alexa Purification and Characterization of a Keratinase from a Feather-Degrading Bacillus licheniformis Strain.
Environmental Sciences

Environmental Sciences

Journal of Bioremediation & Biodegradation

Author(s): Lin X, Lee CG, Casale ES, Shih JC

Abstract Share this page

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 degrees C. The enzyme is stable when stored at -20 degrees 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.
This article was published in Appl Environ Microbiol and referenced in Journal of Bioremediation & Biodegradation

Relevant Expert PPTs

Relevant Speaker PPTs

Recommended Conferences

  • 6th World Congress on Biofuels and Bioenergy
    Sep 5-6, 2017 London, UK
  • 6th World Congress on Biopolymers
    September 7-9, 2017 Paris, France
  • 7th International Conference and Exhibition on Biopolymers and Bioplastics
    October 19-21, 2017 San Francisco, USA

Relevant Topics

Peer Reviewed Journals
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version