Abstract: In contrast to the caseins, whey proteins, including beta-lactoglobulin, alpha-lactalbumin, bovine serum albumin and immunoglobulins, exhibit well developed secondary and tertiary structures and are therefore susceptible to protein denaturation. Although protein denaturation can be induced by a variety of agents, thermal denaturation is of greatest industrial significance. Because almost all dairy processes involve the use of heat, a better understanding of the effects of heat on whey proteins in dairy foods is desirable. However, the thermal behaviour of whey protein has generally been studied in simple model systems, rather than real foods. Furthermore, reported values for the thermodynamic properties of individual whey proteins, such as temperatures and enthalpies of denaturation and activation energies, vary widely, reflecting differences in methodology and environmental conditions. Elucidating the thermal behaviour of whey proteins and their interactions with other food constituents, especially the caseins, might permit the development of new functionalization treatments and/or improvement of existing technological processes.
Publication Year: 1995
Publication Date: 1995-01-01
Language: en
Type: article
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Cited By Count: 61
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