Characterization of a keratinolytic serine proteinase from Streptomyces pactum DSM 40530.
A serine protease from the keratin-degrading Streptomyces pactum DSM 40530 was purified by casein agarose affinity chromatography. The enzyme had a molecular weight of 30,000 and an isoelectric point of 8.5. The proteinase was optimally active in the pH range from 7 to 10 and at temperatures from 40...
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| Wydane w: | Appl Environ Microbiol |
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| Główni autorzy: | , , |
| Format: | Artigo |
| Język: | Inglês |
| Wydane: |
American Society for Microbiology (ASM)
1995
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| Hasła przedmiotowe: | |
| Dostęp online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC167669/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7487006/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.61.10.3705-3710.1995 |
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