Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/58444
Type: Artigo de periódico
Title: Purification and characterization of a keratinolytic metalloprotease from Chryseobacterium sp kr6
Author: Riffel, A
Brandelli, A
Bellato, CD
Souza, GHMF
Eberlin, MN
Tavares, FCA
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 degrees C, respectively. The inhibitory effect of EDTA, EGTA and 1, 10-phenanthroline characterized Q I 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 M 14 metalloprotease family, with a consensus glycosylation region similar to proteins from Chryseobacerium meningosepticum. (c) 2006 Elsevier B.V. All rights reserved.
Subject: Chryseobacterium
keratinase
metalloprotease
M14 carboxypeptidase A family
Country: Holanda
Editor: Elsevier Science Bv
Rights: fechado
Identifier DOI: 10.1016/j.jbiotec.2006.11.007
Date Issue: 2007
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File Description SizeFormat 
WOS000244404400025.pdf467.31 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.