Action Pattern and Substrate Specificity of alpha‐Amylase K, a Novel Amylase from a Strain of Bacillus subtilis

Abstract

AbstractThe action pattern of α‐amylase K on amylopectin, glycogen and a number of starches is reported. It was found that the predominant component of the hydrolysis mixture was maltohexaose under most conditions with varying amounts of maltoheptaose, maltopentaose and maltotriose being present depending on the time of hydrolysis. Michaelis constants and maximum rates of reaction were determined for a number of substrates which indicated that the enzyme was most active against amylopectin. Conditions for large scale industrial use of the enzyme, including high substrate concentration and the absence of buffer from the hydrolysis mixture are discussed. A thin layer chromatographic technique for the rapid separation and identification of the hydrolysis products (up to maltodecaose) is reported.