Structural Characterization Reveals the Keratinolytic Activity of an Arthrobacter nicotinovorans Protease
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چکیده
منابع مشابه
Characterization of the keratinolytic activity of indigenous Bacillus subtilis keratinase
Keratins are water insoluble proteins of our environment. Being extremely resistant to degradation by proteolytic enzymes, keratins are digested mainly by alkali and keratinase enzymes. The aim of present study was to characterize the indigenous keratinase for potentials of keratin-degrading activities. We report the purification and characterization of keratinase from Bacillus subtilis isolate...
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Nicotine catabolism by Arthrobacter nicotinovorans is linked to the presence of the megaplasmid pAO1. Genes involved in this catabolic pathway are arranged on the plasmid into gene modules according to function. During nicotine degradation gamma-N-methylaminobutyrate is formed from the pyrrolidine ring of nicotine. Analysis of the pAO1 open reading frames (ORF) resulted in identification of the...
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Proteases are catabolic enzymes that catalyze the complete hydrolysis of protein. They constitute one of the most important groups of industrial enzymes, accounting for nearly 60% of the total worldwide enzyme sale1. Keratinolytic protease is a specific protease that has immense commercial importance. It acts on keratin of the hides thus can be used in dehairing2. This enzyme along with proteas...
متن کاملTemplate Synthesis, Structural Characterization and Antibacterial Activity of an Unsymmetrical Tridentate Schiff Base Nickel(II) Complex
Nickel(II) complex of [NiL2](ClO4)2, where L is an unsymmetrical tridentate ligand of 2-(2-aminoethyl)imino-3-butanone oximehas been synthesized by a template condensation reaction. The complex was characterized on the basis of microanalytical, spectroscopic, and other physicochemical properties. X-ray diffraction study of the complex revea...
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ژورنال
عنوان ژورنال: Protein & Peptide Letters
سال: 2014
ISSN: 0929-8665
DOI: 10.2174/0929866521666140919100851