Model infant milk formula systems (5.5% protein) were formulated to contain α-lactalbumin:β-lactoglobulin ratios of 0.1, 0.5, 1.3, 2.1 or 4.6 and assessed for heat stability and heat-induced changes. 'Humanising' the model formulas by increasing α-lactalbumin:β-lactoglobulin enhanced heat stability at 140°C in the pH range 6.6-6.9. The model formulas were analysed after lab-scale high-temperature short-time heating at pH 6.8. Gel electrophoresis indicated that increased heat stability in high α-lactalbumin:β-lactoglobulin samples was due to decreased covalent interactions between proteins. In low α-lactalbumin:β-lactoglobulin formulas, protein-protein interactions caused marked increases in protein particle size and viscosity of the heated systems; conversely, covalent interactions between proteins were minimal in high α-lactalbumin:β-lactoglobulin formulas. Reduced protein-protein interactions with increasing α-lactalbumin:β-lactoglobulin has important implications for subsequent processing; for example, lower viscosity post-heating may affect bulk density in spray-dried products or physical stability in ready-to-feed products.
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