Purification anc characterization of a keratinase from a feather-degrading bacterium, Bacillus sp. SH-517

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Title
Purification anc characterization of a keratinase from a feather-degrading bacterium, Bacillus sp. SH-517
Author(s)
E J Jeong; Moon Soo Rhee; G P Kim; K H Lim; D H Yi; B H Bang
Bibliographic Citation
Journal of Korean Society for Applied Biological Chemistry, vol. 53, no. 1, pp. 43-49
Publication Year
2010
Abstract
We isolated Bacillus sp. SH-517 from decomposed chicken feathers at a local poultry plant. This strain produced a keratinase that degrades poultry feathers and therefore will be very valuable for industrial use. Most feathers were degraded by the strain within 40 h at 40°C by shaking culture (180 rpm). The keratinase from the culture medium of Bacillus sp. SH-517 was purified by centrifugation, 30?80% ammonium sulfate fractionation, twin-column DEAE-cellulose ion exchange chromatography and Sephadex G-150 gel filtration, to obtain a purified keratinase at 10.82% yield and 14-fold overall purification. The purified enzyme had a specific activity of 825 U/mg. A single protein band was shown on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The molecular weight of the keratinase from Bacillus sp. SH-517 was estimated as 51 kDa. The optimum pH and temperature for the enzyme reaction were 7.5 and 40°C, respectively. The enzyme remained stable over the pH range from 4.0 to 9.0 and at temperatures below 50°C. Proteins such as milk casein and chicken feathers were easily hydrolyzed by this enzyme. The enzyme activity was significantly inhibited by Hg2+, Ag2+, ethylene diamine tetraacetic acid (EDTA) and ethylene glycol tetraacetic acid (EGTA), but slightly stimulated by K+ and Na+.
Keyword
Bacillusfeatherkeratinaseproteasepurification
ISSN
I000-0171
Publisher
Springer
DOI
http://dx.doi.org/10.3839/jksabc.2010.008
Type
Article
Appears in Collections:
Jeonbuk Branch Institute > Biological Resource Center > 1. Journal Articles
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