Activity-stability trade-off observed in variants at position 315 of the GH10 xylanase XynR
Abstract XynR is a thermostable alkaline GH10 xylanase, for which we have previously examined the effects of saturation mutagenesis at position 315 on enzyme alkaliphily, and found that at pH 10, the activities of variants could be ordered as follows: T315Q > T315S = T315N > T315H = wild-type...
| Main Authors: | , , , , , , |
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| 格式: | Article |
| 語言: | English |
| 出版: |
Nature Portfolio
2024-04-01
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| 叢編: | Scientific Reports |
| 在線閱讀: | https://doi.org/10.1038/s41598-024-57819-z |