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Structuring liquid oil into a self-standing semisolid material without trans and saturated fat has become a challenge for the food industry after the recent ban of trans fat by the US Food and Drug Administration and Health Canada. Lately, the use of hydrocolloids such as animal proteins and modified cellulose for oleogel preparation has gained more attention. However, plant proteins have never been explored for the development of oleogels. The present study explored the use of freeze-dried foams prepared using protein concentrates and isolates of pea and faba bean with xanthan gum at different pH values for oil adsorption and subsequent oleogelation. Compared to protein isolate stabilized foams, protein concentrate-stabilized foams displayed (i) higher oil binding capacity (OBC) due to a higher number of smaller pore size; and (ii) lower storage modulus and firmness due to the higher oil content. At all pH values, there was no significant difference between the OBC of different protein isolates, but among the concentrates, pea displayed higher OBC than faba bean at pH 5 and faba bean displayed higher OBC than pea at pH 9. Results showed that such oleogels could be used as a shortening alternative. Cakes prepared using the pea protein-based oleogel at pH 9 displayed a similar specific volume as that of shortening-based cake, although with higher hardness and chewiness. ; Tel: +1 306 966 2555 † Electronic supplementary information (ESI) available. See

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Sodium caseinate (SC)-stabilized 40% oil-in-water nanoemulsions (NEs) could be transformed into elastic gels below a critical droplet size due to increase in ϕeff by a thicker steric barrier of SC, while whey protein (WPI)-stabilized NEs remained liquid due to thinner steric barrier of WPI.

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Use of oleogels prepared from hydrocolloids has recently gained considerable attention as an alternative for trans and saturated fats. Lately, pulse proteins such as faba bean protein and pea protein have been successfully used to prepare oleogels using a foam‐templated approach. Although the pulse proteins are healthy oleogelators, high oil loss and low quality of cake baked using pulse protein‐stabilized oleogels due to its poor rheological properties challenged its use. The present study explored whether the addition of small amount of high‐melting monoglyceride (MAG) or candelilla wax (CW) can be used to improve the oil binding capacity, rheological properties, and baking qualities of pulse protein‐stabilized oleogels composed of 5% faba bean or pea protein concentrate with 0.25% xanthan gum foams. Different concentrations (0.5–3%) of MAG or CW were dissolved in canola oil at 80 °C, followed by addition into the freeze‐dried protein‐polysaccharide foams (pH 7) and quickly transferred to a refrigerator to facilitate the formation of oleogels. The crystallized additives were found to be reinforcing the protein foam network in the oleogels. With increase in concentration of CW and MAG, the oil binding capacity, firmness, cohesiveness, and storage moduli of the oleogels were increased. Oleogels with and without MAG or CW were then characterized and tested for their performance as a shortening replacer in model baked cakes. Findings showed improved textural properties of cake upon addition of MAG in the foam‐templated oleogels, however, compared to the shortening, negative effect on cake hardness and chewiness was still observed with the oleogels.

This research aimed to investigate the possibility of forming gelled nanoemulsions (NEs) by inducing attractive interactions among the nanodroplets. The effect of salt concentration and changes in pH on the stability and gelation behavior of 2, 4, and 5% sodium caseinate (SC) and whey protein isolate (WPI)-stabilized 40% canola oil-in-water NEs were investigated. For the effect of salt, sodium chloride was added in a concentration of 0.1, 0.5, and 1 M in the continuous phase of the NEs at neutral pH, whereas to study the effect of acidification, the pH of the NEs was adjusted to the isoelectric point (pI) of the proteins. The addition of salt led to attractive gelation in WPI NEs because of a screening of charge. In contrast, the gel strength of SC-stabilized NEs was reduced with salt, which was attributed to the loss of close packing of droplets and their surrounding repulsive barriers because of charge screening and to the steric barrier of interfacial SC preventing droplet aggregation. All the NEs with pH at the pI of proteins transformed into strong attractive gels made of droplet aggregates irrespective of the type or concentration of protein because of the complete charge neutralization. The strength of the acidified NE gels increased with a decrease in droplet size and the type of protein used. Overall, research on the effect of different environmental factors on the stability and gelation behavior of protein-stabilized NEs could be useful for possible applications of these nanoscale materials in various food systems.

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