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• W2160446811 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." @default.
• W2160446811 created "2016-06-24" @default.
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• W2160446811 date "1999-06-01" @default.
• W2160446811 modified "2023-10-16" @default.
• W2160446811 title "Purification and Characterization of a Keratinolytic Serine Proteinase from <i>Streptomyces albidoflavus</i>" @default.
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• W2160446811 doi "https://doi.org/10.1128/aem.65.6.2570-2576.1999" @default.
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