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首页> 外文期刊>Applied Microbiology >Characteristics of a Proteinase of a Trichosporon Species Isolated from Dungeness Crab Meat
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Characteristics of a Proteinase of a Trichosporon Species Isolated from Dungeness Crab Meat

机译：从太平洋大蟹肉中分离到的一种毛孢菌属蛋白酶的特征

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The proteinase of a Trichosporon species was partially purified by dialysis, ammonium sulfate fractionation, and Sephadex G-100 gel filtration. A 170-fold purification of the enzyme with a 1.4% recovery of the activity was achieved. The proteinase was separated into a major component and possibly two minor components by starch gel electrophoresis. The pH optimum of the enzyme was 5.8 to 6.2. It was active against casein, hemoglobin, and crab protein substrates, but inactive against bovine serum albumin, lysozyme, and benzoylarginine ethyl ester. It was slightly activated by 10 mm cysteine, 0.1 mm ethylenediaminetetraacetic acid, and 0.1 mm Co++. There was slight inhibition by 10 mm Co++ and 0.1 mm phenylmethylsulfonylfluoride, and total inhibition by 1 mmp-chloromercuribenzoate. The proteinase was completely inactivated by heating at 60 C for 10 min.
机译：通过透析，硫酸铵分级分离和Sephadex G-100凝胶过滤，部分纯化了曲孢菌属的蛋白酶。实现了酶的170倍纯化，活性回收率为1.4％。通过淀粉凝胶电泳将蛋白酶分为主要成分和可能的两个次要成分。该酶的最适pH为5.8至6.2。它对酪蛋白，血红蛋白和螃蟹蛋白底物有活性，但对牛血清白蛋白，溶菌酶和苯甲酰精氨酸乙酯没有活性。它被10毫米半胱氨酸，0.1毫米乙二胺四乙酸和0.1毫米Co ++轻微活化。 10 mm Co ++和0.1 mm苯基甲基磺酰氟略有抑制作用，而1 mmp-氯汞基苯甲酸酯则总抑制作用。通过在60℃加热10分钟使蛋白酶完全失活。

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