Purification and characterization of the thermostable protease produced by Serratia grimesii isolated from channel catfish.

摘要: Microbial spoilage of fishery products accounts for significant financial losses, yearly on a global scale. Psychrotrophic bacteria often secrete extracellular enzymes to break down surrounding fish tissue, rendering the product unsuitable human consumption. For better understanding bacterial due enzymatic digestion products, proteases in Serratia grimesii isolated from North American catfish fillets (Ictalurus punctatus) were investigated. RESULTS Mass spectrometric evidence demonstrated that S. secretes two distinct and one lipase. Protease secretion displayed broad thermostability 30?90 °C range. The major protease-secretion (O-1) was most active under alkaline conditions utilized manganese as co-factor. Organic solvents significantly disrupted efficacy and, series bactericidal detergents, protease activity highest when treated with Triton X-100. Ethylenediaminetetraacetic acid (EDTA) phenylmethylsulfonyl fluoride (PMSF) inhibited enzyme activity, while moderately stable freeze?thaw refrigerated storage. CONCLUSION influence spoilage-related enzymes, depending various factors, is discussed this paper. This study will provide new insight into its control, which can be exploited enhance food safety shelf-life worldwide. ? 2018 Society Chemical Industry