Related Experiment Video
Updated: Jun 24, 2025

05:45
Author Spotlight: Process Development for the Spray-Drying of Probiotic Bacteria and Evaluation of the Product Quality
Published on: April 7, 2023
3.3K
Enhancing casein micelle dissociation in diluted skim milk systems using combined processing techniques
D R Stroinski1, K Petersen1, G E Lewis1
1Department of Animal and Food Science, University of Wisconsin-River Falls, River Falls, WI 54022.
Journal of Dairy Science
|June 2, 2024
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.
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.
Related Concept Videos
Detergent Purification of Membrane Proteins
5.2K
Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...
5.2K
Colloidal precipitates
561
The high insolubility of some precipitates can result in an unfavorable relative supersaturation. This can lead to colloidal particles with a large surface-to-mass ratio, where adsorption is promoted. For instance, in the precipitation of silver chloride, silver ions are adsorbed on the surface of the colloidal particles, forming a primary layer. This layer attracts ions of opposite charge (such as nitrate ions), forming a diffuse secondary layer of adsorbed ions. This electric double layer...
561

