Wang Z.,Northeast Agricultural University |
Liang J.,Northeast Agricultural University |
Jiang L.,Northeast Agricultural University |
Li Y.,Northeast Agricultural University |
And 8 more authors.
CYTA - Journal of Food | Year: 2015
The effect of the interaction between myofibrillar protein (MP) and heat-induced soy protein isolates (SPI) on gel properties was examined. To enhance the interaction between MP and SPI, SPI was subjected to thermal treatments at 60, 80, and 95 °C. The results showed that hydrophobic interactions played the most important role in MP-heated SPI (HSPI) gels. Hydrogen bonds played an important role in stabilizing the mixed gels, but this decreased with increasing heat treatment temperature of SPI. Disulfide bonds were not a significant force stabilizing the mixed gels. The gel properties of HSPI-MP were enhanced significantly (P < 0.05) by the inclusion of preheated SPI (95 °C, 30 min), including hardness, springiness, and water-holding capacity (WHC). Dynamic rheological analysis showed that heat treatment decreased the onset temperature of mixed gels and significantly increased the final G'. Notable cross-linked strands formed in MP-HSPI (80 °C) and MP-HSPI (95 °C) gels, while the smoothest and most ordered gel network structure was observed in the MP-HSPI (95 °C) gel. © 2015 The Author(s). Published by Taylor & Francis.