Enhanced Production of Recombinant Thermostable Keratinase of Bacillus pumilus KS12: Degradation of Sup35 NM Aggregates
نویسندگان
چکیده
منابع مشابه
Biochemical Characterization of a Thiol-Activated, Oxidation Stable Keratinase from Bacillus pumilus KS12
An extracellular keratinase from Bacillus pumilus KS12 was purified by DEAE ion exchange chromatography. It was a 45 kDa monomer as determined by SDS PAGE analysis. It was found to be an alkaline, serine protease with pH and temperature optima of 10 and 60°C, respectively. It was thiol activated with two- and eight-fold enhancement in presence of 10 mM DTT and β-mercaptoethanol, respectively. I...
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results the pcr approved the bacillus genus of the isolates. the strain of bacillus subtilis was identified using biochemical tests. 40 ºc and ph 11 are the optimum condition for maximum keratinase enzyme activity. objectives the aim of this study was the isolation of feather degrading bacillus spp.from a poultry waste and the optimization of conditions for the highest enzyme activity and feath...
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ژورنال
عنوان ژورنال: Research Journal of Microbiology
سال: 2011
ISSN: 1816-4935
DOI: 10.3923/jm.2011.839.850