Abstract
Gelatin extracted from fish skin was used as an expedient substrate and a vital source of protein to assess the efficient production of gelatinase by Serratia marcescens MF599353 over hydrolysis of the gelatin. During the growth of the organism, a pigment called prodigiosin was produced, and its molecular weight was determined to be 324Da by ESI-MS and further characterized by FTIR. Using the OFT (one-factor at-a-time) approach, various parameters such as time, pH, temperature, gelatin, and yeast extract concentration were optimized for gelatinase activity. The molecular weight of purified gelatinase was determined to be 44 kDa using SDS-PAGE. Thus, the cultivation of Serratia marcescens MF599353 under optimized conditions could enhance the gelatinase production and its potential applicability at industrial scale.
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