Halobacterium halobium amylase had optimal activity at pH 6.4 to 6.6 in sodium beta-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.
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Good et al. (1970) studied this question.
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