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Engineering a carbohydrate binding module to enhance chitinase catalytic efficiency on insoluble chitinous substrate
Haipeng Su1, Li Gao1, Jianan Sun1
1College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China.
Food Chemistry
|April 13, 2021
Summary
Engineered chitinase R-SaChiA4 shows significantly improved activity on insoluble chitin. Substituting chitin-binding domains (ChBDs) enhances substrate affinity for industrial biotransformation applications.
Area of Science:
- Biotechnology
- Enzymology
- Protein Engineering
Background:
- Chitin biotransformation is valuable for industry.
- High-performance chitinases are needed for efficient substrate hydrolysis.
- Chitin-binding domains (ChBDs) play a role in enzyme-substrate interactions.
Purpose of the Study:
- To engineer a high-performance chitinase by modifying its ChBDs.
- To improve the enzymatic activity of chitinase SaChiA4.
- To understand the role of ChBDs in substrate binding and hydrolysis.
Main Methods:
- Chitinase SaChiA4 ChBD was substituted with an exogenous ChBD (ChBDChiA1) from Bacillus circulans WL-12.
- Enzymatic activity assays were performed on chitin powder and colloidal chitin.
- Substrate-binding assays and molecular dynamics simulations were conducted.
Main Results:
- The engineered variant R-SaChiA4 showed a 54% increase in activity on chitin powder and a 49% increase on colloidal chitin compared to the wild-type.
- ChBD substitution enhanced substrate affinity, promoting enzymatic hydrolysis.
- Molecular dynamics simulations suggested hydrophobic interactions contribute to substrate binding.
Conclusions:
- Chitin-binding domains are crucial for enhancing chitinase activity and substrate affinity.
- The engineered R-SaChiA4 variant offers potential for industrial-scale chitin hydrolysis.
- This study advances understanding of ChBD function in chitin biotransformation.
