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Interaction between casein and the oppositely charged surfactant.

Yan Liu1, Rong Guo

  • 1College of Chemistry and Chemical Engineering, Yangzhou University, Yangzhou 225002, People's Republic of China.

Biomacromolecules
|August 19, 2007
PubMed
Summary

Dodecyltrimethylammonium bromide (DTAB) interacts with casein, forming insoluble complexes at critical concentrations. Further DTAB addition redissolves these complexes, influenced by electrostatic interactions and micelle formation.

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Area of Science:

  • Biochemistry
  • Colloid and Surface Chemistry

Background:

  • Casein, a major milk protein, interacts with surfactants.
  • Cationic surfactants like dodecyltrimethylammonium bromide (DTAB) are widely used.

Purpose of the Study:

  • To investigate the interaction mechanism between DTAB and casein.
  • To elucidate the structural changes and complex formation.

Main Methods:

  • Isothermal titration calorimetry (ITC)
  • Turbidity measurements
  • Dynamic light scattering (DLS)
  • Fluorescence spectroscopy

Main Results:

  • DTAB binds electrostatically to negatively charged sites on casein.
  • Formation of insoluble casein/DTAB complexes at critical surfactant concentrations (c1).
  • Redissolution of complexes at higher DTAB concentrations due to net positive charge and free micelle formation.

Conclusions:

  • The interaction proceeds through sequential binding, aggregation, and redissolution phases.
  • Salt addition weakens DTAB-casein binding, promoting free micelle formation.