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Appl Environ Microbiol. 1992 October; 58(10): 3271-3275
Copyright © 1992, American Society for Microbiology. All Rights Reserved.

Purification and Characterization of a Keratinase from a Feather-Degrading Bacillus licheniformis Strain

Xiang Lin{dagger}, Chung-Ginn Lee{ddagger}, Ellen S. Casale and Jason C. H. Shih*

Department of Poultry Science and University Biotechnology Program, North Carolina State University, Raleigh, North Carolina 27695-7608

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.

FOOTNOTES

* Corresponding author.

{dagger} Permanent address: Shenyang Agricultural University, Shenyang, Liaoning, People's Republic of China.

{ddagger} Present address: Department of Animal Production, Council of Agriculture, Taipei, Taiwan, Republic of China.

Appl Environ Microbiol. 1992 October; 58(10): 3271-3275
Copyright © 1992, American Society for Microbiology. All Rights Reserved.



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