Comprehensive biochemical, molecular and structural characterization of subtilisin with fibrinolytic potential in bioprocessing.

ABSTRACT: Enzyme deployment is proliferating extensively in industries owing to their environmentally friendly and easily degradable attributes. This article undertakes an exhaustive examination of wild subtilisin enzyme, covering purification, biochemical delineation, analytical techniques, and practical implementations. The purification methodology involved partial refinement, anionic exchange, and gel filtration chromatography, culminating in a purification factor of 3.406, corroborated by SDS-PAGE showcasing a molecular weight of ~ 42 kDa. Biochemical scrutiny unveiled the enzyme's response, with an optimal pH at 9 and temperature peak at 60 ℃. Various surfactants, metal ions, organic solvents and inhibitors exhibited notable efficacy. Substrate specificity and kinetics showcased the utmost spec

SUBMITTER: Shettar SS 

PROVIDER: S-EPMC11928348 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature