beta-Glucosidase, exo-beta-glucanase and pyridoxine transglucosylase activities of rice BGlu1
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- Rodjana OPASSIRI
- Institute of Science, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand
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- Yanling HUA
- Center for Scientific and Technological Equipment, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand
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- Onnop WARA-ASWAPATI
- Institute of Science, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand
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- Takashi AKIYAMA
- Department of Low Temperature Science, National Agricultural Research Center for the Hokkaido Region, Sapporo 062-8555, Japan
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- Jisnuson SVASTI
- Department of Biochemistry and Center for Protein Structure and Function, Faculty of Science, Mahidol University, Bangkok 10400, Thailand
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- Asim ESEN
- Department of Biology, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061-0406, U.S.A.
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- James R. KETUDAT CAIRNS
- Institute of Science, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand
説明
<jats:p>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.</jats:p>
収録刊行物
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- Biochemical Journal
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Biochemical Journal 379 (1), 125-131, 2004-04-01
Portland Press Ltd.
