Affiliation:
1. Department of Bacteriology, Iowa State University, Ames, Iowa 50010
Abstract
Halobacterium halobium
amylase had optimal activity at
p
H 6.4 to 6.6 in sodium β-glycerophosphate buffer containing 0.05% NaCl at 55 C; Ca
2+
was not required. End products from amylose were maltose, maltotriose, and glucose. The amylase, which was devoid of transglucosylase activity, had a multichain attack mechanism.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
64 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献