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Improvement of thermostability and catalytic efficiency of xylanase from Myceliophthora thermophilar by N-terminal and C-terminal truncation.
Yang, Yue; Zhang, Chengnan; Lu, Hongyun; Wu, QiuHua; Wu, Yanfang; Li, Weiwei; Li, Xiuting.
Affiliation
  • Yang Y; Key Laboratory of Geriatric Nutrition and Health (Beijing Technology and Business University), Ministry of Education, Beijing, China.
  • Zhang C; Beijing Engineering and Technology Research Center of Food Additives, Beijing Technology and Business University (BTBU), Beijing, China.
  • Lu H; Department of Exercise Biochemistry, Exercise Science School, Beijing Sport University, Beijing, China.
  • Wu Q; Key Laboratory of Geriatric Nutrition and Health (Beijing Technology and Business University), Ministry of Education, Beijing, China.
  • Wu Y; Beijing Engineering and Technology Research Center of Food Additives, Beijing Technology and Business University (BTBU), Beijing, China.
  • Li W; Key Laboratory of Geriatric Nutrition and Health (Beijing Technology and Business University), Ministry of Education, Beijing, China.
  • Li X; Beijing Engineering and Technology Research Center of Food Additives, Beijing Technology and Business University (BTBU), Beijing, China.
Front Microbiol ; 15: 1385329, 2024.
Article de En | MEDLINE | ID: mdl-38659990
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.
Mots clés

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Langue: En Journal: Front Microbiol Année: 2024 Type de document: Article Pays d'affiliation: Chine Pays de publication: Suisse

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Langue: En Journal: Front Microbiol Année: 2024 Type de document: Article Pays d'affiliation: Chine Pays de publication: Suisse