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Rational Design of Alginate Lyase AlgL3199 for Thermal Stability and Specific Activity Enhancement
Zhifang Chen1,2, Jianhua Hao1,3, Yingying Guo1
1Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Laboratory for Marine Drugs and Byproducts, Qingdao Marine Science and Technology Center, Qingdao 266071, China.
Journal of Agricultural and Food Chemistry
|June 7, 2025
Summary
Engineered alginate lyase (enzyme) shows improved thermal stability and activity. Rational design using computer analysis and mutagenesis created enhanced mutants, paving the way for industrial applications.
Area of Science:
- Biochemistry
- Enzyme Engineering
- Structural Biology
Background:
- Alginate lyase is crucial for alginate degradation but limited by low thermal stability.
- Industrial applications of alginate lyase are hindered by its poor performance at high temperatures.
Purpose of the Study:
- To develop a rational design strategy for enhancing alginate lyase thermal stability.
- To improve the industrial applicability of alginate lyase through protein engineering.
Main Methods:
- Computer-aided structure analysis and energy calculations guided rational design.
- Site-directed mutagenesis was employed to create enhanced alginate lyase mutants.
- Enzyme activity and half-life assays were performed at 60 °C.
Main Results:
- Four mutants (K81A, D148P, K81A/D148P, K81A/D148P/V163T) showed significantly increased half-lives (up to 5.18-fold).
- Specific activities increased by up to 42.56% compared to the wild-type AlgL3199.
- Mutants exhibited enhanced hydrogen-bond networks, structural rigidity, and hydrophobic interactions.
Conclusions:
- A rational design strategy effectively improved alginate lyase thermal stability and specific activity.
- The K81A mutant demonstrated the most significant structural modifications and performance enhancements.
- This approach offers a valuable method for engineering thermostable alginate lyases for industrial use.
