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

San Lang Wang, Wan Ting Hsu, Tzu Wen Liang, Yue Horng Yen, Chuan Lu Wang

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60 Citations (Scopus)

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 °C for one day in 50 mL of medium containing 0.5% shrimp shell powder (w/v), 0.1% K2HPO4, and 0.05% MgSO4 · 7H2O. 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.

Original languageEnglish
Pages (from-to)5679-5686
Number of pages8
JournalBioresource technology
Volume99
Issue number13
DOIs
Publication statusPublished - 2008 Sep

All Science Journal Classification (ASJC) codes

  • Bioengineering
  • Environmental Engineering
  • Renewable Energy, Sustainability and the Environment
  • Waste Management and Disposal

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