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...

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Detalles Bibliográficos
Autores principales: Fang, Zhen, Zhang, Juan, Liu, Baihong, Du, Guocheng, Chen, Jian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2015
Materias:
Research Articles
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

Internet

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

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