Keratinolytic activity of Streptomyces sp. S.K1-02: a new isolated strain

A Streptomyces sp. producing a high keratinolytic activity when cultured on feather meal medium was isolated from a naturally degraded feather. Maximal keratin degradation using supernatant fluid obtained from batch culture of this organism was observed at 70 °C and pH 10. Keratinolytic activity was...

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Veröffentlicht in:	Letters in applied microbiology 1998, Vol.26 (1), p.77-80
Hauptverfasser:	Letourneau, F, Soussotte, V, Bressollier, P, Branland, P, Verneuil, B
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Bacteriology Biodegradation, Environmental Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology Caseins - metabolism Edetic Acid - pharmacology Feathers Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Industrial Microbiology Industrial Waste keratin Keratins - metabolism Metabolism. Enzymes Metals - pharmacology Microbiology Mission oriented research Peptide Hydrolases - metabolism Physiology and metabolism Protease Inhibitors - pharmacology proteinases proteolysis Streptomyces - enzymology Streptomyces - growth & development Streptomyces - isolation & purification Temperature Tosyl Compounds - pharmacology
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Zusammenfassung:	A Streptomyces sp. producing a high keratinolytic activity when cultured on feather meal medium was isolated from a naturally degraded feather. Maximal keratin degradation using supernatant fluid obtained from batch culture of this organism was observed at 70 °C and pH 10. Keratinolytic activity was only partially inhibited by EDTA or PMSF, suggesting that the overall keratinolytic activity was supported by different proteases. Comparisons between proteolytic activities derived from this new strain (S.K1–02) and commercial proteases indicated that S.K1–02 could be a useful biotechnological tool in valorization of keratin‐containing wastes, or in the depilation process in the leather industry.
ISSN:	0266-8254 1472-765X
DOI:	10.1046/j.1472-765X.1998.00281.x