Purification and Some Properties of a Novel α-Amylase Produced by a Strain of Thermoactinomyces vulgaris
Purification and Some Properties of a Novel α-Amylase Produced by a Strain of Thermoactinomyces vulgaris
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一株普通嗜热放线菌生产的新型α-淀粉酶的纯化及部分性质
DOI：
10.1271/bbb1961.42.1681
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发表时间：
1978
期刊：
影响因子：
--
通讯作者：
M. Suekane
中科院分区：
文献类型：
--
作者：
M. Shimizu;M. Kanno;M. Tamura;M. Suekane
α-淀粉酶[α-1，4-葡聚糖4-葡聚糖水解酶，EC 3.2.1.1.]，在普通高温放线菌菌株的培养滤液中发现，通过硫酸铵分级分离和DEAE-纤维素和CM-纤维素层析纯化。纯化后的酶在盘状凝胶电泳上呈单一条带。最佳反应pH和温度被确定为约pH 5.0和70°C。等电点测定为pH 5.2。Ca ~（2+）对α-淀粉酶的稳定性有一定的影响，该α-淀粉酶能将普鲁兰糖水解为潘糖。因此，该酶的水解模式不同于支链淀粉酶和异支链淀粉酶。
An α-amylase[α-l,4-glucan 4-glucanohydrolase, EC 3.2.1.1.], found in the culture filtrate of a strain of Thermoactinomyces vulgaris, was purified by ammonium sulfate fractionation, and DEAE-cellulose and CM-cellulose chromatographies. The purified enzyme showed a single band on disc gel electrophoresis. The optimum reaction pH and temperature were determined to be around pH 5.0 and 70°C. The isoelectric point was determined to be pH 5.2. The α-amylase was stabilized by Ca2+.The α-amylase was found to hydrolyze pullulan to panose. Therefore, the hydrolytic pattern of this enzyme is different from those of pullulanase and isopullulanase.