Partial Purification and Characterization of a Thermostable Actinomycete β-Amylase

Abstract

A thermostable amylase, possibly a β-amylase from Thermoactinomyces sp. no. 2 isolated from soil, is reported. The enzyme was purified 36-fold by acetone precipitation, ion-exchange chromatography, and Sephadex G-200 gel filtration, and the molecular weight was estimated at 31,600. The enzyme was characterized by demonstration of optimum activity at 60°C and pH 7 and by retention of 70% activity at 70°C (30 min). It was stimulated by Mn 2+ and Fe 2+ but strongly inhibited by Hg 2+ . Maltose was the only detectable product of hydrolysis of starches and was quantitatively highest in plantain starch hydrolysate.