The α-amylase of the beetle Callosobruchus chinensis. Purification and action pattern

Abstract

Callosobruchus chinensis larval amylase was isolated and purified in five steps, which included co-precipitation with glycogen and column chromatography on ECTEOLA-cellulose. The enzyme was homogeneous by disc gel electrophoresis on polyacrylamide. The α-amylase nature was evidenced by the action on amylopectin β-amylase limit-dextrin, by the effect on the substrate–iodine complex and by the action pattern on several polysaccharide substrates. These action patterns are compared with those of other α-amylases.