Binding of aroma compounds with soy protein isolate in aqueous model: Effect of preheat treatment of soy protein isolate

Abstract

The interactions between flavors (hexyl acetate [HxAc], heptyl acetate [HpAc], linalyl formate [LiFo], linalyl acetate [LiAc], geraniol, linalool, limonene and myrcene) and soy protein isolate (SPI) were investigated, the influence of flavors structure and preheated SPI (PSPI) were determined by using headspace solid-phase microextraction gas chromatography–mass spectrometry (HS–SPME/GC–MS) technology. For HxAc and HpAc, the binding of SPI and the flavors decreased in the order nature > 80 °C > 90 °C > 100 °C PSPI, for LiFo, LiAc, geraniol, and linalool, nature < 80 °C < 90 °C < 100 °C PSPI. For limonene and myrcene, an increase in headspace concentration or “salting out” effect was noticed. The NSPI (nature SPI) and PSPI of 80 °C showed two class binding sites for HxAc and HpAc. These results serve as a foundation for further investigation into the effect of preheating of SPI on its ability to bind to flavor-inducing compounds.