Purification and Some Properties of a Novel α-Amylase Produced by a Strain of Thermoactinomyces vulgaris
- 1 September 1978
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 42 (9), 1681-1688
- https://doi.org/10.1080/00021369.1978.10863231
Abstract
An α-amylase[α-l,4-glucan 4-glucanohydrolase, EC 3.2.1.1.], found in the culture filtrate of a strain of Thermoactinomyces vulgaris, was purified by ammonium sulfate fractionation, and DEAE-cellulose and CM-cellulose chromatographies. The purified enzyme showed a single band on disc gel electrophoresis. The optimum reaction pH and temperature were determined to be around pH 5.0 and 70°C. The isoelectric point was determined to be pH 5.2. The α-amylase was stabilized by Ca2+. The α-amylase was found to hydrolyze pullulan to panose. Therefore, the hydrolytic pattern of this enzyme is different from those of pullulanase and isopullulanase.This publication has 1 reference indexed in Scilit:
- Classification of Amylases in α- or β- Type according to Mutarotation of Fission ProductsJournal of the agricultural chemical society of Japan, 1952