Affiliation:
1. Laboratoire de Génie Enzymatique et Biovalorisation (Unité du Laboratoire de Chimie des Substances Naturelles), I.U.T., Département de Génie Biologique, Limoges,1 and
2. Laboratoire de Microbiologie et Biochimie Appliquée, E.N.I.T.A., Bordeaux,2 France
Abstract
ABSTRACT
Streptomyces
strain K
1-02
, 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 NH
2
-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.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
Cited by
168 articles.
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