Suspensions (2% and 5%, w/v) of soy protein isolate (SPI) were heated at 80, 90, or 100 °C for different time periods to produce soluble aggregates of different molecular sizes to investigate the relationship between particle size and surface properties (emulsions and foams). Soluble aggregates generated in these model systems were characterized by gel permeation chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Heat treatment increased surface hydrophobicity, induced SPI aggregation via hydrophobic interaction and disulfide bonds, and formed soluble aggregates of different sizes. Heating of 5% SPI always promoted large-size aggregate (LA; >1000 kDa) formation irrespective of temperature, whereas the aggregate size distribution in 2% SPI was temperature dependent: the LA fraction progressively rose with temperature (80→90→100 °C), corresponding to the attenuation of medium-size aggregates (MA; 670 to 1000 kDa) initially abundant at 80 °C. Heated SPI with abundant LA (>50%) promoted foam stability. LA also exhibited excellent emulsifying activity and stabilized emulsions by promoting the formation of small oil droplets covered with a thick interfacial protein layer. However, despite a similar influence on emulsion stability, MA enhanced foaming capacity but were less capable of stabilizing emulsions than LA. The functionality variation between heated SPI samples is clearly related to the distribution of aggregates that differ in molecular size and surface activity. The findings may encourage further research to develop functional SPI aggregates for various commercial applications.
This study investigated the mechanism of instability of soy protein isolate (SPI) as influenced by thermal aggregation during SPI preparation. Samples with different degrees of aggregation but similar protein solubility were prepared by heating native SPI (5 % w/v) at 80 or 90 °C for different times before spray‐drying. The samples were then stored at 37 °C for up to 12 weeks and analyzed periodically by atomic force microscopy, gel permeation chromatography, and SDS–PAGE. All SPI samples underwent remarkable protein solubility decreases during the first 8 weeks of storage. The rates of solubility loss were positively correlated with the amounts and/or sizes of soluble aggregates contained in the initial samples (time zero), suggesting their nucleation and activation effects. Solubility tests in SDS–urea solutions and disulfide analysis indicated that non‐covalent interactions were the main driving forces for protein storage instability. Conversely, disulfide bonds and protein carbonyls were abundant in soluble aggregates, and their content increased markedly during storage. This effect suggested that covalent linkages acted as blockers for hydrophobic aggregation.
The 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 SPI 60+130 sample was, respectively, 1.45-, 1.64-and 3.19-fold as strong as those of SPI 60 , SPI 25+130 , and SPI 25 . 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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