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

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

doi:10.1385/ABAB:97:2:123

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

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

Research output: Contribution to journal › Article › peer-review

47 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 language	English
Pages (from-to)	123-133
Number of pages	11
Journal	Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology
Volume	97
Issue number	2
DOIs	https://doi.org/10.1385/ABAB:97:2:123
Publication status	Published - 2002

Keywords

Bacillus sp.
Keratinolytic activity
Metalloprotease

ASJC Scopus subject areas

Biotechnology
Bioengineering
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology

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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.",

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AU - Suh, D. B.

AU - Hwang, J. H.

AU - Suh, H. J.

PY - 2002

Y1 - 2002

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AB - 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.

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

Abstract

Keywords

ASJC Scopus subject areas

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