What is the impact of amino acid mutations in the primary structure of caseins on the composition and functionality of milk and dairy products?

Abstract

The impact of amino acid mutations within the peptide structure of bovine milk protein is important to understand as it can effect processability and subsequently effect its physiological properties. Genetic polymorphisms of bovine caseins can influence the chemical, structural, and technological properties, including casein micelle morphology, calcium distribution, network creation upon gelation, and surface activity. The A1 and A2 genetic variants of β-casein have recently acquired growing attention from both academia and industry, prompting new developments in the area. The difference between these two genetic variants is the inclusion of either proline in β-casein A2 or histidine in β-casein A1 at position 67 in the peptide chain. The aim of this review was to examine the extent to which milk and ingredient functionality is influenced by β-casein phenotype. One of the main findings of this review was although β-casein A1 was found to be the dominant variant in milks with superior acid gelation and rennet coagulation properties, milks comprised of β-casein A2 possessed greater emulsion and foam formation capabilities. The difference in the casein micelle assembly, hydrophobicity, and chaperone activity of caseins may explain the contrast in the functionality of milks containing β-casein from either A1 or A2 families. This review provides new insights into the subtle variations in the physicochemical properties of bovine milks, which could potentially support dairy producers in the development of new dairy products with different functional properties.