Changes of secondary structure and protein interactions of whey protein (WPs) present in native, sweet, acid and salty-WPCs were analyzed following storage at 4, 25 or 45 °C and 22 or 33% relative humidity for a period of 90-days. WPs aggregated predominantly through covalent crosslinking, achieving maximum at 45 °C and 33% RH. Greater participation of β-lactoglobulin in covalent crosslinking was evident in all WPCs, while that of α-lactalbumin was significantly (p < 0.05) high in acid-WPC only. Reaction order of β-LG denaturation in acid and salty-WPCs was approximately 2 while approximately 1 in native and sweet-WPCs. Activation energy was significantly (p < 0.05) higher in native and sweet-WPCs, with averages recorded as 97 and 49.8 kJ mol−1, respectively, than that in acid and salty-WPCs with averages of 27.5 and 33.8 kJ mol−1, respectively, mainly attributed to inherently high concentrations of lactic acid and salts in these WPCs.
Journal of Food Engineering – Elsevier
Published: Dec 1, 2017
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