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Hydrophobic interactions between aroma compounds and beta-Lactoglobulin using a specific fluorescent probe and NMR

Abstract : Many aroma compounds are known to bind with proteins, and elucidating these bindind interactions is a key in a better knowledgment of flavour perception mechanisms (1). beta-Lactoglobulin (bLg), the major whey protein of milk, has been used as a model food protein in numerous studies. Previous work have shown different binding sites on bLg for aroma compounds as a function of their chemical class, and emphasized the importance of hydrophobic interactions (2). (...)
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https://hal.inrae.fr/hal-02754978
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Submitted on : Wednesday, June 3, 2020 - 9:18:51 PM
Last modification on : Thursday, August 5, 2021 - 4:30:02 PM

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  • HAL Id : hal-02754978, version 1
  • PRODINRA : 51460

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Laurette Tavel, Céline Moreau, Eunice Li-Chan, Elisabeth Guichard. Hydrophobic interactions between aroma compounds and beta-Lactoglobulin using a specific fluorescent probe and NMR. 12. Weurman Flavour Research Symposium, Labo/service de l'auteur, Ville service, Pays service., Jul 2008, Interlaken, Switzerland. ⟨hal-02754978⟩

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