ABSTRACT
A soil streptomycete (Streptomyces sp. A11) degraded collagen isolated from bovine Achilles tendon, calf skin, human placenta, carp swim bladder and rat tail tendon and released appreciable quantities of hydroxyproline. It also degraded hide powder and vegetable tanned leather. The organism was taxonomically characterized, compared with allied species, identified and designated as Streptomyces wartii.
Subject(s)
Animals , Cattle , Collagen/isolation & purification , Collagenases/biosynthesis , Female , Humans , Microscopy, Electron, Scanning , Pregnancy , Rats , Soil Microbiology , Streptomyces/classificationSubject(s)
Animals , Bacterial Proteins/isolation & purification , Biodegradation, Environmental , Chickens , Endopeptidases/isolation & purification , Feathers/drug effects , Goats , Hair/drug effects , Humans , Hydrolysis , Industrial Microbiology , Insect Proteins , Keratins/drug effects , Proteins/drug effects , Silk , Soil Microbiology , Streptomyces/enzymology , Wool/drug effectsABSTRACT
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.