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Strong electrostatic attraction drives milk heteroprotein complex coacervation.

Isabel Vinterbladh1, Rima Hachfi Soussi2, Jan Forsman1

  • 1Division of Computational Chemistry, Lund University, Naturvetarvägen 24, SE-223 62 Lund, Sweden.

International Journal of Biological Macromolecules
|November 27, 2024
PubMed
Summary

Milk protein coacervates, essential for encapsulating bioactives in functional foods, are driven by electrostatic interactions between lactoferrin and beta-lactoglobulin. These interactions depend on pH and salt concentration, revealing key amino acid

Keywords:
CoacervatesHeteroprotein complex coacervationLactoferrinMetropolis-Hastings Monte CarloMilk proteinsParallel temperinglactoglobulin

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Area of Science:

  • Food Science and Technology
  • Biophysics
  • Materials Science

Background:

  • Coacervates formed from oppositely charged milk proteins, specifically lactoferrin and beta-lactoglobulin, are utilized in functional food development.
  • These coacervates serve as primary vehicles for encapsulating bioactive compounds.
  • Understanding the fundamental forces governing coacervate formation is crucial for optimizing their application.

Purpose of the Study:

  • To elucidate the driving forces behind the formation of milk protein coacervates.
  • To investigate the association of lactoferrin and beta-lactoglobulin at the amino acid level.
  • To provide detailed insights into the thermodynamics and molecular interactions governing coacervation.

Main Methods:

  • Utilized molecular simulations to study the association of lactoferrin and beta-lactoglobulin.
  • Analyzed inter-protein electrostatic interactions, including isotropic and anisotropic components.
  • Investigated amino acid contacts within trimeric and pentameric protein complexes.

Main Results:

  • Inter-protein electrostatic interactions were identified as the dominant force in coacervate formation.
  • These electrostatic interactions were found to be equally divided between monopole-monopole attraction and uneven surface charge distributions.
  • Calculated protein-protein interaction free energy showed strong dependence on pH and salt concentration, aligning with experimental data.

Conclusions:

  • The study reveals that electrostatic forces, both isotropic and anisotropic, are key drivers of milk protein coacervate formation.
  • pH and salt concentration significantly influence the thermodynamic stability of these coacervates.
  • Specific amino acid 'hot-spots' were identified as critical for heteroprotein complex coacervation.