosides and xylosides by transglycosylation
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26Sulfolobus solfataricus beta-glycosidase synthesis high yield production of hydroxytyrosol from a commercially available oleuropein by using the immobilised recombinant EcSbgly from the hyperthermophilic archaeon Sulfolobus solfataricus on chitosan support
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26Sulfolobus solfataricus beta-glycosidase synthesis industrial production of galactooligosaccharides, very efficient enzyme for the synthesis of beta-galactooligosaccharides because of its high product yields, transfer rates, substrate specificity, and thermostability
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26Sulfolobus solfataricus beta-glycosidase synthesis optimization of hexyl-beta-D-glycoside synthesis from lactose in hexanol at low water activity and high temperature. Compared to other beta-glycosidases in lactose conversion into alkyl glycoside, the enzyme shows high activity in a hexanol one-phase system and synthesized high yields of both hexyl-beta-D-galactoside and hexyl-beta-D-glucoside. Using 32 g/l lactose (93 mM), the enzyme synthesizes yields of 41% galactoside (38.1 mM) and 29% glucoside (27.0 mM)
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26Sulfolobus solfataricus beta-glycosidase synthesis synthesis of 2-deoxyglycosides and 2-deoxygalactosides from glucal or galactal as donors. The yields observed with alkyl acceptors confirms that the robustness of the biocatalyst is of great help in designing practical syntheses of pure beta-anomers of 2-deoxy derivatives of 4-penten-1-ol (obtained in 80% yield at 20 fold molar excess) and 3,4-dimethoxybenzyl alcohol (obtained in 19% yield at 3.3 fold molar excess). The attachment of 2-deoxyglyco units is performed on various pyranosidic acceptors (4-nitrophenyl alpha-D-glucopyranoside, 2-nitrophenyl 2-deoxy-N-acetyl-alpha-D-glucosamine and 4-nitrophenyl 2-deoxy-N-acetyl-beta-D-glucosamine). At low molecular excesses of the acceptors, satisfactory yields (20-40%) of chromophoric 2-deoxy di- and trisaccharides are obtained
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26Sulfolobus solfataricus beta-glycosidase synthesis synthesis of ginsenoside K (20-O-beta-D-glucopyranosyl-20(S)-protopanaxadiol) by a recombinant enzyme. 20-O-beta-D-Glucopyranosyl-20(S)-protopanaxadiol has anti-tumor, anti-inflammatory, anti-allergic and hepatoprotective effects
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26Sulfolobus solfataricus beta-glycosidase synthesis the immobilized enzyme is useful for the production of galactooligosaccharides by using a packed-bed enzyme reactor operated at 70°C
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26Sulfolobus solfataricus beta-glycosidase synthesis application of the alpha-L-arabinofuranosidase from Caldicellulosiruptor saccharolyticus along with the beta-glycosidase from Sulfolobus solfataricus to yield ginsenoside compound K from the protopanaxadiol-type ginsenosides in red-ginseng extracts. The optimal reaction conditions are pH 6.0, 80°C, 2 U/ml beta-glucosidase, 3 U/ml alpha-L-arabinofuranosidase, and 7.5 g/l ginsenosides in red-ginseng extract. Under these optimized conditions 4.2 g/l ginsenoside compound K from 7.5 g/l protopanaxadiol-type ginsenosides is obtained in 12 h without other ginsenosides, with a molar yield of 100% and a productivity of 348 mg/l/h
Show all pathways known for 3.2.1.28Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.28alpha,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
Display the reaction diagram Show all sequences 3.2.1.B28Pyrococcus furiosus beta-glycosidase synthesis a continuous stirred-tank reactor charged with the enzyme and operated at steady-state conditions could be a useful reaction system for the production of galacto-oligosaccharides in which composition is narrower and more easily programmable, in terms of the individual components contained, as compared to the batchwise reaction
Display the reaction diagram Show all sequences 3.2.1.B28Pyrococcus furiosus beta-glycosidase synthesis optimization of hexyl-beta-glycoside synthesis from lactose in hexanol at low water activity and high temperature. Compared to other beta-glycosidases in lactose conversion into alkyl glycoside, the enzyme shows high activity in a hexanol one-phase system and synthesized high yields of both hexyl-beta-galactoside and hexyl-beta-glucoside. The enzyme synthesizes yields of 63% galactoside (58.6mM) and 28% glucoside (26.1 mM)
Display the reaction diagram Show all sequences 3.2.1.B28Pyrococcus furiosus beta-glycosidase synthesis the immobilized enzyme is useful for the production of galactooligosaccharides by using a packed-bed enzyme reactor operated at 70°C
Display the reaction diagram Show all sequences 3.2.1.B28Pyrococcus furiosus beta-glycosidase synthesis beta-glycosidase converts ginsenosides Rb1, Rb2, Rc, and Rd to protopanaxadiol aglycone via compound K. With increases in the enzyme activity, the productivities increase. The substrate concentration is optimal at ginsenoside Rd or 10% (w/v) ginseng root extract. 4 mM of ginsenoside Rd is converted to 3.3 mM compound K with a yield of 82.5% (mol/mol) and a productivity of 2010 mg per l and h at 1 h and is hydrolyzed completely to the aglycone with 364 mg per l and h after 5 h
Display the reaction diagram Show all sequences 3.2.1.B28Pyrococcus furiosus beta-glycosidase synthesis continuous enzymatic process for the production of the prebiotic disaccharide lactulose through transgalactosylation by CelB. CelB is immobilized onto anion-exchange resin Amberlite IRA-93 or onto Eupergit C with immobilization yields of 72% and 83%, respectively, giving specific activities of 920 nkat/g dry carrier and 1500 nkat/g dry carrier at 75°C with 4-nitrophenyl-beta-D-galactopyranoside as substrate. Maximum lactulose yields of 43% related to the initial lactose concentration are reached. The corresponding productivities are 52 g lactulose per l and h using Amberlite IRA-93 and 15 g lactulose per l and h unsing Eupergit C, respectively. While both carrier-bound CelB preparations are 100% stable for at least 14 days, the half-life of the free CelB in the enzyme membrane reactor is only about 1.5 days
Display the reaction diagram Show all sequences 3.2.1.B28Pyrococcus furiosus beta-glycosidase synthesis development of a microstructured immobilized enzyme reactor for production of beta-glucosylglycerol, transglycosylation reaction, under conditions of continuous flow at 70°C. CelB is covalently attached onto coated microchannel walls to give an effective enzyme activity of 30 U per total reactor working volume of 25 ml. Glycerol causes a concentration-dependent decrease in the conversion of the glucosyl donors 2-nitrophenyl beta-D-glucoside and cellobiose via hydrolysis and strongly suppresses participation of the substrate in the reaction as glucosyl acceptor. The yields of beta-glucosylglycerol are about 80% and 60% based on 2-nitrophenyl beta-D-glucoside and cellobiose converted, respectively, and maintain up to near exhaustion of substrate, giving about 120 mM (30 g/l) of beta-glucosylglycerol from the reaction of cellobiose and 1 M glycerol. The structure of the transglucosylation products is 1-O-beta-D-glucopyranosyl-rac-glycerol (79%) and 2-O-beta-D-glucopyranosyl-sn-glycerol (21%)
Display the reaction diagram Show all sequences 3.2.1.B28Pyrococcus furiosus beta-glycosidase synthesis expression of CleB gene in Escherichia coli gives approx 100000 U of enzyme activity/l of culture medium after 8 h of growth
Display the reaction diagram Show all sequences 3.2.1.B28Pyrococcus furiosus beta-glycosidase synthesis expression of enzyme using a baculovirus expression vector system in silkworm, Bombyx mori and purification to about 81% homogeneity in a single heat-treatment step. The expressed beta-glucosidase accounts for more than 10% of silkworm total haemolymph proteins. The expression level reaches 10199.5 U per ml hemolymph and 19797.4 U per silkworm larva, and the specific activity of the one-step purified crude enzyme is 885 U per mg
Display the reaction diagram Show all sequences 3.2.1.B28Pyrococcus furiosus beta-glycosidase synthesis hydrolysis of lactose in UHT skim milk at 70°C using CelB covalently attached onto Eupergit C in yields of 80%, and in a packed-bed immobilized enzyme reactor. The packed-bed reactor is about 10fold more stable and gives about the same productivity at 80% substrate conversion as the hollow-fiber reactor at 60% substrate conversion. The marked difference in the stability of free and immobilized CelB seems to reflect mainly binding of the soluble enzyme to the membrane surface of the hollow-fiber module. Microbial contamination of the reactors did not occur during reaction times of up to 39 d
Display the reaction diagram Show all sequences 3.2.1.B28Pyrococcus furiosus beta-glycosidase synthesis improvement of the stability of recombinant CelB by entrapment into Escherichia coli cells under conditions promoting strong inactivation. Glutardialdehyde-mediated protein cross-linking or rigidification of the cell membrane by adding magnesium ions is required to prevent release of CelB from within the cell into the bulk solution. In the presence of 1M glucose or when applying recirculation rates of 2.6per min, the entrapped enzyme is around 2fold more stable at 80°C than free CelB. The significance of the stabilisation is attenuated by the decrease in CelB initial activity which wis due to cross-linking and glutardialdehyde concentration-dependent
Display the reaction diagram Show all sequences 3.2.1.B28Pyrococcus furiosus beta-glycosidase synthesis use of CelB for oligosaccharide production from lactose in a kinetically controlled reaction. At reaction temperatures of 80°C and higher, the inactivation rate of the enzyme in the presence of sugars is increased by a factor of 2, caused by the occurrence of Maillard reactions between the sugar and the enzyme
Show all pathways known for 3.2.1.31Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.31beta-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
Show all pathways known for 3.2.1.31Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.31beta-glucuronidase synthesis mutant enzyme A365H/R563E has great potential in the industrial production of glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
Show all pathways known for 3.2.1.32Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.32endo-1,3-beta-xylanase synthesis the enzyme may be an essential component for the preparation of protoplasts from some groups of seaweed
Show all pathways known for 3.2.1.32Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.32endo-1,3-beta-xylanase synthesis preparation of a large number of protoplasts are isolated from Porphyra yezoensis, Phorphyra tenera, and Bangia atropurpurea
Show all pathways known for 3.2.1.32Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.32endo-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
Show all pathways known for 3.2.1.33Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.33amylo-alpha-1,6-glucosidase synthesis use of enzyme for industrial production of cycloamylose
Display the reaction diagram Show all sequences 3.2.1.B33Sulfolobus shibatae beta-glycosidase synthesis synthesis of beta-glucosylglycerol and its derivatives through the transglycosylation by Sulfolobus shibatae beta-glycosidase SSG and Deinococcus geothermalis amylosucrase DGAS. SSG catalyzes a transglycosylation reaction with glycerol as an acceptor and cellobiose as a donor to produce 56% of beta-D-glucopyranosyl-(1->1/3)-D-glycerol and beta-D-glucopyranosyl-(1->4)-D-glycerol. As a result, 61% of alpha-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->1/3)-D-glycerol and 28% of alpha-D-maltopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->1/3)-D-glycerol are synthesized as unnatural glucosylglycerols
Display the reaction diagram Show all sequences 3.2.1.B34Sulfolobus acidocaldarius beta-glycosidase synthesis enzyme is a potential producer of the rare ginsenosides compound K, compound Y, and compound Mc from the major ginsenosides Rb1, Rb2, Rc, and Rd
Display the reaction diagram Show all sequences 3.2.1.B34Sulfolobus acidocaldarius beta-glycosidase synthesis use of alpha-L-arabinofuranosidase from Caldicellulosiruptor saccharolyticus, EC 3.2.1.55, 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
Show all pathways known for 3.2.1.37Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.37xylan 1,4-beta-xylosidase synthesis synthesis of a group of uncommon xylosides via the transxylosylation activity
Show all pathways known for 3.2.1.37Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.37xylan 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
Show all pathways known for 3.2.1.37Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.37xylan 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
Show all pathways known for 3.2.1.37Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.37xylan 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
Show all pathways known for 3.2.1.37Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.37xylan 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
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.38beta-D-fucosidase synthesis synthesis of fucosylsugars using the transglycosylation activity
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.39glucan 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 (125–150 rev/min)
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.39glucan 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
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.40alpha-L-rhamnosidase synthesis synthesis of aglycones from glycosides
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.40alpha-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
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.40alpha-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
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.40alpha-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
Display the reaction diagram Show all sequences 3.2.1.B40Pyrococcus horikoshii beta-glycosidase synthesis in the presence of sodium formate buffer pH 4.0 at 75°C the E324G mutant acts as a hyperthermophilic glycosynthase. Though the yield of the reaction does not exceed 10%, it is demonstrated that this could be a general strategy for the preparation of hyperthermophilic glycosynthase. The peculiar specificity of the enzyme for alkyl-glycosides makes the resulting glycosynthase a promising tool for biocatalysis
Show all pathways known for 3.2.1.41Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.41pullulanase synthesis use of enzyme for synthesis of novel heterobranche beta-cyclodextrins
Show all pathways known for 3.2.1.41Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.41pullulanase 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
Show all pathways known for 3.2.1.41Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.41pullulanase 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
Display the reaction diagram Show all sequences 3.2.1.B44glycyrrhizin glucuronohydrolase (glycyrrhetinic acid 3-O-beta-D-glucuronide-forming) synthesis the enzyme is potentially a powerful biocatalyst for environmentally friendly and cost-effective production of glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
Show all pathways known for 3.2.1.51Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.51alpha-L-fucosidase synthesis the transfucosylation ability of one of the fucosidase isoform might be of interest for the synthesis of fucosides
Show all pathways known for 3.2.1.54Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.54cyclomaltodextrinase 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
Show all pathways known for 3.2.1.54Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.54cyclomaltodextrinase synthesis the G415E mutant is an excellent candidate for the industrial production of specific-length maltooligosaccharides from cyclodextrins
Show all pathways known for 3.2.1.55Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.55non-reducing end alpha-L-arabinofuranosidase synthesis application of the recombinant enzyme in the production of xylobiose
Show all pathways known for 3.2.1.55Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.55non-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
Show all pathways known for 3.2.1.55Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.55non-reducing end alpha-L-arabinofuranosidase synthesis the enzyme might be useful for enzymatic synthesis of galactosylfuranoside-containing pharmacophores to be used in mammals
Show all pathways known for 3.2.1.55Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.55non-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
Show all pathways known for 3.2.1.55Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.55non-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
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.61mycodextranase synthesis the enzyme seems to be a useful tool for the preparation of expensive nigerose and nigerooligosaccharides
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.65levanase synthesis protection from aging
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.65levanase synthesis paper industry
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.65levanase synthesis synthesis of various products such as ethanol or aceton-butanol
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.65levanase synthesis commercial production of ultra-high-fructose syrups
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.65levanase 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
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.65levanase 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
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.67galacturonan 1,4-alpha-galacturonidase synthesis pectic enzymes used to generate protoplasts in cell cultures
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.67galacturonan 1,4-alpha-galacturonidase synthesis pectic enzymes industrially important in processing of agricultural products, production of pectinolytic enzymes, specifical enzyme for modification of pectins
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.67galacturonan 1,4-alpha-galacturonidase synthesis preparing methylated pectins
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.67galacturonan 1,4-alpha-galacturonidase synthesis as adjunct to cellulases and hemicellulases in cellulosic biomass treatment
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.67galacturonan 1,4-alpha-galacturonidase synthesis mutant strain M3 can be used for production of exopolygalacturonase
Show all pathways known for 3.2.1.68Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.68isoamylase 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
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.73licheninase 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
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.73licheninase 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%
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.73licheninase synthesis over-expression in Pichia pastoris, with a yield of about 1000 U/ml in a 3.7 l fermentor
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.73licheninase synthesis upon expression in Pichia pastoirs as active extracellular beta-1,3-1,4-glucanase, the recombinant protein is secreted predominantly into the medium and comprises up to 85% of the total extracellular proteins and reaches a protein concentration of 9.1 g/l with an activity of 55,300 U/ml in 5-l fermentor culture
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.73licheninase synthesis analysis of fermentation conditions for beta-1,3-1,4-glucanase production under solid-state fermentation. Under the optimized fermentation conditions, viz. oatmeal as sole carbon source, 5% (w/w) peptone as sole nitrogen source, initial moisture of 80% (w/w), initial culture pH of 5.0, incubation temperature of 50°C and incubation time of 6 days, the highest beta-1,3-1,4-glucanase activity of 20025 U/g dry substrate is achieved. The addition of the purified beta-1,3-1,4-glucanase in mash obviously reduces its filtration time (24.6%) and viscosity (2.61%)
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.73licheninase synthesis expression of mutant K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P in Bacillus subtilis to maximal extracellular activity of 4840.4 U/ml
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.73licheninase synthesis immobilization of enzyme on porous silica using glutaraldehyde. Enzyme activity decreases sharply at high concentrations of glutaraldehyde. Immobilized protein is stable over a wide range of pH and can be stored long term at 4°C. After 10 cycles, the enzyme retains 42% of its initial catalytic activity
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.73licheninase synthesis the enzyme can be used in the production of anti-hypercholesterolemic agents
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.78mannan endo-1,4-beta-mannosidase synthesis production of enzyme by expression in Aspergillus niger under control of the Aspergillus niger glyceraldehyde-3-phosphate dehydrogenase promoter gpdP and the Aspergillus awamori glucoamylase terminator glaAT. The glucose concentration and the organic nitrogen source have an effect on both the volumetric enzyme activity and the specific enzyme activity. The highest mannanase activity levels of 16596 nkat ml-1 and 574 nkat mg-1 dcw are obtained for Aspergillus niger when cultivated in a process-viable medium containing corn steep liquor as the organic nitrogen source and high glucose concentrations
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.78mannan endo-1,4-beta-mannosidase synthesis expression in Yarrowia lipolytica using beta-mannosidase's own secretion signal. Fed batch fermentations result in a 3.9fold increase in volumetric enzyme activity compared with batch fermentation, and a maximum titre of 26,139 nkat/ml
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.78mannan endo-1,4-beta-mannosidase synthesis production of beta-mannanase using palm kernel cake as substrate in solid substrate fermentation. Optimal conditions are incubation temperature of 32°C, initial moisture level of 59% and aeration rate of 0.5 l/min, resulting in a beta-mannanase yield of 2231.26 U/g
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.78mannan endo-1,4-beta-mannosidase synthesis development of a fed-batch strategy for engineered enzyme, using high cell-density fermentation. Mannanase activity reaches 5069 U/ml after cultivation for 56 h in 50 l fermenter
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.78mannan endo-1,4-beta-mannosidase synthesis expression in Escherichia coli based on T7 RNA polymerase promoter and tac promoter systems. Both Escherichia coli OmpA signal peptide and native Bacillus signal peptide can be used efficiently for secretion of recombinant protein. Enzyme can be harvested from whole cell lysate, periplasmic extract or culture broth 4-20 h after induction by IPTG
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.78mannan endo-1,4-beta-mannosidase synthesis production of beta-mannanase from palm kernel cake as a substrate in solid substrate fermentation. A statistical model suggests that the optimal conditions for attaining the highest level of beta-mannanase are incubation temperature of 32°C, initial moisture level of 59% and aeration rate of 0.5 l/min. A beta-mannanase yield of 2231.26 U/g is obtained under these optimal conditions
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.80fructan beta-fructosidase synthesis microbial production of high fructose syrup, alcohol, acetone and butanol
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.80fructan beta-fructosidase synthesis the enzyme preparation is used to hydrolyze pure inulin and raw inulin from Asparagus racemosus for the preparation of a high-fructose syrup
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.80fructan beta-fructosidase synthesis expression of bacterial levanase in yeast enables simultaneous saccharification and fermentation of grass juice to bioethanol
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.81beta-agarase synthesis use of enzyme for preparation of neoagarohexaose and neoagarotetraose and separation of neoagaro-oligosaccharides by consecutive column chromatography
Show all pathways known for 3.2.1.91Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.91cellulose 1,4-beta-cellobiosidase (non-reducing end) synthesis expression in Pichia pastoris after codon optimization and using the strong methanol-inducible promoter AOX1. 5.84 U CBH II per ml can be obtained at 96 h
Show all pathways known for 3.2.1.91Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.91cellulose 1,4-beta-cellobiosidase (non-reducing end) 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
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