Rodjana OpassiriYanling HuaOnnop Wara-AswapatiTakashi AkiyamaJisnuson SvastiAsim EsenJames R. Ketudat CairnsSuranaree University of TechnologyHokkaido Agricultural Research Center, NAROMahidol UniversityVirginia Polytechnic Institute and State University2018-07-242018-07-242004-04-01Biochemical Journal. Vol.379, No.1 (2004), 125-131026460212-s2.0-1842866212https://repository.li.mahidol.ac.th/handle/20.500.14594/21204The 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.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyArticleSCOPUS10.1042/BJ20031485