Abstract

SummaryThis work compared the thermal stability, microstructure and functional properties of casein (CN) in goat milk processed by different methods, including homogenisation, low‐temperature long‐time (LTLT), high‐temperature short‐time (HTST), ultrapasteurisation (UP) and ultrahigh temperature (UHT) treatment. The greatest development of CN‐whey protein complexes was observed in LTLT goat milk and the least in HTST goat milk. The CN micelles in LTLT, UP and UHT milk were more obviously changed than the CN micelles in HTST milk, and the random coil content increased significantly after the homogenisation, UP and UHT treatments. The homogenisation had a significant effect on the functional properties of CN. In addition, the most obvious changes in the properties of CN were observed in LTLT and UHT goat milk. The results suggested that homogenisation, pasteurisation and UHT can cause effective changes in the functional properties of CN in goat milk that facilitate its application in the milk industry.

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