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Encapsulation of β-Galactosidase into Polyallylamine/Polystyrene Sulphonate Polyelectrolyte Microcapsules
Yuri S Chebykin1, Egor V Musin1, Aleksandr L Kim1
1Institute of Theoretical and Experimental Biophysics Russian Academy of Science, Institutskaya St., 3, 142290 Puschino, Moscow Region, Russia.
International Journal of Molecular Sciences
|October 26, 2024
Summary
Encapsulating beta-galactosidase (β-galactosidase) in microcapsules offers a promising solution for lactose intolerance. The co-precipitation method effectively protects enzyme activity, improving enzyme replacement therapy for hypolactasia.
Area of Science:
- Biomaterials Science
- Biotechnology
- Enzyme Engineering
Background:
- Lactose intolerance affects over half the global population, necessitating improved therapeutic strategies.
- Current enzyme replacement therapies for lactose intolerance exhibit limited efficacy.
- Encapsulation of enzymes presents a potential method to enhance therapeutic effectiveness.
Purpose of the Study:
- To investigate the encapsulation of beta-galactosidase (β-galactosidase) in polyelectrolyte microcapsules using layer-by-layer assembly.
- To compare the efficacy of adsorption and co-precipitation methods for β-galactosidase encapsulation.
- To evaluate the stability and release profile of encapsulated β-galactosidase under simulated physiological conditions.
Main Methods:
- Utilized the layer-by-layer method to create polyelectrolyte microcapsules from polyallylamine and polystyrene sulfonate.
- Employed both adsorption and co-precipitation techniques for encapsulating β-galactosidase within the microcapsules.
- Assessed enzyme encapsulation efficiency, activity retention, and release kinetics at low pH (2) and high ionic strength (1 M NaCl).
Main Results:
- The co-precipitation method demonstrated significantly higher enzyme encapsulation efficiency compared to the adsorption method (six-fold increase).
- β-galactosidase encapsulated via co-precipitation showed minimal release (≤20%) under low pH or high salt conditions, preserving enzyme activity.
- Enzymes encapsulated using the adsorption method exhibited near-complete release (≈100%) under the same conditions, indicating poor stability.
Conclusions:
- Co-precipitation is a superior method for encapsulating β-galactosidase, ensuring enzyme stability and activity retention.
- Encapsulated β-galactosidase using co-precipitation shows significant potential as a therapeutic agent for treating lactose intolerance (hypolactasia).
- This approach offers a more effective enzyme replacement therapy for individuals with hypolactasia.
