Interactions and Rheological Properties of Milk Proteins

The structural diversity of milk proteins, chiefly casein micelles and whey proteins, underpins a range of interactions that determine texture, stability and flow behaviour in dairy products. Casein micelles provide a colloidal framework stabilised by calcium phosphate, while whey proteins, such as β-lactoglobulin and α-lactalbumin, interact with the casein matrix upon heat treatment to form complexes. These interactions influence gelation kinetics, network microstructure and rheological parameters, including viscoelastic moduli and yield stress. Understanding the balance between covalent and non-covalent bonds, calcium cross-linking and protein aggregation is critical for tailoring product consistency, processing conditions and end-use qualities. Rheological measurements guide the optimisation of cheese curd firmness, yoghurt texture and the stability of acid- or heat-induced gels, with implications for industrial scale-up, sensory attributes and nutritional delivery.

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Interactions and Rheological Properties of Milk Proteins publication trend

The graph below shows the total number of articles in interactions and rheological properties of milk proteins across all publications each year (not limited to Nature Index journals).

Technical terms

Casein micelle: Colloidal aggregates of casein proteins and calcium phosphate that stabilise milk and form the backbone of dairy gels.

Whey proteins: Soluble milk proteins, primarily β-lactoglobulin and α-lactalbumin, that denature and associate with casein during heat treatment.

Rheology: The study of flow and deformation behaviour of matter, applied to assess viscosity, elasticity and yield stress of dairy systems.

Elastic modulus: A measurement of a material’s stiffness, reflecting the ability of a gel network to resist deformation under stress.

Gelation: The process by which proteins aggregate to form a three-dimensional network that traps water and imparts gel structure.

Denaturation: The unfolding of protein secondary and tertiary structures, often induced by heat, leading to new intermolecular interactions.

References

1. Effect of coagulation temperature on cooking integrity of heat and acid-induced milk gels. Food Research International (2023).
2. Inline Determination of the Gel Elastic Modulus During Milk Coagulation Using a Multifiber Optical Probe. Food and Bioprocess Technology (2024).
3. Kinetics of heat-induced interactions among whey proteins and casein micelles in sheep skim milk and aggregation of the casein micelles. Journal of Dairy Science (2022).