Heterologous expression, purification, and biochemical characterization of protease 3075 from Cohnella sp. A01.

ABSTRACT: Proteases as one of the most significant categories of commercial enzymes, serve nowadays as the key ingredients in detergent formulations. Therefore, identifying detergent-compatible proteases with better properties is a continuous exercise. Accordingly, we were interested in the recombinant production and characterization of protease 3075 as a novel enzyme from thermophilic indigenous Cohnella sp. A01. The biochemical and structural features of the protease were probed by employing bioinformatic methods and in vitro studies. The bioinformatics analysis discovered that protease 3075 belongs to the C56-PfpI superfamily. The protease 3075 gene was cloned and heterologous expressed in Escherichia coli (E. coli) BL21. It was found that the enzyme contains 175 amino acids and 525 bp with a mol

SUBMITTER: Hashemi Shahraki F 

PROVIDER: S-EPMC11649109 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature