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

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

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

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
Volume97
Issue number2
DOIs
Publication statusPublished - 2002 Apr 10

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Metalloproteases
Bacilli
Bacillus
Enzymes
Gels
Column chromatography
Egtazic Acid
Reducing Agents
Ethylenediaminetetraacetic acid
Enzyme activity
Sodium dodecyl sulfate
Reducing agents
Ointments
Polyacrylates
Electrophoresis
Edetic Acid
Sodium Dodecyl Sulfate
Microorganisms
Polyethylene glycols
Purification

Keywords

  • Bacillus sp.
  • Keratinolytic activity
  • Metalloprotease

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biotechnology
  • Bioengineering

Cite this

Characterization of a keratinolytic metalloprotease from Bacillus sp. SCB-3. / Lee, H.; Suh, D. B.; Hwang, J. H.; Suh, Hyung Joo.

In: Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology, Vol. 97, No. 2, 10.04.2002, p. 123-133.

Research output: Contribution to journalArticle

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