摘要 : The heat-induced interactions between whey proteins and casein micelles were investigated by defining the final product of the reaction when milk was heated up to 90deg C. By examining changes of the interactions in skim milk and ... 展开 The heat-induced interactions between whey proteins and casein micelles were investigated by defining the final product of the reaction when milk was heated up to 90deg C. By examining changes of the interactions in skim milk and in resuspended caseinmicelles, to which different amounts of whey protein had been added, information on the mechanisms that determine the heat-induced protein-protein interactions in milk was derived. The ratio of alpha-lactalbumin and beta-lactoglobulin:kappa-casein and ofalpha-lactalbumin:beta-lactoglobulin found in the micellar pellet were used as indices of these heat-induced reactions occurring in milk. The results suggested that at these low temperature (70-90deg C) with batch heating conditions, whey proteins form soluble complexes which act as intermediates in the heat-induced association of alpha-lactalbumin and beta-lactoglobulin with the micelles. The presence of beta-lactoglobulin was necessary for any association of whey protein with casein micelles to occur. Furthermore, the amount of beta-lactoglobulin found in the micellar pellet after heating was limited by a discrete number of binding sites available on the micelles. 收起