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Tuning alginate β-lactoglobulin complex coacervation by modulating pH and temperature.

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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.

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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.