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.
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