DOI:
ABSTRACT
Halobacterium halobium amylase had optimal activity at pH 6.4 to 6.6 in sodium β-glycerophosphate buffer containing 0.05% NaCl at 55 C; Ca2+ 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.
FOOTNOTES
↵1 Journal Paper no. J-6568 of the Iowa Agriculture and Home Economics Experiment Station, Ames, Iowa. Projects no. 1485 and 1763.
- Copyright © 1970 American Society for Microbiology
