Purification and characterization of thermoactive serratiopeptidase from Serratia marcescens AD-W2
نویسندگان
چکیده
منابع مشابه
Purification 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...
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Serratia marcescens isolated from raw milk was found to produce extracellular lipase. The growth of this organism could contribute to flavor defects in milk and dairy products. Serratia marcescens was streaked onto spirit blue agar medium, and lipolytic activity was detected after 6 h at 30 degrees C and after 12 h at 6 degrees C. The extracellular crude lipase was collected after inoculation o...
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An extracellular, nonelastolytic, neutral metalloprotease of Serratia marcescens was purified by sequential ammonium sulfate precipitation, hydroxyapatite adsorption chromatography, flat-bed isoelectric focusing, and Sephadex G-100 gel filtration. The protease preparation had a 280/260 nm absorbance ratio of 1.8, was free of detectable amounts of endotoxin, carbohydrate, phosphorus, and other k...
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The purification and properties of a tumor inhibitory l-asparaginase from Serratia marcescens are described. The following properties of the enzyme were examined: kinetics of the enzyme reaction, catalytic activity as a function of pH, boundary sedimentation velocity, electrophoresis on polyacrylamide gel, immuno-electrophoresis against homologous and heterologous antisera, immunodiffusion, blo...
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ژورنال
عنوان ژورنال: AMB Express
سال: 2021
ISSN: 2191-0855
DOI: 10.1186/s13568-021-01215-7