Abstract
α-Glucosidase (EC 3.2.1.20) from Trichoderma viride was purified by a procedure including Sephacryl S-200 HR column chromatography, preparative isoelectric focusing, and Superdex 200 HR column chromatography. The enzyme was found to have an apparent molecular weight of 67, 000 on SDS/PAGE and 65, 000 on gelfiltration, showing that the enzyme is a single peptide. The isoelectric point of the enzyme was 5.0. The enzyme hydrolyzed α-1, 4-glucosidic linkage more rapidly than α-1, 6-glucosidic and α-1, 3-glucosidic link-ages. The enzyme was weakly inhibited by castanospermine.
