Interactions of Bioactive Compounds with Milk Proteins

Milk proteins such as caseins and whey constituents form dynamic complexes with a wide range of bioactive molecules, including polyphenols, carotenoids, vitamins and fatty acids. These interactions govern the stability, solubility and functional properties of both the proteins and the bound compounds. Casein micelles, as supramolecular assemblies of phosphoproteins and colloidal calcium phosphate, present hydrophobic and charged domains that enable incorporation of lipophilic nutraceuticals. Whey proteins—chiefly β-lactoglobulin and α-lactalbumin—undergo conformational adjustments upon binding, often leading to enhanced antioxidant capacity and protection of labile bioactives from oxidation and photodegradation. Binding mechanisms encompass non-covalent hydrophobic interactions, hydrogen bonding and electrostatic attraction, as well as covalent conjugation via Maillard chemistry. Spectroscopic and calorimetric techniques have revealed that complexation can stabilise native protein folds while modulating the gastrointestinal release profile of the cargo. In parallel, protein–polysaccharide assemblies and nano-emulsions exploit these interactions to create delivery vehicles that afford targeted release, improved oral bioavailability and sensory functionality. Collectively, these innovations underpin the development of functional foods, nutraceutical formulations and therapeutic platforms designed to address antioxidant delivery, micronutrient supplementation and gut health on a global scale.

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Interactions of Bioactive Compounds with Milk Proteins publication trend

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

Technical terms

Casein micelle: A colloidal assembly of casein proteins and calcium phosphate, forming spherical structures capable of binding hydrophobic molecules.

β-lactoglobulin: The major whey protein in bovine milk, containing a hydrophobic cavity for ligand binding and recognised for its nutritional and functional versatility.

Hydrophobic interaction: Non-polar associations that drive lipophilic molecules to associate with hydrophobic regions of proteins.

Maillard reaction: A non-enzymatic reaction between reducing sugars and amino groups in proteins, resulting in covalent conjugates that modify functional and sensory attributes.