Purification and characterization of a propanol-tolerant neutral protease from Bacillus sp. ZG20 |
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Authors: | Ping Yu Xinxin Wang Xingxing Huang Qian Ren Tingting Yan |
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Affiliation: | 1. College of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou, People’s Republic of Chinayup9202@hotmail.com;3. College of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou, People’s Republic of China |
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Abstract: | AbstractA propanol-tolerant neutral protease was purified and characterized from Bacillus sp. ZG20 in this study. This protease was purified to homogeneity with a specific activity of 26,655?U/mg. The recovery rate and purification fold of the protease were 13.7% and 31.5, respectively. The SDS-PAGE results showed that the molecular weight of the protease was about 29?kDa. The optimal temperature and pH of the protease were 45?°C and 7.0, respectively. The protease exhibited a good thermal- and pH stability, and was tolerant to 50% propanol. Mg2+, Zn2+, K+, Na+ and Tween-80 could improve its activity. The calculated Km and Vmax values of the protease towards α-casein were 12.74?mg/mL and 28.57?µg/(min mL), respectively. This study lays a good foundation for the future use of the neutral protease from Bacillus sp. ZG20. |
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Keywords: | Bacillus sp. ZG20 characterization neutral protease purification |
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