Keratinase of a streptomycete.
Keratinase produced from Streptomyces Sp.A11 decomposed human hair, chicken feather, wool, silk and pure keratin extracted from human epidermis. Purification of the enzyme by DEAE-cellulose column chromatography resulted in 7.5-fold increase in activity relative to the activity of the culture filtrate. The enzyme was inducible, extracellular, homogeneous with a molecular weight of 49,000. The enzyme activity was inhibited by reduced glutathione, phenylmethyl sulphonyl fluoride and 2-mercaptoethanol.
Department of Microbiology, Bose Institute, Calcutta, India.
R P
RP
Mukhopadhyay
A L
AL
Chandra
D000818:Animals; D002645:Chickens; D005241:Feathers / Q000378:metabolism; D005978:Glutathione / Q000494:pharmacology; D006801:Humans; D007633:Keratins / Q000378:metabolism*; D008623:Mercaptoethanol / Q000494:pharmacology; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D010664:Phenylmethylsulfonyl Fluoride / Q000494:pharmacology; D013302:Streptomyces / Q000201:enzymology*
D010664:Phenylmethylsulfonyl Fluoride; D008623:Mercaptoethanol; D007633:Keratins; D010447:Peptide Hydrolases; C035855:keratinase; D005978:Glutathione