Isolation, Purification, and Characterization of Serratiopeptidase Enzyme from Serratia marcescens

Abstract

Serratiopeptidase is a proteolytic enzyme that is derived from a member of Enterobacteriaceae. Serratia marcescens is a gram-negative bacteria identified characteristically, which produces a red pigment called prodigiosin. Serratiopeptidase is a multifunctional proteolytic enzyme that dissolves non-living tissues such as fibrin, blood clots, inflammation in all forms without harming living tissues. In this study, the organism was isolated from the diseased silkworm's pupa by using Luria- Bertani (LB) agar media. The enzyme production can be enhanced by applying different physical and chemical parameters. Serratia marcescens was subjected to production such that in order to obtain the maximum level of cell-free supernatant Serratiopeptidase enzyme with all the optimized conditions. The enzyme was subjected to purification by four methods such as salt precipitation, dialysis, ion-exchange chromatography and gel filtration. When subjected to enzyme kinetics, Serratiopeptidase was active at temperature 350C, pH-9 with 8 minutes of the incubation period. The molecular weight of serratiopep