The interactions of whey protein isolate (WPI) and flavor compounds (2-nonanone, 1-nonanal, and trans-2-nonenal) were investigated, and the influence of flavor compound structure and heat and high pressure denaturation on the interactions were determined by using headspace solid-phase microextraction (SPME) and gas chromatography (GC). The binding of WPI and the flavor compounds decreased in the order trans-2-nonenal > 1-nonanal > 2-nonanone. The differences in binding can be explained with hydrophobic interactions only in the case of 2-nonanone, whereas the aldehydes, in particular trans-2-nonenal, can also react covalently. Heat and high pressure treatment affected protein-flavor interactions depending on the structure of the flavor compound. Upon both heat and high pressure denaturation, the binding of 2-nonanone to WPI decreased, while the binding of 1-nonanal remained unchanged, and the affinity for trans-2-nonenal increased rapidly. The results suggest that hydrophobic interactions are weakened upon heat or high pressure denaturation, whereas covalent interactions are enhanced.
