| Purification and Characterization of An Alkaline Protease from Acetes chinensis |
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| 作者姓名： | XU Jiachao LIU Xin LI Zhaojie XU Jie XUE Changhu GAO Xin |
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| 作者单位： | College of Food Science and Engineering, Ocean University of China, Qingdao 266003, P. R. China |
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| 基金项目： | the National Key Technology R & D Program，国家高技术研究发展计划(863计划)，教育部留学回国人员科研启动基金 |
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| 摘 要： | An alkaline protease from Acetes chinensis was purified and characterized in this study. The steps of purification include ammonium sulfate precipitation, ion-exchange chromatography with Q-sepharose Fast Flow, gel filtration chromatography with S300 and the second ion-exchange chromatography with Q-sepharose Fast Flow. The protease was isolated and purified, which was present and active on protein substrates （azocasein and casein）. The specific protease activity was 17.15 folds and the recovery was 4.67. The molecular weight of the protease was estimated at 23.2kD by SDS-PAGE. With azocasein as the susbstrate, the optimal temperature was 55℃ and the optimal pH value was 5.5. Ion Ca^2＋ could enhance the proteolytic activity of the protease, while Cu^2＋, EDTA and PMSF could inhibit its activity.
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| 关 键 词： | 蛋白酶 中国 渤海 营养需要 鱼类 |
| 文章编号： | 1672-5182（2005）03-257-05 |
| 收稿时间： | 2005-04-04 |
| 修稿时间： | 2005-06-04 |
Purification and Characterization of An Alkaline Protease from Acetes chinensis |
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| XU Jiachao LIU Xin LI Zhaojie XU Jie XUE Changhu GAO Xin.Purification and Characterization of An Alkaline Protease from Acetes chinensis[J].Journal of Ocean University of China,2005,4(3):257-261. |
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| Authors: | XU Jiachao LIU Xin Li Zhaojie XU Jie XUE Changhu GAO Xin |
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| Abstract: | An alkaline protease from Acetes chinensis was purified and characterized in this study. The steps of purification include ammonium sulfate precipitation, ion-exchange chromatography with Q-sepharose Fast Flow, gel filtration chromatography with S300 and the second ion-exchange chromatography with Q-sepharose Fast Flow. The protease was isolated and purified, which was present and active on protein substrates (azocasein and casein). The specific protease activity was 17.15folds and the recovery was 4.67. The molecular weight of the protease was estimated at 23.2 kD by SDS-PAGE. With azocasein as the susbstrate, the optimal temperature was 55 ℃ and the optimal pH value was 5.5. Ion Ca2+ could enhance the proteolytic activity of the protease, while Cu2+ , EDTA and PMSF could inhibit its activity. |
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| Keywords: | Acetes chinensis protease purification characterization |
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