Binding of dual‐flavour compounds by soy protein isolate in aqueous model systems

Summary By the technique of headspace solid‐phase microextraction/gas chromatography–mass spectrometry (SPME‐GC/MS) and static headspace/gas chromatography (HS/GC), the interaction of dual‐flavours and soy protein isolates (SPI) was determinated at low flavour concentration (0.04–0.16 m m ) and high flavour concentration (0.4–1.6 m m ). The results show that the mixture of ethyl caprylate and undecanal that has elongated structure possesses the same binding sites on SPI and shows competitive binding; the mixture of carvone that has compact structure, at low flavour concentration, possesses different and independent binding sites on SPI, and there maybe existed noncompetitive binding. If high concentration multi‐flavour binding with SPI induces the conformational change and increased more binding sites for another single flavour, there may be existed anticompetitive binding. ‘Salt out’ effects of interaction model were observed for terpene flavours.