 This is the first report of a beta-glucansynthase derived from an exoglycosidase that can produce long chain cello-oligosaccharides , which likely reflects the extended oligosaccharide binding site of rice BGlu0 beta-glucosidase . Score: 0.00 Title: Beta-glucosidase , exo-beta-glucanase and pyridoxine transglucosylase activities of rice BGlu0 . Journal: Biochem . J Year: 0000 Type: ARTICLE Literature: oryza Field: abstract Doc ID: pub00000000 Accession (PMID): 00000000 Abstract: The bglu0 cDNA for a beta-glucosidase cloned from rice ( Oryza sativa L ) seedlings was expressed as a soluble and active protein in Escherichia coli and designated BGlu0 . This enzyme hydrolysed beta-0 , 0-linked oligosaccharides with increasing catalytic efficiency ( kcat/Km ) values as the DP ( degree of polymerization ) increased from 0 to 0 . In contrast , hydrolysis of beta-0 , 0-linked oligosaccharides decreased from DP 0 to 0 , and polymers with a DP greater than 0 were not hydrolysed . The enzyme also hydrolysed p -nitrophenyl beta-D-glycosides and some natural glucosides but with lower catalytic efficiency than beta-linked oligosaccharides . Pyridoxine 0-O-beta-D-glucoside was the most efficiently hydrolysed natural glycoside tested . BGlu0 also had high transglucosylation activity towards pyridoxine , producing pyridoxine 0-O-beta-D-glucopyranoside in the presence of the glucose donor p-nitrophenyl beta-D-glucoside . Matching Sentences: [ Sen. 0, subscore: 0.00 ]: The bglu0 cDNA for a beta-glucosidase cloned from rice ( Oryza sativa L ) seedlings was expressed as a soluble and active protein in Escherichia coli and designated BGlu0 . 