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Skim milk and ultrafiltered milk were heated at temperatures in the range 80–140 °C for 4s in a UHT plate heat exchanger. The extent of denaturation of β-lactoglobulin and its association with the casein micelles increased with increase in heating temperature; the extent of association was markedly less than the amount that denatured. There was no noticeable difference in the extent of denaturation and association of β-lactoglobulin between skim milk and the corresponding ultrafiltered milk. The coagulation properties of renneted heated milks were measured by dynamic oscillation rheometry. Gelation times and storage modulus (G′) could be related to the extent of denaturation of β-lactoglobulin and its association with the casein micelles. Denaturation of β-lactoglobulin up to 60% had no effect on the gelation time, but additional denaturation markedly increased the gelation times. In contrast, G' decreased gradually with increase in the extent of denaturation of β-lactoglobulin and its association with casein micelles. The effects of β-lactoglobulin denaturation and association on coagulation properties were less pronounced in ultrafiltered milk. G' values for ultrafiltered milk were markedly higher than the corresponding skim milks under all heating conditions.  相似文献   
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Abstract

One of the most striking demonstrations of the intermolecular forces is the tension at the surface of a liquid. Recently, a new expression for the surface tension prediction of a binary liquid system. Using the proposed equation, surface tensions are predicted within an overall 2.5 AAD%, which is better than the other available prediction methods.  相似文献   
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