The author(s) declare that financial support was received for the research and/or publication of this article. This research was financially supported by the National Key Research and Development Program (Grant No. 2021YFC2100202).
机构署名：
本校为第一且通讯机构
院系归属：
生命科学与技术学院
摘要：
The aprBP gene from Bacillus patagoniensis DB-5, encoding a 378-amino-acid alkaline protease, was cloned and expressed in Escherichia coli. The amino acid sequence of APrBP showed 62.8-84.4% identity with the S8 peptidase subtilisin family alkaline proteases reported in the literature. Recombinant APrBP was purified using Ni-NTA affinity chromatography with 45.61% recovery and a homogeneous band was detected at approximately 38 kDa on the SDS-PAGE gel. The optimum temperature of APrBP was 60°C. The presence of 2 mM Ca(2+) significantly enhanc...
