A commercial cellulase from Trichoderma viride was fractionated into three
fractions, F1, F2, and F3, in order to investigate transglycosylation activ
ities. Among these fi actions, F3, which demonstrated highly hydrolytic act
ivity toward p-nitrophenyl P-D-glucopyranoside and Avicel, most effectively
catalyzed the transglycosylation of cellobiose and converted cellobiose in
to beta-Glc-(1 --> 6)-beta-glc-(1 --> 4)-Glc and beta-Glc-(1 --> 6)-beta-Gl
c-(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. (C) 1999 Elsevier Science Ltd. All rights reserved.