| Literature DB >> 17187889 |
Alessandro Riffel1, Adriano Brandelli, Cláudia de M Bellato, Gustavo H M F Souza, Marcos N Eberlin, Flavio C A Tavares.
Abstract
The Chryseobacterium sp. kr6 strain has been described as a highly keratinolytic bacterium showing effective feather-degrading and de-hairing activities. A keratinase Q1 enzyme was purified from Chryseobacterium sp. kr6 culture by Phenyl Sepharose and Superose 12HR chromatography. This enzyme showed a specific activity of 967U/mg for keratin azure. Electrophoresis under denaturing conditions showed a monomeric protein with approximately 64kDa. The enzyme showed pH and temperature optima of 8.5 and 50 degrees C, respectively. The inhibitory effect of EDTA, EGTA and 1,10-phenanthroline characterized Q1 enzyme as a Zn-metalloprotease. Its activity was increased by three-fold in the presence of Ca(2+). ESI-MS/MS analysis of peptides generated from a tryptic digestion revealed sequence homology which may characterize the Q1 keratinase as a member of the M14 metalloprotease family, with a consensus glycosylation region similar to proteins from Chryseobacerium meningosepticum.Entities:
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Year: 2006 PMID： 17187889 DOI： 10.1016/j.jbiotec.2006.11.007
Source DB: PubMed Journal: J Biotechnol ISSN： 0168-1656 Impact factor: 3.307