嗜热栖热硫化叶菌α-淀粉酶和支链淀粉酶活性的表征。一种新型耐热淀粉酶的证据。
Characterization of alpha-amylase and pullulanase activities of Clostridium thermohydrosulfuricum. Evidence for a novel thermostable amylase.
作者信息
Melasniemi H
机构信息
Research Laboratories of the Finnish State Alcohol Company (Alko Ltd.), Helsinki.
出版信息
Biochem J. 1987 Aug 15;246(1):193-7. doi: 10.1042/bj2460193.
Abstract
Thermostable extracellular alpha-amylase and pullulanase activities of Clostridium thermohydrosulfuricum E 101-69 were characterized in a crude enzyme preparation. The activities responded similarly to temperature and pH, with optima at 85-90 degrees C and pH 5.6. The activities were stable at 65 degrees C, but were inactivated gradually in an identical manner at higher temperatures in the absence of Ca2+ and substrate. Ca2+ stabilized both activities similarly at high temperatures. Ca2+ also stimulated both activities, whereas EDTA reversed this stimulation. The activities were similarly inactivated at pH extremes. The two activities distributed in the same way during isoelectric focusing. The results suggest that the two activities are properties of the same protein, representing a novel, thermostable, amylase.
摘要
在粗酶制剂中对嗜热栖热硫化叶菌E 101-69的耐热性胞外α-淀粉酶和支链淀粉酶活性进行了表征。这些活性对温度和pH的响应相似，最适温度为85-90℃，最适pH为5.6。这些活性在65℃时稳定，但在没有Ca2+和底物的情况下，在较高温度下以相同方式逐渐失活。Ca2+在高温下以相似的方式稳定这两种活性。Ca2+也刺激这两种活性，而EDTA则逆转这种刺激作用。在极端pH值下，这两种活性以相似的方式失活。在等电聚焦过程中，这两种活性的分布方式相同。结果表明，这两种活性是同一蛋白质的特性，代表一种新型的耐热淀粉酶。
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