Expression, purification, and characterization of a thermophilic neutral protease from Bacillus stearothermophilus in Bacillus subtilis |
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| Authors: | Min Zhang Cong Zhao LianXiang Du FuPing Lu Chen Gao |
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| Institution: | (1) College of Engineering, Shenyang Agricultural University, Shenyang, 110161, China;(2) College of Biotechnology, Tianjin University of Science and Technology, Tianjin, 300457, China;(3) College of Life Science, Nankai University, Tianjin, 300071, China |
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| Abstract: | The gene coding for a thermophilic neutral protease from Bacillus stearothermophilus was expressed in Bacillus subtilis DB104, under the control of the sacB gene promoter. This was followed by either the native signal peptide sequence of this protease or the signal peptide sequence
of the sacB gene. The protease was purified 3.8-fold, with a specific activity of 16530 U mg−1. As analyzed by SDS-PAGE, the molecular mass of the expressed protease was about 35 kDa, and the optimal temperature and
pH of the protease were 65°C and 7.5, respectively. Moreover, it still had about 80% activity after 1 h reaction at 65 °C.
Supported by the “863” High-Tech Research Project of China (Grant No. 2007AA 02Z212) |
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| Keywords: | Bacillus subtilis thermophilic neutral protease expression purification characterization |
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