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...
| Main Authors: | , , , , |
|---|---|
| Format: | Online |
| Language: | English |
| Published: |
John Wiley and Sons Inc.
2015
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4720410/ |