Partial purification and biochemical characterization of a soluble α-glucosidase II-like activity from Candida albicans

Abstract

A soluble α-glucosidase was partially purified from Candida albicans cells by a three-step procedure consisting of size-exclusion, ion-exchange and adsorption chromatographies. After the last step, enzyme was enriched about 8.7-fold with a yield of 13% over the starting material and analysis of the purified preparation revealed two major polypeptides of 36 and 47 kDa. The latter was responsible for enzyme activity as visualized with a fluorescent substrate. Nigerose, an α-1,3-linked glucose disaccharide, was preferentially hydrolyzed by the purified enzyme over other glucosedisaccharides bearing distinct α-linkages. The purified α-glucosidase also converted the GlcMan9GlcNAc2 oligosaccharide into the Man9GlcNAc2 product in a time-dependent manner. These and other determined properties are consistent with a type GII α-glucosidase probably involved in N-glycan processing. © 2004 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.