Abstract
A keratinolytic enzyme produced by Bacillus subtilis KS-1 isolated from poultry waste was purified and characterized using ultrafiltration, DEAE-Sephadex, and Sephadex G-100 chromatographies. The specific activity of the purified protease was 538.2 units/mg. The enzyme was shown to have a relative molecular mass of 25.4 kDa. The enzyme was made completely inactive by PMSF, which indicates a serine-protease. Dithiothreitol enhanced keratinolytic activity by 1.6 times at a concentration of 5.0 mM. These results suggest that the cleavage of the disulfide bonds with reducing agents can occur directly or by excretion of sulfite, which causes the sulfitolysis of the disulfide bonds. The first 10 amino acids of the N-terminal sequence are Ala-Gin-Pro-Val-Glu-Trp-Gly-Ile-Ser-Gln. The enzyme hydrolyzed casein and feather, but hydrolyzed casein more effectively than it did feather.
| Original language | English |
|---|---|
| Pages (from-to) | 165-169 |
| Number of pages | 5 |
| Journal | Journal of Protein Chemistry |
| Volume | 20 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2001 Sep 21 |
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Keywords
- Bacillus subtilis
- Keratinolytic activity
- Serine-protease
ASJC Scopus subject areas
- Biochemistry
Cite this
Characterization of a keratinolytic serine protease from Bacillus subtilis KS-1. / Suh, Hyung Joo; Lee, Hyo K.
In: Journal of Protein Chemistry, Vol. 20, No. 2, 21.09.2001, p. 165-169.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Characterization of a keratinolytic serine protease from Bacillus subtilis KS-1
AU - Suh, Hyung Joo
AU - Lee, Hyo K.
PY - 2001/9/21
Y1 - 2001/9/21
N2 - A keratinolytic enzyme produced by Bacillus subtilis KS-1 isolated from poultry waste was purified and characterized using ultrafiltration, DEAE-Sephadex, and Sephadex G-100 chromatographies. The specific activity of the purified protease was 538.2 units/mg. The enzyme was shown to have a relative molecular mass of 25.4 kDa. The enzyme was made completely inactive by PMSF, which indicates a serine-protease. Dithiothreitol enhanced keratinolytic activity by 1.6 times at a concentration of 5.0 mM. These results suggest that the cleavage of the disulfide bonds with reducing agents can occur directly or by excretion of sulfite, which causes the sulfitolysis of the disulfide bonds. The first 10 amino acids of the N-terminal sequence are Ala-Gin-Pro-Val-Glu-Trp-Gly-Ile-Ser-Gln. The enzyme hydrolyzed casein and feather, but hydrolyzed casein more effectively than it did feather.
AB - A keratinolytic enzyme produced by Bacillus subtilis KS-1 isolated from poultry waste was purified and characterized using ultrafiltration, DEAE-Sephadex, and Sephadex G-100 chromatographies. The specific activity of the purified protease was 538.2 units/mg. The enzyme was shown to have a relative molecular mass of 25.4 kDa. The enzyme was made completely inactive by PMSF, which indicates a serine-protease. Dithiothreitol enhanced keratinolytic activity by 1.6 times at a concentration of 5.0 mM. These results suggest that the cleavage of the disulfide bonds with reducing agents can occur directly or by excretion of sulfite, which causes the sulfitolysis of the disulfide bonds. The first 10 amino acids of the N-terminal sequence are Ala-Gin-Pro-Val-Glu-Trp-Gly-Ile-Ser-Gln. The enzyme hydrolyzed casein and feather, but hydrolyzed casein more effectively than it did feather.
KW - Bacillus subtilis
KW - Keratinolytic activity
KW - Serine-protease
UR - http://www.scopus.com/inward/record.url?scp=0034851668&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034851668&partnerID=8YFLogxK
U2 - 10.1023/A:1011075707553
DO - 10.1023/A:1011075707553
M3 - Article
VL - 20
SP - 165
EP - 169
JO - The BMJ
JF - The BMJ
SN - 0730-6512
IS - 2
ER -