Heat-induced changes in oil-in-water emulsions stabilized with soy protein isolate

Changes in the structure and dissociation of soybean protein isolate induced by ultrasound-assisted acid pretreatment

“…Li, Wang, Hu, and Liao (2014) reported that more intense high pressure CO 2 treatment caused the dissociation of larger aggregates and further aggregation in the smaller aggregates, which resulted in the change of polyphenol oxidase activity of thaumatin-like protein. The effect of heat_in-duced dissociation and aggregation on the functional properties of soy protein was also reported (Guo et al, 2012;Keerati-u-rai & Corredig, 2009). Both soy 7S and 11S globulin in their isolated form can aggregate on heating, the nature of which depends upon the precise conditions of protein concentration, pH and ionic strength (Li et al, 2007).…”

Flocculation of protein-stabilized oil-in-water emulsions

“…Some representative examples are as follows: the heat-induced flocculation of BSA emulsions [152] and egg-yolk protein emulsions [153] in the presence of surfactant, the flocculation of phosvitin-stabilized emulsions by divalent cations [62,154], the bridging flocculation in emulsions made with a mixture of gelatin + milk protein [155], the depletion flocculation of fish gelatin emulsions by non-adsorbed gelatin [156] and of egg-yolk stabilized emulsions by non-adsorbed egg-white protein (albumen) [157], the heat-induced flocculation of soy protein emulsions [158,159], the bridging flocculation of emulsions prepared with high-pressure-treated soy proteins [160], the saltinduced flocculation of wheat protein emulsions [161], and the flocculation of emulsions made with coconut milk protein near its isoelectric point [162]. For many of these cases, however, one has less confidence (as compared with the milk protein systems) in interpreting the reported stability behaviour in terms of basic colloid science principles.…”

Freeze–thaw stability of emulsions with soy protein isolate through interfacial engineering

“…These biopolymers choose because they are plentiful natural biopolymers with opposite charges. Soy protein isolates (SPI) used as an emulsifier in food emulsions because of the surface-active properties of their constitutive proteins, the storage globulin 7S (β -conglycinin) and 11S (glycinin) and it has positively charged at pHs below its isoelectric point (pI ≈ 4.6) (Huang et al, 2012;Keerati-u-rai and Corredig, 2009;Palazolo et al, 2011). The OSA starch contains a negatively charged carboxylic acid part and could absorb to the positive charged.…”