Abstract
SummaryThe effects of combined two heating steps with low (LT, 60 °C for 1 h) and ultrahigh (UHT, 130 or 140 °C for 4 s) temperatures on the thermal gelation of soy protein isolate (SPI) were studied. UHT pretreatments significantly increased protein solubility and enhanced the gelling potential of SPI. Yet, the two‐stage preheating treatment with LT and then UHT‐130 °C had a most remarkable effect: the gel strength of the SPI60+130 sample was, respectively, 1.45‐, 1.64‐ and 3.19‐fold as strong as those of SPI60, SPI25+130, and SPI25. In comparison with single LT or UHT treatments, this two‐stage heating also produced greater amounts of soluble protein aggregates stabilised predominantly by disulphide bonds and hydrophobic forces, contributing to the improved gel network structure.
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