Tuning alginate β-lactoglobulin complex coacervation by modulating pH and temperature
Mikkel Madsen1, Hossein Mohammad-Beigi1, Peter Westh2
1Enzyme and Protein Chemistry, Technical University of Denmark, DK-2800 Kgs, Lyngby, Denmark. M.Madsen_bio@outlook.com.
Soft Matter
|February 7, 2023
Summary
Complex coacervation of alginate and beta-lactoglobulin (β-Lg) can be controlled by pH and temperature. This study reveals molecular interactions and proton exchange during coacervation, enabling tunable encapsulation.
Area of Science:
- Food Science and Technology
- Biochemistry
- Materials Science
Background:
- Green chemistry trends favor natural biomolecules in food and encapsulation.
- Complex coacervation between anionic polysaccharides (alginate) and proteins (β-Lg) is a key green technology.
- Previous studies focused on macromolecular interactions, overlooking molecular details.
Purpose of the Study:
- To investigate the molecular mechanisms of alginate-β-Lg complex coacervation.
- To explore the influence of pH and temperature on coacervation properties.
- To provide insights for optimizing microencapsulation and drug delivery systems.
Main Methods:
- Detailed biophysical and chemical characterization of coacervation and coacervate particles.
- Isothermal titration calorimetry (ITC) to quantify proton exchange.
- Investigation of pH and temperature effects on coacervation behavior.
Main Results:
- Carboxylate resonance stabilization in alginate influences proton exchange during coacervation.
- Quantified proton release (4 per β-Lg) at pH 2.65 and uptake (2 per β-Lg) at pH 4.00.
- A secondary, temperature-induced (65 °C) coacervation step was observed, forming large, entropy-driven assemblies.
Conclusions:
- Alginate-β-Lg coacervation is tunable via pH and temperature, offering control over particle formation.
- Understanding molecular interactions and proton exchange is crucial for optimizing coacervation processes.
- Findings advance the application of complex coacervation in microencapsulation and drug delivery.


