Physical properties of emulsion gels formulated with sonicated soy protein isolate

Abstract

This study aimed to determine the effect of high‐intensity ultrasound (HIU) on physical properties of soy protein isolate dispersions (SPI) and their addition to emulsion gels (EG) containing soybean oil (SBO), inulin (IN) and carrageenan (CAR). Sonicated and non‐sonicated SPI dispersions were mixed with CAR, IN and SBO and heated at 90 °C for 30 min to gel the emulsion. An increase in solubility and oil binding capacity was observed in sonicated SPI dispersions (S‐SPI) compared to the non‐sonicated ones. HIU changed the molecular weight of SPI and decreased apparent viscosity in the dispersions. The use of S‐SPI in the EG reduced the droplet size and increased the hardness and G′ values. The use of S‐SPI allowed a reduction of 75% of carrageenan in the EG without affecting the hardness of the gel. The results suggest that HIU can be used to improve rheological properties of functional EG.

Effect of soy protein isolate on the techno‐functional properties and protein conformation of low‐sodium pork meat batters treated by high pressure

“…The TR, WR, and FR were significantly decreased ( p < .05) with soy protein isolate increased. It is well known that as a binder or filling agent of commonly useful vegetable protein in the meat industry, soy protein isolate has a good water and fat holding capacity, excellent gelling and structuring behavior (Berghout, Boom, & Goot, ; Kang et al, ; Paglarini, Martini, & Pollonio, ). Meanwhile, the emulsifying activity of 11S globulins was much significantly improved at 200 MPa, which enhanced the emulsified stability of soy protein isolate (Tang & Ma, ).…”

Influence of transglutaminase‐assisted ultrasound treatment on the structure and functional properties of soy protein isolate

“…Ultrasound treatment caused cavitation bubbles collapse and increased local pressure and temperature in bubbles' surrounding area, resulting in unfolding of protein and breaking of peptide bonds, and exposing hydrophilic amino acid residues to water, thus improving the solubility of SPI. On the other hand, Paglarini and et al () found that the ultrasound treatment can reduce the SPI particle size, causing conformational changes in proteins and the formation of soluble protein aggregates, which can enhance protein–water interactions, resulting in higher solubility of SPI. The solubility of TSPI samples decreased drastically (Table ), which could be due to the formation of insoluble aggregates during cross‐linking (Song & Zhao, ).…”

“…Hu, Li‐Chan, Wan, Tian, and Pan () explored a novel approach to make SPI gel with higher gel strength by ultrasonication. Paglarini, Martini, and Pollonio () showed that high‐intensity ultrasound is an efficient tool to improve the functional properties of SPI dispersions increasing their solubility and oil binding capacity.…”

Improving Stability and Accessibility of Quercetin in Olive Oil-in-Soy Protein Isolate/Pectin Stabilized O/W Emulsion

“…Unlike conventional emulsifying procedure, Kobayashi prepared monodispersed stable emulsion by using microchannel emulsification [33]. More researchers [34][35][36][37] used ultrasonic treatment to obtain small droplet size emulsion by benefiting from ultrasonic cavitation function [38]. It was reported that ultrasonic treatment can improve surface hydrophobicity, surface activity and protein aggregation.…”