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酵母细胞外酸性蛋白酶的部分纯化及特性研究

Partial purification and characterization of a yeast extracellular acid protease.

作者信息

Alessandro M, Federico F

出版信息

J Dairy Sci. 1980 Sep;63(9):1397-402. doi: 10.3168/jds.S0022-0302(80)83096-7.

DOI:10.3168/jds.S0022-0302(80)83096-7
PMID:6776173
Abstract

During screening of 143 yeasts for proteolytic milk coagulating activity, a strain belonging to the species Cryptococcus albidus var. aerius was found which produced extracellular protease in shake culture. An enzyme preparation was obtained from the cell-free broth by ammonium sulphate precipitation. It possessed an optimum pH for milk-clotting at 5.5 to 5.7 at 35 degrees C. Maximum stability occurred between pH 3.5 and 5.5. The optimum temperature for the enzyme was 45 degrees C. Activity of the enzyme was inhibited by copper+2, iron+2, and mercury+2 ions.

摘要

在对143株酵母进行蛋白水解凝乳活性筛选的过程中,发现了一株属于浅白隐球酵母空气变种的菌株,该菌株在摇瓶培养中能产生胞外蛋白酶。通过硫酸铵沉淀从无细胞培养液中获得了一种酶制剂。它在35℃时使牛奶凝固的最适pH值为5.5至5.7。在pH 3.5至5.5之间稳定性最高。该酶的最适温度为45℃。该酶的活性受到铜离子、亚铁离子和汞离子的抑制。

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