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Using DSC for monitoring protein conformation stability and effects on fat droplets crystallinity in complex food emulsions

  • Chapter
The Nature of Biological Systems as Revealed by Thermal Methods

Part of the book series: Hot Topics in Thermal Analysis and Calorimetry ((HTTC,volume 5))

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Conclusion

DSC is used to investigate heat-induced conformational or structural changes of a broad range of food ingredients (biopolymers, proteins, fats, sugars, emulsifiers) in various physico-chemical conditions, and at various weight fractions of water. Detailed description of principles and methodologies employed to obtain DSC signals and to extract information may be found in the large body of data that were published since several de cades. They show a great influence of several intrinsic and extrinsic factors on calorimetric data, making difficult any generalization. In the present work, we showed that DSC can give valuable information on how examples of protein solutions and emulsions behave under various physico-chemical conditions used for preparation of complex food emulsions. Besides the well established effects of physico-chemical environmental parameters on heat-induced conformation changes of globular proteins, DSC in scanning mode can be used for evaluation of growing of fat crystals in complex food emulsions as a function of cooling temperature and in relation to other characteristics of emulsion stability.

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  1. Unité Mixte de Recherche Science de ľAliment et de ľEmballage 1, Ecole Nationale Supérieure des Industries Alimentaires, Avenue des Olympiades, F- 91 744, Massy, France

    P. Relkin

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  1. Biophysical Department, Faculty of Medicine, University of Pécs, Hungary

    Dénes Lörinczy

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Relkin, P. (2004). Using DSC for monitoring protein conformation stability and effects on fat droplets crystallinity in complex food emulsions. In: Lörinczy, D. (eds) The Nature of Biological Systems as Revealed by Thermal Methods. Hot Topics in Thermal Analysis and Calorimetry, vol 5. Springer, Dordrecht. https://doi.org/10.1007/1-4020-2219-0_5

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