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• W1520821142 endingPage "3275" @default.
• W1520821142 startingPage "3271" @default.
• W1520821142 abstract "A keratinase was isolated from the culture medium of feather-degrading Bacillus licheniformis PWD-1 by use of an assay of the hydrolysis of azokeratin. Membrane ultrafiltration and carboxymethyl cellulose ion-exchange and Sephadex G-75 gel chromatographies were used to purify the enzyme. The specific activity of the purified keratinase relative to that in the original medium was approximately 70-fold. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis and Sephadex G-75 chromatography indicated that the purified keratinase is monomeric and has a molecular mass of 33 kDa. The optimum pH and the pI were determined to be 7.5 and 7.25, respectively. Under standard assay conditions, the apparent temperature optimum was 50°C. The enzyme is stable when stored at −20°C. The purified keratinase hydrolyzes a broad range of substrates and displays higher proteolytic activity than most proteases. In practical applications, keratinase is a useful enzyme for promoting the hydrolysis of feather keratin and improving the digestibility of feather meal." @default.
• W1520821142 created "2016-06-24" @default.
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• W1520821142 date "1992-10-01" @default.
• W1520821142 modified "2023-10-18" @default.
• W1520821142 title "Purification and Characterization of a Keratinase from a Feather-Degrading <i>Bacillus licheniformis</i> Strain" @default.
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• W1520821142 doi "https://doi.org/10.1128/aem.58.10.3271-3275.1992" @default.
• W1520821142 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/183090" @default.
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• W1520821142 hasPublicationYear "1992" @default.
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