Whey thermal properties

MT Patel, A Kilara, LM Huffman, SA Hewitt, AV Houlihan. Studies on whey protein concentrates. 1. Compositional and thermal properties. J Dairy Sci 73 1439-1449, 1990. 

Harwalker, V. R. 1979. Comparison of physico-chemical properties of different thermally denatured whey proteins. Milchwissenschaft 34, 419-422,... 

Homogenization of cream results inevitably in the formation of a secondary fat globule membrane, consisting predominantly of micellar casein and (denatured) whey proteins (Walstra et al., 1999). To obtain desirable product properties, the formation of larger, thermally induced... 

Aguilera, J.M., and Baffieo, P. (1997). Structure-meehanieal property relationships in thermally induced whey protein-eassava stareh gels. J. FoodSci. 62, 1048-1053. 

Aguilera, J. M. and Rojas, E. 1996. Rheological, thermal and microstructural properties of whey protein-cassava starch gels. J. Food Sci. 61 962-966. 

A combination of heat and shear has been used to create whey protein particles with controlled particle size and properties. A well-known example of the use of microparticulation of thermally denatured whey protein is for the production of Simplesse 100, a whey-based fat replacer (Lieske and Konrad, 1993). Shear can be used to modulate gel properties of whey protein isolate gels. 

The dissociation of a quaternary structure or denaturation of proteins is required prior to emulsification. Therefore, casein micelles are adsorbed at an interface in a semi-intact form (Oortwijn et al., 1977). The thermal denaturation of globular proteins prior to emulsification was reported to improve the emulsifying properties. The high level of the thermally denatured whey protein fraction in mixed proteins (of denatured and undenatured proteins) increased the emulsion viscosity and coalescence stability compared with the low-level denatured fraction (Britten et al., 1994). 

The conformational changes in /J-lactoglobulin during foaming and thermal denaturation were studied by H NMR and 2H exchange spectroscopy.92-93 The properties of three equine whey proteins, alpha-lactoalbumin, /J-lactoglobulin, and lysozyme, have been studied and compared with those of the corresponding bovine milk.94... 

Kokoszka, S., Debeaufort, F., Lenart, A., Voilley, A. Water vapour permeability, thermal and wetting properties of whey protein isolate based edible films. Int. Dairy J. 20, 53-60 (2010)... 

It should be noted that ultrasonic technology is a non-thermal process and hence very little changes to the physical and functional properties of dairy system is observed due to sonication. In most studies, the processing time required is a few seconds to less than a minute. In order to evaluate the effect of sonication on the constituents of milk, Chandrapala et al. [85] and Shanmugam et al. [86] carried out extensive research in recent years. Their studies have shown that sonication of a dairy system causes very little changes to the physical properties of whey proteins. They observed reversible changes to partial denaturation of whey proteins. In order to see the effect, the constituents of whey proteins, namely, pure- and 3 1 mixtures of p-Lactoglobulin (P-LG) and a-Lactalbumin (a-LA)... 

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