World Journal of Microbiology & Biotechnology

, Volume 10, Issue 5, pp 563–567 | Cite as

A thermostable, alkaline-active, keratinolytic proteinase from chrysosporium keratinophilum

  • I. N. S. Dozie
  • C. N. Okeke
  • N. C. Unaeze
Research

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 Mr of 69 kDa.

Key words

Chrysosporium keratinophilum keratinolytic proteinase 

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Copyright information

© Rapid Communications of Oxford Ltd 1994

Authors and Affiliations

  • I. N. S. Dozie
  • C. N. Okeke
  • N. C. Unaeze

There are no affiliations available

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