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Transglycosylation of cellobiose by partially purified Trichoderma viride cellulase
H Kono1, M R Waelchli, M Fujiwara
1Division of Molecular Chemistry, Graduate School of Engineering, Hokkaido University, Sapporo, Japan. kohno@dove-mc.eng.hokudai.ac.jp
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 beta-D-glucopyranoside and Avicel, most effectively catalyzed the transglycosylation of cellobiose and converted cellobiose into beta-Glc-(1-->6)-beta-glc-(1-->4)-Glc and beta-Glc-(1-->6)-beta-Glc-(1-->6)-beta-Glc(1-->4)-Glc. The F3 fraction contained the enzyme to catalyze beta-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.