Abstract
α-Glucosidase was purified and crystallized from the mycelia of Mucor javanius, by procedures including extraction with urea, fractionations with acetone and polyethylene glycol 6000, successive separation on columns of Sephadex G-200 and DEAF-cellulose, and crystallization by the addition of ampholine reagent. The crystalline enzyme was homogeneous in ultracentrifugal analysis and gel electrophoresis. The purified enzyme showed a sedimentation constant of 5.6S and isoelectric point of pH 8.6. Some properties of the purified enzyme were also investigated. It was recognized that the synthesis of riboflavin α-glucoside was catalyzed by the transglucosylation activity of this α-glucosidase.
