Purification and Characterization of a Keratinase from a Feather-degrading Bacterium, Bacillus sp. SH-517

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℃ by shaking culture (180 rpm...

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Veröffentlicht in:Applied biological chemistry 2010, 53(1), , pp.43-49
Hauptverfasser: Jeong, E.J., Eulji University, Sungnam, Republic of Korea, Rhee, M.S., Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea, Kim, G.P., Lotte Confectionery Co., Ltd., Seoul, Republic of Korea, Lim, K.H., Konkuk University, Seoul, Republic of Korea, Yi, D.H., Konkuk University, Seoul, Republic of Korea, Bang, B.H., Eulji University, Sungnam, Republic of Korea
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Zusammenfassung: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℃ 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℃, respectively. The enzyme remained stable over the pH range from 4.0 to 9.0 and at temperatures below 50℃. 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+.
ISSN:1738-2203
2468-0834
2234-344X
2468-0842
DOI:10.3839/jksabc.2010.008