Simple jQuery Dropdowns
Please use this identifier to cite or link to this item:
Title: β-Glucosidase, exo-β-glucanase and pyridoxine transglucosylase activities of rice BGlu1
Authors: Rodjana Opassiri
Yanling Hua
Onnop Wara-Aswapati
Takashi Akiyama
Jisnuson Svasti
Asim Esen
James R. Ketudat Cairns
Suranaree University of Technology
Hokkaido Agricultural Research Center, NARO
Mahidol University
Virginia Polytechnic Institute and State University
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Apr-2004
Citation: Biochemical Journal. Vol.379, No.1 (2004), 125-131
Abstract: The bglu1 cDNA for a β-glucosidase cloned from rice (Oryza sativa L.) seedlings was expressed as a soluble and active protein in Escherichia coli and designated BGlu1. This enzyme hydrolysed β-1,4-linked oligosaccharides with increasing catalytic efficiency (kcat/Km) values as the DP (degree of polymerization) increased from 2 to 6. In contrast, hydrolysis of β-1,3-linked oligosaccharides decreased from DP 2 to 3, and polymers with a DP greater than 3 were not hydrolysed. The enzyme also hydrolysed p-nitrophenyl β-D-glycosides and some natural glucosides but with lower catalytic efficiency than β-linked oligosaccharides. Pyridoxine 5′-O-β-D- glucoside was the most efficiently hydrolysed natural glycoside tested. BGlu1 also had high transglucosylation activity towards pyridoxine, producing pyridoxine 5′-O-β-D-glucopyranoside in the presence of the glucose donor p-nitrophenyl β-D-glucoside.
ISSN: 02646021
Appears in Collections:Scopus 2001-2005

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.