3.2.1.B28: Pyrococcus furiosus beta-glycosidase
This is an abbreviated version!
For detailed information about Pyrococcus furiosus beta-glycosidase, go to the full flat file.
Reaction
The enzyme produces mannose and glucose mainly from mannooligosaccharides and cellobiose by hydrolyzing them from the reducing end. It can not hydrolyze alpha-form substrates and bulk polymers like mannan and starch =
Synonyms
beta-glycosidase, Bgl, BGLPf, CelB, PFTG
ECTree
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Application on EC 3.2.1.B28 - Pyrococcus furiosus beta-glycosidase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
degradation
encapsulation of CelB into silica microcapsules for degradation of biomass. The encapsulated enzyme is active at 80-100°C, but diffusion of cellobiose into the silica microcapsules is a rate-limiting step
food industry
pharmacology
the hyperthermostable beta-glycosidase may be useful for food and pharmaceutical applications
synthesis
additional information
the enzyme converts flavanone glycoside to flavanone aglycone via a one-step reaction. It may be useful in the production of the flavanone aglycones naringenin and hesperetin from flavanone glycosides in citrus extracts
food industry
the hyperthermostable beta-glycosidase may be useful for food and pharmaceutical applications
food industry
the enzyme suitable for hydrolysis of lactose at temperatures at 70-80°C
food industry
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the immobilized enzyme is useful for the hydrolysis of lactose in whey or milk by using a packed-bed enzyme reactor operated at 70°C
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
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)
synthesis
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the immobilized enzyme is useful for the production of galactooligosaccharides by using a packed-bed enzyme reactor operated at 70°C
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
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
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%)
synthesis
expression of CleB gene in Escherichia coli gives approx 100000 U of enzyme activity/l of culture medium after 8 h of growth
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
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
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
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
