Improvement of thermostability and catalytic efficiency of xylanase from Myceliophthora thermophilar by N-terminal and C-terminal truncation

Yue Yang; Chengnan Zhang; Hongyun Lu; QiuHua Wu; Yanfang Wu; Weiwei Li; Xiuting Li

doi:10.3389/fmicb.2024.1385329

Improvement of thermostability and catalytic efficiency of xylanase from Myceliophthora thermophilar by N-terminal and C-terminal truncation

Front Microbiol. 2024 Apr 10:15:1385329. doi: 10.3389/fmicb.2024.1385329. eCollection 2024.

Authors

Yue Yang^#^{1

2}, Chengnan Zhang^#³, Hongyun Lu^{1

2}, QiuHua Wu^{1

2}, Yanfang Wu^{1

2}, Weiwei Li^{1

2}, Xiuting Li^{1

2}

Affiliations

¹ Key Laboratory of Geriatric Nutrition and Health (Beijing Technology and Business University), Ministry of Education, Beijing, China.
² Beijing Engineering and Technology Research Center of Food Additives, Beijing Technology and Business University (BTBU), Beijing, China.
³ Department of Exercise Biochemistry, Exercise Science School, Beijing Sport University, Beijing, China.

^# Contributed equally.

Abstract

Introduction: Extracting xylanase from thermophilic filamentous fungi is a feasible way to obtain xylanase with good thermal stability.

Methods: The transcriptomic data of Myceliophthora thermophilic destructive ATCC42464 were differentially expressed and enriched. By comparing the sequences of Mtxylan2 and more than 10 xylanases, the N-terminal and C-terminal of Mtxylan2 were truncated, and three mutants 28N, 28C and 28NC were constructed.

Results and discussion: GH11 xylan Mtxylan2 was identified by transcriptomic analysis, the specific enzyme activity of Mtxylan2 was 104.67 U/mg, and the optimal temperature was 65°C. Molecular modification of Mtxylan2 showed that the catalytic activity of the mutants was enhanced. Among them, the catalytic activity of 28C was increased by 9.3 times, the optimal temperature was increased by 5°C, and the residual enzyme activity remained above 80% after 30 min at 50-65°C, indicating that redundant C-terminal truncation can improve the thermal stability and catalytic performance of GH11 xylanase.

Keywords: GH11 xylanase; N-terminal and C-terminal truncation; catalytic efficiency; intrinsic mechanism; thermostability.

Grants and funding

The author(s) declare that financial support was received for the research, authorship, and/or publication of this article. This research was funded by National Key R&D Program of China (No. 2022YFD2101401) and National Natural Science Foundation of China (Nos. 31972016 and 32001638), and the Beijing Municipal Natural Science Foundation & Beijing Municipal Education Commission (No. KZ202110011016).