Abstract
Thermostable alkaline proteinase was produced by a strain of Chrysosporium keratinophilum when cultured in lactose/mineral salt medium incorporating keratin solubilized with DMSO. The proteinase, partially purified by cold-acetone precipitation followed by gel-filtration on Sephadex G-75, was optimally active at pH 9 and stable from pH 7 to 10 with over 90% relative residual activity after incubation at 25°C for 24 h. The optimum temperature for enzyme activity was 90°C at which the activity half-life was 30 min. Enzyme activity was stimulated by Fe2+ and inhibited by 1,10 o-phenanthroline. Gel-filtration indicated an M r of 69 kDa.
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The authors are with the Department of Microbiology, Faculty of Biological Sciences, P.M. B.006, University of Nigeria, Nsukka, Enugu State, Nigeria
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Dozie, I.N.S., Okeke, C.N. & Unaeze, N.C. A thermostable, alkaline-active, keratinolytic proteinase from chrysosporium keratinophilum . World J Microbiol Biotechnol 10, 563–567 (1994). https://doi.org/10.1007/BF00367668
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DOI: https://doi.org/10.1007/BF00367668