STUDIES ON TRANSGLYCOSYLATION OF CELLOBIOSE BY PARTIALLY PURIFIED TRICHODERMA VIRIDE β-GLUCOSIDASE

Abstract

In order to obtain enzyme catalyzing regioselective β-glucosyl transfer to hydroxyl group on sugar acceptor, β-glucosidase, which was active in producing trisaccharide from cellobiose, was fractionated from a Trichoderma viride (T. viride) cellulase complex by chromatographic methods. In the transglycosylation with excess of cellobiose as an initial substrate, the β-glucosidase exhibited not only cellobiose hydrolysis but also conversion of the cellobiose into Glcβ(1→6)Glcβ(1→4)Glc and Glcβ(1→6)Glc β(1→6)Glcβ(1→4)Glc. The β-glucosidase catalyzed the high regio- and stereoselective glucosyl transfer to C-6 position of non-reducing end of the acceptor, and thus could be expected to apply to syntheses of functional carbohydrates.