Journal
BIORESOURCE TECHNOLOGY
Volume 101, Issue 1, Pages 344-350Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.biortech.2009.08.026
Keywords
Keratinase; Native human foot skin; Streptomyces sp strain 16; Purification; Characterization
Funding
- National High Technology Research and Development Program of China [2006AA020204]
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Four extracellular keratinases (designated KI, KII, KIII, and KIV) were produced during submerged aerobic cultivation in a medium containing native human foot skin (NHFS) for enzyme synthesis. The molecular weights, determined by SIDS-PAGE, were 25, 50. 34, and 19 kDa, respectively. Gel filtration of the four purified enzymes in native conditions indicated that active keratinase KI is a novel homo-octamer KII, a homo-dimer, and KIII and KIV monomers. All four keratinases exhibited high activities at pH 8.0-10.0 with an optimal pH of 9.0. The optimal temperature for keratinolytic activity of KI, KII, and KIII was approximately 50, and 60 degrees C for KIV. One millimolar of PMSF completely inhibited the keratinolytic activities of the four enzymes. The N-terminal sequences of KI, KII, and KIII showed that they were different from previously described enzymes, whereas KIV shared an identical N-terminal sequence with two other peptidases from Streptomyces. (C) 2009 Elsevier Ltd. All rights reserved.
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