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Enhancing casein micelle dissociation in diluted skim milk systems using combined processing techniques.

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Summary

This study explored casein micelle dissociation in skim milk using ethanol or emulsifying salts combined with ultra-high-pressure homogenization (UHPH). Optimized conditions achieved significant micelle breakdown, creating potential for novel food ingredient applications.

Keywords:
caseinemulsifying saltsethanolhigh-pressure homogenization

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Area of Science:

  • Food Science
  • Dairy Science
  • Physical Chemistry

Background:

  • Casein micelles are complex colloidal structures in milk.
  • Understanding casein micelle dissociation is key for modifying milk functionalities.
  • Existing methods for dissociation have limitations.

Purpose of the Study:

  • To evaluate casein micelle dissociation in diluted skim milk.
  • To investigate the combined effects of solvent/emulsifying salt treatments and ultra-high-pressure homogenization (UHPH).
  • To explore potential applications of dissociated casein systems.

Main Methods:

  • Diluted skim milk solutions were treated with varying ethanol concentrations (0-60%) or emulsifying salts (sodium hexametaphosphate, sodium citrate).
  • Treatments were combined with ultra-high-pressure homogenization (UHPH) at pressures ranging from 100-300 MPa.
  • Casein micelle dissociation was assessed via changes in sample absorbance, particle size, and hydrophobicity.

Main Results:

  • High ethanol concentrations (40-60%) at elevated temperatures (45-65°C) combined with UHPH (≥200 MPa) significantly dissociated casein micelles.
  • Emulsifying salts, specifically sodium hexametaphosphate (≥1 mM) and sodium citrate (≥10 mM), also induced dissociation, enhanced by UHPH (≥200 MPa).
  • Dissociation was evidenced by reduced absorbance, altered particle size distribution, and increased hydrophobicity.

Conclusions:

  • Both solvent-based (ethanol) and emulsifying salt-based methods effectively dissociate casein micelles when coupled with UHPH.
  • Optimized processing parameters enhance the extent of casein micelle dissociation.
  • These findings suggest potential for using dissociated casein systems as functional ingredients or encapsulation agents in the food industry.