The global trend toward low-fat diets is creating a critical need for efficient fat replacement technologies. This study explored the stabilization behavior of soybean protein isolate (SPI)-citrus pectin (CP) Pickering emulsions and their effectiveness as butter substitutes in pound cakes. The results indicated that emulsions with 5% particle concentration (c) and 50% oil phase volume fraction (ϕ) exhibited excellent storage, centrifugal, thermal, and lipid oxidation stability. It also demonstrated superior structural and rheological properties, effectively replicating the physical characteristics of butter. Moreover, replacing butter with SPI-CP Pickering emulsion significantly enhanced the quality of pound cakes, with a 40% substitution level proving optimal. At this ratio, the specific volume increased by 21.01%, while hardness and chewiness decreased by 57.48% and 52.43%, respectively. Meanwhile, a decrease in fat migration capacity was observed, along with increases in in vitro cholesterol adsorption capacity and sodium cholate adsorption capacity. Electronic nose analysis confirmed similar aroma profiles, and sensory evaluation yielded the highest scores, indicating that the SPI-CP-stabilized emulsion effectively maintained cake quality while serving as a butter alternative. This study offers valuable insights for developing low-fat foods and novel functional ingredients.
Yang Yang, Huixin Zheng, Yue Xu et al.· Food Research International· 0 citations
Despite the advantageous functional properties of soybean protein isolate (SPI), its inherent conformation is susceptible to environmental influences, thereby limiting its utility in food systems. This work investigated the effect of mass ratio between soybean protein isolate (SPI) and citrus pectin (CP) on the structure and functionality of composite particles. Results showed that a 1:1 SPI-to-CP ratio produced the smallest particle size (280.13 nm) and the best dispersion stability. This ratio also significantly improved emulsifying activity (EAI: 54.80 m2/g) and emulsion stability (ESI: 105.91%), while enhancing the adsorption capacity of interfacial proteins. The composite particles were driven by hydrogen bonding, hydrophobic interactions, and electrostatic forces. These interactions promoted the conformational unfolding of SPI, increasing surface hydrophobicity and facilitating a structural transition from α-helix to β-sheet. This work provides fundamental insights for designing food-grade particles with enhanced interfacial activity and stability.
Yang Yang, Xiao-ning Wang, Yue Xu et al.· Food Chemistry· 0 citations