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Bioresour Technol. 2008 Sep;99(13):5679-86. Epub 2007 Nov 26.

Purification and characterization of three novel keratinolytic metalloproteases produced by Chryseobacterium indologenes TKU014 in a shrimp shell powder medium.

Author information

1
Graduate Institute of Life Sciences, Tamkang University, Taipei 251, Taiwan. sabulo@mail.tku.edu.tw

Abstract

A protease-producing bacterium was isolated and identified as Chryseobacterium indologenes TKU014. The optimized condition for protease production was found when the culture was shaken at 30 degrees C for one day in 50 mL of medium containing 0.5% shrimp shell powder (w/v), 0.1% K(2)HPO(4), and 0.05% MgSO(4).7H(2)O. Three extracellular proteases (P1, P2, and P3) were purified from culture by DEAE-Sepharose and Phenyl Sepharose chromatography. Three enzymes all showed activities of keratinase and elastase with molecular weights of 56, 40, 40 kDa, respectively. The inhibitory effect of metal chelator EDTA and Zn-specific chelator 1,10-phenanthroline characterized three enzymes as Zn-metalloproteases. Peptide mass fingerprints of P1, P2, and P3 were determined by using liquid chromatography-tandem mass spectrometry (LC-MS/MS). Similarity search in the NCBI non-redundant protein sequence database revealed that three enzymes exhibited no significant homology to any other reported microbial peptides. Therefore, P1, P2, and P3 are most likely novel proteins.

PMID:
18037288
DOI:
10.1016/j.biortech.2007.10.024
[Indexed for MEDLINE]

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