A Thermostable PL7 Alginate Lyase <i>Vf</i> Aly17 from <i>Vibrio fortis</i> with Broad Substrate Specificity: Structural and Mechanistic Insights into Heat Stability

. It exhibits an optimal temperature of 50 °C, retains >50% of its enzymatic activity after incubation at 40-70 °C for 120 min, and maintains >20% activity even at 90 °C. Alanine substitutions at residues Asn94, Lys174, Cys308, and Cys321 resulted in significant reductions in both enzymatic activity and thermostability. Molecular docking and molecular dynamics simulation results revealed a decrease in the number of hydrogen bonds, alterations in the electrostatic interaction network, and a notable decline in the stability of the enzyme-substrate complex. These findings strongly indicate that these residues play crucial roles in mediating thermostability.

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Publication Details

Journal
Journal of Agricultural and Food Chemistry
Published
2026-04-27
DOI
https://doi.org/10.1021/acs.jafc.5c15248
Primary Topic
Seaweed-derived Bioactive Compounds
Type
article
Field-Weighted Citation Impact
0.00

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article

A Thermostable PL7 Alginate Lyase Vf Aly17 from Vibrio fortis with Broad Substrate Specificity: Structural and Mechanistic Insights into Heat Stability

Yining Zheng, Lianshun Wang, Guojun Yang, Lu Yanan et al.
Journal of Agricultural and Food Chemistry
Seaweed-derived Bioactive Compounds
article

A Thermostable PL7 Alginate Lyase Vf Aly17 from Vibrio fortis with Broad Substrate Specificity: Structural and Mechanistic Insights into Heat Stability

Yining Zheng, Lianshun Wang, Guojun Yang, Lu Yanan, Xin Wang, Hua Wang, Yuting Cong, Wulong Jiang, Jing Gu, Jingyun Zhang, Li Wang, Yuan Wang
article en

Abstract

. It exhibits an optimal temperature of 50 °C, retains >50% of its enzymatic activity after incubation at 40-70 °C for 120 min, and maintains >20% activity even at 90 °C. Alanine substitutions at residues Asn94, Lys174, Cys308, and Cys321 resulted in significant reductions in both enzymatic activity and thermostability. Molecular docking and molecular dynamics simulation results revealed a decrease in the number of hydrogen bonds, alterations in the electrostatic interaction network, and a notable decline in the stability of the enzyme-substrate complex. These findings strongly indicate that these residues play crucial roles in mediating thermostability.

Journal of Agricultural and Food ChemistryVol. 74(17)
Dalian Ocean University (CN)
Foundation of Liaoning Province Education Administration, Department of Science and Technology of Liaoning Province
Affordable and clean energy
Openalex Percentile: Top 16%
Seaweed-derived Bioactive Compounds
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