Biochemical and molecular characterization of novel keratinolytic protease from Bacillus licheniformis (KRLr1).

ABSTRACT: The keratin-degrading bacterium Bacillus licheniformis secretes a keratinase with potential industrial interest. Here, the Keratinase gene was intracellularly expressed in Escherichia coli BL21(DE3) using pET-21b (+) vector. Phylogenetic tree analysis showed that KRLr1 is closely related to Bacillus licheniformis keratinase that belongs to the serine peptidase/subtilisin-like S8 family. Recombinant keratinase appeared on the SDS-PAGE gel with a band of about 38 kDa and was confirmed by western blotting. Expressed KRLr1 was purified by Ni-NTA affinity chromatography with a yield of 85.96% and then refolded. It was found that this enzyme has optimum activity at pH 6 and 37°C. PMSF inhibited the KRLr1 activity and Ca²⁺ and Mg²⁺ increased the KRLr1 ac

SUBMITTER: Rahimnahal S 

PROVIDER: S-EPMC10206251 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature