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Updated: May 14, 2025

Manufacture of Concentrated, Lipid-based Oxygen Microbubble Emulsions by High Shear Homogenization and Serial Concentration
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Casein Functionalization Using High-Pressure Homogenization and Emulsifying Salts.

Anthony Fuchs1, Danielle Stroinski1, Ashley Gruman1

  • 1Department of Animal and Food Science, University of Wisconsin-River Falls, River Falls, WI 54022, USA.

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|April 12, 2025
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Summary

Emulsifying salts and high-pressure homogenization significantly dissociate casein micelles in skim milk, enhancing protein functionality for dairy applications.

Keywords:
caffeinecaseinemulsifying saltsemulsionsencapsulationfoaminghigh-pressure homogenization

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Area of Science:

  • Dairy Science
  • Food Chemistry
  • Protein Science

Background:

  • Casein proteins form spherical micelles in milk, with hydrophobic cores and hydrophilic exteriors.
  • Previous studies indicated emulsifying salts and high-pressure homogenization can dissociate casein micelles.

Purpose of the Study:

  • To quantify casein micelle dissociation in diluted skim milk after specific processing treatments.
  • To evaluate the impact of processing on casein protein functionality.

Main Methods:

  • Diluted skim milk (20% v/v) was subjected to no processing, emulsifying salts (E), high-pressure homogenization (H), or combined EH treatments.
  • Samples were filtered (0.22 µm, 0.05 µm), and permeates analyzed via SDS-PAGE to quantify casein dissociation.
  • Functional properties including foam expansion, foam stability, emulsifying activity, and caffeine interaction were assessed.

Main Results:

  • The EH treatment resulted in significant casein micelle dissociation, with 93.2% ± 7.71% of casein passing through a 0.05 µm filter, compared to 9.35% ± 2.53% in controls.
  • EH-treated milk exhibited enhanced foam expansion (138.3% vs. 33.33%), foam stability (113.3% vs. 21.67%), and emulsifying activity (two-fold higher).
  • EH treatment also improved casein interaction with caffeine.

Conclusions:

  • Combining emulsifying salts (E) and high-pressure homogenization (H) effectively dissociates casein micelles in skim milk.
  • This dissociation exposes functional hydrophobic subunits, leading to improved functional properties of skim milk systems.
  • The findings have direct applications in dairy product development and potential implications for other protein-rich systems.