Characterization of a keratinolytic metalloprotease from Bacillus sp. SCB-3

H. Lee, D. B. Suh, J. H. Hwang, H. J. Suh

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45 Citations (Scopus)


A keratinolytic protease-producing microorganism was isolated from soybean paste waste and was identified as a strain of Bacillus sp. The keratinase was purified by polyethylene glycol precipitation and two successive column chromatographies with DEAE-Toyopearl 650C and Sephacryl S-200 HR. The purified enzyme had overall 11 purification folds with an 18% yield. The results of sodium dodecyl sulfate polyacrylamide gel electrophoresis and gel filtration on Sephacryl G-200 indicated that the purified enzyme was monomeric and had a molecular weight of 134 kDa. The optimum temperature and pH were 40°C and 7.0, respectively. This enzyme was completely inhibited by EDTA and EGTA, and it was restored by the addition of Ca+2 and Mg+2. These results suggested that it is a metalloprotease. The stimulated enzyme activity by reducing agents indicated that the reducing condition was important in the expression of the activity.

Original languageEnglish
Pages (from-to)123-133
Number of pages11
JournalApplied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology
Issue number2
Publication statusPublished - 2002


  • Bacillus sp.
  • Keratinolytic activity
  • Metalloprotease

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology


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