Abstract
A commercial cellulase from Trichoderma viride was fractionated into three fractions, F1, F2, and F3, in order to investigate transglycosylation activities. Among these fractions, F3, which demonstrated highly hydrolytic activity toward p-nitrophenyl β- d-glucopyranoside and Avicel, most effectively catalyzed the transglycosylation of cellobiose and converted cellobiose into β-Glc-(1→6)-β-glc-(1→4)-Glc and β-Glc-(1→6)-β-Glc-(1→6)-β-Glc(1→4)-Glc. The F3 fraction contained the enzyme to catalyze β-glucosyl transfer toward only the C-6 position of the sugar acceptor, and thus it is expected to be of use for syntheses of functional oligosaccharides.
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