insights into the role of exposed surface charged residues in the alkali-tolerance of gh11 xylanase

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ID: 134907
2020
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Ranked #744 of 875 articles by views in journal of magnetic resonance (san diego, calif : 1997)

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Abstract
Thermostable and alkaline- or acid-stable xylanases are more advantageous in agricultural and industrial fields. In this study, a rational structure-based design was conducted based on a thermostable GH11 xylanase TlXynA from Thermomyces lanuginosus to improved pH-tolerance. Four mutant enzymes (P1, P2, P3, and P4) and five variants (N1, N2, N3, N4, and N5) were constructed by substituting surface charged residue combinations using site-directed mutagenesis. Compared to the native enzyme, two mutants P1 and P2 showed higher acid tolerance, especially at pH 3.0, presented 50 and 40% of their maximum activity, respectively. In addition, four mutants N1, N2, N3 and N4 had higher tolerance than the native enzyme to alkaline environments (pH 7.0–9.0). At pH 9.0, the residual activities of N1, N2, N3, and N4 were 86, 78, 77, and 66%, respectively. In summary, an improved pH-tolerance design principle is being reported.
Reference Key
wu2020frontiersinsights Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Xiuyun Wu;Qun Zhang;Lanzeng Zhang;Shijia Liu;Guanjun Chen;Huaiqiang Zhang;Lushan Wang
Journal journal of magnetic resonance (san diego, calif : 1997)
Year 2020
DOI
10.3389/fmicb.2020.00872
URL
https://www.frontiersin.org/article/10.3389/fmicb.2020.00872/full
Keywords
xylanase

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