Production and Characterization of Serratiopeptidase Enzyme from Serratia Marcescens
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چکیده
منابع مشابه
Production and Characterization of Protease from Serratia marcescens
Extracellular protease produced by Serratia marcescens isolated from the gut of termite (Centrocestus formosanus) was investigated in this study. The effect of temperature, pH, carbon and nitrogen sources on protease production was examined. The extracellular protease was separated from the culture supernatant of the organism through precipitation with ammonium sulfate. The protease was purifie...
متن کاملChitinases from Serratia marcescens
Serratia marcescens is one of the most effective bacteria for degradation of chitin, a 1,4-β-linked polymer of N-acetyl-β-Dglucosamine (GlcNAc). Chitinolysis by S. marcescens involves at least four enzymes and a chitin-binding protein. Studies of the enzymology and the structures of the enzymes provide insight in how a natural set of chitinolytic enzymes may be built up. S. marcescens chitinase...
متن کاملPurification and partial characterization of a bacteriocin from Serratia marcescens.
Bacteriocin JF246 has been purified from mitomycin C-induced Serratia marcescens cells by salt extraction, ammonium sulfate fractionation, and chromatography on QAE-Sephadex and SP-Sephadex. The purified material is homogeneous on polyacrylamide gel electrophoresis in the presence of 2% sodium dodecyl sulfate or 6 m urea. In the absence of these agents, the bacteriocin associates into aggregate...
متن کاملR factors from Serratia marcescens.
In recent years, Serratia marcescens has become established in certain localities as an agent of hospital infection and cross-infection (Clayton & von Graevenitz, 1966; Wilfert, Barrett & Kass, 1968; Davis, Foltz & Blakemore, 1970; Wilkowske, Washington, Martin & Ritts, 1970). In general, strains of S. marcescens isolated from infective lesions differ from those from other sources in being non-...
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ژورنال
عنوان ژورنال: International Journal of Biology
سال: 2011
ISSN: 1916-968X,1916-9671
DOI: 10.5539/ijb.v3n3p39