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Purification and characterization of a keratinolytic metalloprotease from Chryseobacterium sp. kr6

Paper ID Volume ID Publish Year Pages File Format Full-Text
25288 43564 2007 11 PDF Available
Title
Purification and characterization of a keratinolytic metalloprotease from Chryseobacterium sp. kr6
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 967 U/mg for keratin azure. Electrophoresis under denaturing conditions showed a monomeric protein with approximately 64 kDa. The enzyme showed pH and temperature optima of 8.5 and 50 °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 Ca2+. 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.

Keywords
Chryseobacterium; Keratinase; Metalloprotease; M14 carboxypeptidase A family
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Purification and characterization of a keratinolytic metalloprotease from Chryseobacterium sp. kr6
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 128, Issue 3, 20 February 2007, Pages 693–703
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
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Any Questions? feel free to contact us