Artículos de revistas
Purification and characterization of a keratinolytic metalloprotease from Chryseobacterium sp kr6
Registro en:
Journal Of Biotechnology. Elsevier Science Bv, v. 128, n. 3, n. 693, n. 703, 2007.
0168-1656
WOS:000244404400025
10.1016/j.jbiotec.2006.11.007
Autor
Riffel, A
Brandelli, A
Bellato, CD
Souza, GHMF
Eberlin, MN
Tavares, FCA
Institución
Resumen
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. 128 3 693 703