Cloning, Expression, and Characterization of a GHF 11 Xylanase from &lt;i&gt;Alteromonas macleodii &lt;/i&gt;HY35&lt;i&gt; &lt;/i&gt;in &lt;i&gt;Escherichia col&lt;/i&gt;&lt;i&gt;i&lt;/i&gt;

Tian, Ye; Xu, Jing; Shi, Jinpeng; Kong, Mengyuan; Guo, Changjiang; Cui, Caixia; Wang, Yongtao; Wang, Yan; Zhou, Chenyan

doi:10.2323/jgam.2021.10.003

Cited by 2 publications

(1 citation statement)

References 52 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Microorganisms that degrade plant cell walls must possess multiple hemicellulose degradation genes, with glycoside hydrolases from family 43 (GH43) typically including various types of glycoside hydrolases (13). In our previous research, we successfully identi ed GH43 xylanase XynZT-2 from Alteromones Macleadii H35 (24). In this study, we aimed to improve the enzymatic properties of XynZT-2 by analyzing protein evolution and constructing a small mutant library through homologous replacement of amino acids near the active site.…”

Section: Introductionmentioning

confidence: 99%

Improving the catalytic properties of xylanase from Alteromones Macleadii H35 through evolution analysis

Cui,

xu,

et al. 2024

Preprint

Self Cite

View full text Add to dashboard Cite

Endo-1,4-β-xylanase is considered one of the most important xylanolytic enzymes, and in this study, we aimed to improve the catalytic properties of Alteromones Macleadii xylanase (Xyn ZT-2) using an evolution-guided design approach. Analysis of the amino acid sequence revealed that the amino acids located in close proximity to the active site were highly conserved, with only a few amino acid differences. By introducing various mutations, we were able to modify the catalytic performance of the enzyme. Notably, the A152G mutation resulted in a 9.8-fold increase in activity and a 23.2-fold increase in catalytic efficiency. Furthermore, the optimal temperature of A152G was raised to 65°C, which is 20°C higher than that of Xyn ZT-2, and the half-life period of T287S was enhanced by 4.9 times. These findings demonstrate the significance of amino acid evolution in determining the catalytic performance of xylanase. By utilizing an evolution analysis to create a smaller mutation library, we efficiently enhanced the catalytic performance, thus providing a novel strategy for improving enzyme catalytic efficiency.

show abstract

Section: Introductionmentioning

confidence: 99%