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Keratinolytic activity from the broth of a feather‐degrading thermophilic Streptomyces thermoviolaceus strain SD8
Author(s) -
Chitte R. R.,
Nalawade V. K.,
Dey S.
Publication year - 1999
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1046/j.1365-2672.1999.00484.x
Subject(s) - thermophile , library science , streptomyces , research article , biology , microbiology and biotechnology , bacteria , genetics , computer science
Keratinolytic activity was detected in the culture broth of feather‐degrading thermophilic Streptomyces thermoviolaceus SD8. The crude enzyme was concentrated by precipitation with 80% saturation of ammonium sulphate and desalted by SephadexG‐10–120 gel chromatography followed by lyophilization. The specific activity of the enzyme was enhanced 50‐fold. PAGE analysis indicated a monomeric form with a molecular weight of 40 kDa. The optimum pH and temperature for production of the enzyme were 8 and 55 °C, respectively. The enzyme was stable at a pH range of 6·5–8·5 and up to 65 °C. The enzyme could hydrolyse fibrin, muscle, collagen, nail and hair and could produce leucine, threonine and tyrosine from feather. It could be a useful enzyme for waste treatment by promoting hydrolysis of the above substances in the sewage, or it could be used for animal feed preparation.