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Enhancement of the catalytic efficiency and thermostability of S tenotrophomonas sp. keratinase KerSMD by domain exchange with KerSMF
In this study, we enhanced the catalytic efficiency and thermostability of keratinase KerSMD by replacing its N/C‐terminal domains with those from a homologous protease, KerSMF, to degrade feather waste. Replacement of the N‐terminal domain generated a mutant protein with more than twofold increased...
| Autores principales: | , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
John Wiley and Sons Inc.
2015
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4720410/ https://www.ncbi.nlm.nih.gov/pubmed/26552936 http://dx.doi.org/10.1111/1751-7915.12300 |