Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/104682
Type: Artigo de periódico
Title: Purification And Characterization Of A Keratinolytic Metalloprotease From Chryseobacterium Sp. Kr6
Author: Riffel A.
Brandelli A.
Bellato C.d.M.
Souza G.H.M.F.
Eberlin M.N.
Tavares F.C.A.
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. © 2006 Elsevier B.V. All rights reserved.
Editor: 
Rights: fechado
Identifier DOI: 10.1016/j.jbiotec.2006.11.007
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-33846431239&partnerID=40&md5=22b9e3b5fbb05186fd9146be0392850b
Date Issue: 2007
Appears in Collections:Unicamp - Artigos e Outros Documentos

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