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Related Experiment Video

Updated: Jun 29, 2025

Novel Production Protocol for Small-scale Manufacture of Probiotic Fermented Foods

Novel Production Protocol for Small-scale Manufacture of Probiotic Fermented Foods

Published on: September 10, 2016

Invited review: Modeling milk stability.

C Holt¹, J A Carver²

¹School of Biomolecular Sciences, University of Glasgow, Glasgow G12 8QQ, United Kingdom.

Journal of Dairy Science

|March 24, 2024

Summary

This summary is machine-generated.

Caseins, intrinsically disordered proteins, influence milk stability. Their solubility, affected by pH and ions, impacts protein aggregation and mineral deposits during processing and storage.

Keywords:

amyloid fibril calcium phosphate nanocluster casein micelle milk protein stability molecular chaperone

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Area of Science:

Food Science
Protein Chemistry
Dairy Science

Background:

Caseins are the primary proteins in milk, crucial for its structure and stability.
Understanding casein behavior is vital for optimizing milk product processing and storage.
Casein micelle structure and interactions influence texture, shelf-life, and processing efficiency.

Purpose of the Study:

To elucidate the role of intrinsically disordered caseins in milk and milk product stability.
To investigate the impact of pH and multivalent ions on casein solubility and micelle integrity.
To present a quantitative model describing casein micelle stability.

Main Methods:

Describing caseins as hydrophilic, intrinsically disordered proteins near neutral pH.
Analyzing the influence of pH and multivalent ion binding on casein solubility.
Utilizing a multivalent-binding model to quantitatively describe casein micelle stability.

Main Results:

Casein solubility is high at neutral pH or above, decreasing as net charge nears zero, and increasing at lower pH.
Free caseins, unbound to calcium phosphate nanoclusters, enhance solubility and act as molecular chaperones.
Casein micelle stability is compromised by the binding of free caseins to amyloid fibrils, destabilized whey proteins, or calcium phosphate.

Conclusions:

Intrinsically disordered caseins play a key role in milk stability through their solubility and chaperone functions.
The pH-dependent solubility and interactions with ions and other proteins dictate casein micelle integrity.
The multivalent-binding model provides a quantitative framework for understanding and predicting milk protein product stability.