Gene cloning and heterologous expression of a serine protease from Streptomyces fradiae var.k11

文献类型： 外文期刊

第一作者： Meng, Kun

作者： Meng, Kun;Li, Jiang;Cao, Yanan;Shi, Pengjun;Wu, Bo;Han, Xiaoyu;Bai, Yingguo;Wu, Ningfeng;Yao, Bin

作者机构：

关键词： Streptomyces fradiae var.k 11;keratiriases;expression

期刊名称：CANADIAN JOURNAL OF MICROBIOLOGY （ 影响因子：2.419； 五年影响因子：2.35 ）

ISSN： 0008-4166

年卷期： 2007 年 53 卷 2 期

页码：

收录情况： SCI

摘要： The gene sfpl, which encodes a predicted serine proteinase designated SFP1, was isolated by the screening of a gene library of the feather-degrading strain Streptomyces fradiae var.k11. The open reading frame of sfpl encodes a protein of 454 amino acids with a calculated molecular mass of 46.19 kDa. Sequence analysis reveals that SFP1 possesses a typical pre-pro-mature organization that consists of a signal sequence, an N-terminal propeptide region, and a mature proteinase domain. The pre-enzyme of SFP1 was expressed in Escherichia coli and consequently purified. The 25.6 kDa fraction with protease activity separated by gel filtration chromatography indicated that the mature enzyme of SFP1 was formed by autolysis of the propeptide after its expression. The purified SFP1 is active under a broad range of pH and temperature. SFP1 has pH and temperature optima of pH 8.5 and 65 degrees C for its caseinolytic activity and pH 9 and 62 degrees C for its keratinolytic activity. SFP1 was sharply inhibited by the serine proteinase inhibitor phenylmethyl sulfonyl fluoride and exhibited a good stability to solvents, detergents, and salts. Comparison of the protease activity of SFP1 with other commercial proteases indicates that SFP1 has a considerable caseinolytic and keratinolytic activity as does proteinase K.

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