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Novel Biocatalysts Based on Bromelain Immobilized on Functionalized Chitosans and Research on Their Structural
Marina G Holyavka1,2, Svetlana S Goncharova1, Andrey V Sorokin1,2,3
1Biophysics and Biotechnology Department, Voronezh State University, 1 Universitetskaya Square, 394018 Voronezh, Russia.
Polymers
|December 11, 2022
Summary
Enzyme immobilization using chitosan derivatives enhances bromelain stability and activity. N-(2-hydroxypropyl)-3-trimethylammonium chitosan hyperactivates bromelain by 208% through unique interactions, preserving enzyme structure.
Area of Science:
- Biochemistry
- Biomaterials Science
- Enzyme Engineering
Background:
- Enzyme immobilization is key to improving enzyme stability and reusability.
- Chitosan derivatives offer versatile platforms for enzyme carrier applications.
Purpose of the Study:
- To investigate the immobilization mechanism of cysteine protease bromelain on various water-soluble chitosan derivatives.
- To characterize the structural and catalytic properties of the resulting enzyme-carrier complexes.
Main Methods:
- Enzyme immobilization using carboxymethylchitosan, N-(2-hydroxypropyl)-3-trimethylammonium chitosan, chitosan sulfate, and chitosan acetate.
- Characterization of immobilized enzyme complexes using FTIR analysis.
- Assay of enzyme activity and specific activity.
Main Results:
- Chitosan sulfate and carboxymethylchitosan yielded higher immobilization efficiency (up to 65%) due to extensive hydrogen bonding.
- Most chitosan derivatives reduced bromelain activity by interacting with His158 in the active site.
- N-(2-hydroxypropyl)-3-trimethylammonium chitosan led to bromelain hyperactivation (up to 208% total activity) via physical interactions, preserving enzyme structure.
Conclusions:
- Chitosan derivative choice significantly impacts bromelain immobilization efficiency and catalytic activity.
- N-(2-hydroxypropyl)-3-trimethylammonium chitosan is a promising carrier for hyperactivating bromelain while preventing aggregation and autolysis.
