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<p>Endo-1,4-xylanase II from <i>Trichoderma reesei</i> is highly sensitive toward grain proteinaceous inhibitors, which remains a major bottleneck for its industrial applications. In this study, the mutant TrXYNII<sub>DT_</sub>TX1 (T2C-T28C, G21W, N124A) was engineered to gain resistance to two types of xylanase inhibitors, TAXI-I and XIP-I. Compared with the wild-type, the sensitivity of TrXYNII<sub>DT</sub>_TX1 toward TAXI-I and XIP-I was decreased by 2.0-and 11.3-fold, respectively. After interaction with two types of inhibitors TAXI-I and XIP-I simultaneously, the residual activity of TrXYNII<sub>DT</sub>_TX1 was 3.4-fold higher than that of the wild-type. During grain saccharification, the reducing sugar released by TrXYNII<sub>DT</sub>_TX1 was 4.3-fold greater than that of the wild-type. In addition, TrXYNII<sub>DT</sub>_TX1 was also more thermostable than the wild-type. All these properties make TrXYNII<sub>DT</sub>_TX1 attractive for&#xa0;potential applications&#xa0;in&#xa0;the feed&#xa0;and brewing industries.</p> Graphical abstract <p></p>

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Rational design of a thermostable Trichoderma reesei endo-1,4-xylanase II variant with improved resistance toward proteinaceous inhibitors

  • 期刊论文

  • 发表日期：

    2025年2月13日

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  • Zhi-Mian Bai,
  • Dan Wu,
  • Su Yan,
  • Jun Wang,
  • Yan Xu,
  • Xiao-Wei Yu

摘要

Endo-1,4-xylanase II from Trichoderma reesei is highly sensitive toward grain proteinaceous inhibitors, which remains a major bottleneck for its industrial applications. In this study, the mutant TrXYNIIDT_TX1 (T2C-T28C, G21W, N124A) was engineered to gain resistance to two types of xylanase inhibitors, TAXI-I and XIP-I. Compared with the wild-type, the sensitivity of TrXYNIIDT_TX1 toward TAXI-I and XIP-I was decreased by 2.0-and 11.3-fold, respectively. After interaction with two types of inhibitors TAXI-I and XIP-I simultaneously, the residual activity of TrXYNIIDT_TX1 was 3.4-fold higher than that of the wild-type. During grain saccharification, the reducing sugar released by TrXYNIIDT_TX1 was 4.3-fold greater than that of the wild-type. In addition, TrXYNIIDT_TX1 was also more thermostable than the wild-type. All these properties make TrXYNIIDT_TX1 attractive for potential applications in the feed and brewing industries.

Graphical abstract