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

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 degrees C > 90 degrees C > 100 degrees C PSPI, for LiFo, LiAc, geraniol, and linalool, nature < 80 degrees C < 90 degrees C < 100 degrees 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 degrees 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.