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Applied and Environmental Microbiology, June 1999, p. 2570-2576, Vol. 65, No. 6
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Purification and Characterization of a Keratinolytic Serine Proteinase from Streptomyces albidoflavus

Philippe Bressollier,1 François Letourneau,1 Maria Urdaci,2 and Bernard Verneuil1,*

Laboratoire de Génie Enzymatique et Biovalorisation (Unité du Laboratoire de Chimie des Substances Naturelles), I.U.T., Département de Génie Biologique, Limoges,1 and Laboratoire de Microbiologie et Biochimie Appliquée, E.N.I.T.A., Bordeaux,2 France

Received 13 October 1998/Accepted 26 March 1999

Streptomyces strain K1-02, which was identified as a strain of Streptomyces albidoflavus, secreted at least six extracellular proteases when it was cultured on feather meal-based medium. The major keratinolytic serine proteinase was purified to homogeneity by a two-step procedure. This enzyme had a molecular weight of 18,000 and was optimally active at pH values ranging from 6 to 9.5 and at temperatures ranging from 40 to 70°C. Its sensitivity to protease inhibitors, its specificity on synthetic substrates, and its remarkably high level of NH2-terminal sequence homology with Streptomyces griseus protease B (SGPB) showed that the new enzyme, designated SAKase, was homologous to SGPB. We tested the activity of SAKase with soluble and fibrous substrates (elastin, keratin, and type I collagen) and found that it was very specific for keratinous substrates compared to SGPB and proteinase K.

* Corresponding author. Mailing address: Département de Génie Biologique, I.U.T., allée André Maurois, 87065 Limoges Cedex, France. Phone: 33 05 55 43 43 90. Fax: 33 05 55 43 43 93. E-mail: labioiut{at}.unilim.fr.

Applied and Environmental Microbiology, June 1999, p. 2570-2576, Vol. 65, No. 6
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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