Purification, characterization, and structural elucidation of serralysin-like alkaline metalloprotease from a novel source.

ABSTRACT:

Background

Serratiopeptidase is an alkaline metalloendopeptidase, which acquired wide significance because of its therapeutic applications. The present study was undertaken for purification, characterization, and structural elucidation of serratiopeptidase produced from Streptomyces hydrogenans var. MGS13.

Result

The crude enzyme was purified by precipitating with ammonium sulfate, dialysis, and Sephadex gel filtration, resulting in 34% recovery with a 12% purification fold. The purified enzyme S.AMP13 was spotted as a single clear hydrolytic band on casein zymogram and whose molecular weight was found to be 32 kDa by SDS-PAGE. The inhibitor and stability studies revealed that this enzyme is metalloprotease, thermostable, and alkaline in nature. The maximum serratiopeptidase

SUBMITTER: Nageswara S 

PROVIDER: S-EPMC6821148 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature