title: Partial Purification and Characterization of a Thermostable Actinomycete beta-Amylase.
abstract: A thermostable amylase, possibly a beta-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 degrees C and pH 7 and by retention of 70% activity at 70 degrees C (30 min). It was stimulated by Mn and Fe but strongly inhibited by Hg. Maltose was the only detectable product of hydrolysis of starches and was quantitatively highest in plantain starch hydrolysate.
authors.affiliation: Department of Microbiology, University of Nigeria, Nsukka, Nigeria.
authors.forename: S K
authors.initials: SK
authors.lastname: Obi
authors.forename: F J
authors.initials: FJ
authors.lastname: Odibo