Jing-Run Ye
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Jing-Run Ye has a total of 10 co-authors. Here are the top co-authors by number of shared publications:
- Chengcheng Jiang
Key Laboratory of Sustainable, Development of Polar Fishery, Ministry of Agriculture and Rural Affairs, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China
1 shared publication - Chuan-Yang Shi
College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China
1 shared publication - Hai-Ying Wang
Key Laboratory of Sustainable, Development of Polar Fishery, Ministry of Agriculture and Rural Affairs, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China
1 shared publication - Qin Wang
Qingdao Institute of Marine Bioresources for Nutrition & Health Innovation, Qingdao 266106, China
1 shared publication - Shou-Fu Zhang
School of Marine Science and Engineering, Qingdao Agricultural University, Qingdao 266109, China
1 shared publication - Tian-Hong Liu
Marine Science Research Institute of Shandong Province, Qingdao 266104, China
1 shared publication
Latest Publications
- Open Access
- 22 December 2025
- Published by MDPI AG in Marine Drugs
- Vol. 24 (1) , 6
Enhanced Thermostability and Catalytic Efficiency of Alginate Lyase Alyw203 by Hydrogen Bond Network Reconstruction
Alginate lyases are commonly employed for producing alginate oligosaccharides (AOS), but their industrial application is often constrained by low thermal stability and catalytic efficiency. This study engineered mutants of alginate lyase Alyw203 from marine Vibrio based on B-factor values and negative ΔΔG values. The L172V mutant exhibited a 2.43-fold increase in half-life at 40 °C, reduced Km (from 107 to 65 mg/mL), and enhanced kcat/Km (from 0.07 to 0.35 mL/mg/s), indicating improved thermal stability, substrate affinity, and catalytic efficiency. Molecular dynamics simulations revealed that these improvements originated from reconstructed hydrogen bond networks, which stabilized enzyme–substrate interactions and reduced conformational flexibility. These results demonstrate that rational design focused on strengthening hydrogen bonding can simultaneously improve both stability and activity, offering a promising strategy for industrial AOS production.
- 22 December 2025
- Published by MDPI AG in Marine Drugs
- Vol. 24 (1) , 6
Open AccessEnhanced Thermostability and Catalytic Efficiency of Alginate Lyase Alyw203 by Hydrogen Bond Network Reconstruction
Alginate lyases are commonly employed for producing alginate oligosaccharides (AOS), but their industrial application is often constrained by low thermal stability and catalytic efficiency. This study engineered mutants of alginate lyase Alyw203 from marine Vibrio based on B-factor values and negative ΔΔG values. The L172V mutant exhibited a 2.43-fold increase in half-life at 40 °C, reduced Km (from 107 to 65 mg/mL), and enhanced kcat/Km (from 0.07 to 0.35 mL/mg/s), indicating improved thermal stability, substrate affinity, and catalytic efficiency. Molecular dynamics simulations revealed that these improvements originated from reconstructed hydrogen bond networks, which stabilized enzyme–substrate interactions and reduced conformational flexibility. These results demonstrate that rational design focused on strengthening hydrogen bonding can simultaneously improve both stability and activity, offering a promising strategy for industrial AOS production.