Redox and solvent-stable alkaline serine protease from <i>Bacillus patagoniensis</i> DB-5: heterologous expression, properties, and biotechnological applications.

ABSTRACT: 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 Ca²⁺ significantly enhanced the optimal temperature and thermostability. The enzyme demonstrated optimum activity at pH 12 and maintained high stability at pH 8.0-11.0. Protease activity was stimulated by Mn²⁺, Ca²⁺, Mg²

SUBMITTER: Li Z 

PROVIDER: S-EPMC11970705 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature