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首页> 外文期刊>Biochemistry >Purification and Characterization of a Subtilisin-Like Proteinases Secreted in the Stationary Growth Phase of Bacillus amyloliquefaciens H2
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Purification and Characterization of a Subtilisin-Like Proteinases Secreted in the Stationary Growth Phase of Bacillus amyloliquefaciens H2

机译：淀粉芽孢杆菌H2固定生长阶段分泌的枯草杆菌蛋白酶样蛋白酶的纯化和鉴定。

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摘要

Proteinases secreted during the early and late stationary phases have been isolated from the culture liquid of Bacillus amyloliquefaciens H2 using CM-cellulose ion-exchange chromatography with subsequent FPLC on a Mono S column. Considering the character of hydrolysis of specific chromogenic substrates and the type of inhibition, these enzymes were identified as subtilisin-like proteinases. The molecular weight of both proteinases is 29 kD. The proteolytic activity of the proteinases secreted during the early and late stationary phases towards the synthetic substrate Z-Ala-Ala-Leu-pNA was maximal at pH 8.5 and 9.0, respectively. The maximal activity of both proteinases was observed at 37°C, and the proteins were stable within the pH range of 7.2-9.5. The subtilisin-like proteinases from B. amyloliquefaciens were shown to catalyze synthesis of peptide bonds.
机译：使用CM-纤维素离子交换色谱和随后的FPLC在Mono S色谱柱上，从解淀粉芽孢杆菌H2的培养液中分离出了早期和晚期稳定期分泌的蛋白酶。考虑到特定生色底物的水解特性和抑制类型，这些酶被鉴定为枯草杆菌蛋白酶样蛋白酶。两种蛋白酶的分子量均为29 kD。在早期和晚期固定阶段分泌的蛋白酶对合成底物Z-Ala-Ala-Leu-pNA的蛋白水解活性分别在pH 8.5和9.0时最大。在37℃下观察到两种蛋白酶的最大活性，并且这些蛋白在7.2-9.5的pH范围内是稳定的。显示出来自解淀粉芽孢杆菌的枯草杆菌蛋白酶样蛋白酶可催化肽键的合成。

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