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Researchers achieved tunable control over protein coacervate properties by adjusting pH. This pH-driven transition, from liquid to solid, impacts food matrix development and protein dynamics.

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Area of Science:

  • Food Science
  • Materials Science
  • Biophysics

Background:

  • Developing novel food matrices requires precise control over concentrated protein coacervates.
  • Protein coacervates, formed from proteins like beta-lactoglobulin (BLG) and lysozyme (LYS), are promising for new food applications.

Purpose of the Study:

  • To investigate the pH-driven liquid-gel-solid phase transition in BLG-LYS protein coacervates.
  • To understand how changes in pH affect the physical properties and dynamics of these coacervates.

Main Methods:

  • Utilized pH adjustments to induce phase transitions in BLG-LYS coacervates.
  • Employed spin-spin relaxation measurements and hydrogen bond competition experiments.
  • Conducted molecular dynamics simulations to analyze structural and dynamic changes.

Main Results:

  • Observed a significant increase in terminal relaxation time from 0.17 ms to 267 s during the pH-driven transition.
  • Determined that increasing pH from 6 to 8 shifted the BLG/LYS stoichiometric ratio from 3:1 to 1:1.
  • Found that enhanced charge symmetry expanded the BLG-LYS interaction interface by 1.8 times, promoting desolvation and hydrogen bond formation.

Conclusions:

  • pH-driven transitions offer a method for tuning the physical properties of protein coacervates.
  • Altered protein stoichiometry and interactions under varying pH influence coacervate dynamics.
  • This study provides a foundation for designing advanced protein-based food models with controllable characteristics.