Rational design of a thermophilic β-mannanase fromBacillus subtilis TJ-102 to improve its thermostability

Enzyme and Microbial Technology
Xiang-Chao WangZhi-Min He

Abstract

A rational design method to improve β-mannanase (ManTJ102) thermostability was developed successfully in this study. The flexible area of residues 330-340 in ManTJ102 was firstly selected from analysis of molecular dynamics simulation and then the critical amino acid residue (Ala336Pro) with the lowest mutation energy was determined by virtual mutation, whose mutant was named as Mutant336. Afterward, the dynamics transition temperature (Tdtt) of ManTJ102 and Mutant336 was evaluated by simulated annealing and heating, and Mutant336 with higher Tdtt was implemented for experimental verification of the enzyme thermostability. As a result, the half-life of Mutant336 activity was 120 min at 60 °C, which was 24-fold of ManTJ102, and the irreversible thermal denaturation constant of Mutant336 was only about 2/5 of ManTJ102, indicating that Mutant336 has better thermostability than ManTJ102. Furthermore, Mutant336 has much higher β-mannanase activity and specific activity than ManTJ102. Therefore, Mutant336 was more suitable to further research for applications.

Citations

Oct 10, 2020·Critical Reviews in Biotechnology·Gaurav Singh Kaira, Mukesh Kapoor
Jan 2, 2021·Frontiers in Bioengineering and Biotechnology·Aneesa Dawood, Kesen Ma
Oct 4, 2020·Therapeutic Drug Monitoring·Jian WangXiaobei Deng
Jun 11, 2019·Journal of Agricultural and Food Chemistry·De-Ying GaoQian Wang

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