This study investigated the effects of controlled thermal modification (95 °C, 10-60 min) on the structural and foaming properties of soybean lipophilic protein (SLP). Results indicated that moderate heating (10-30 min) triggered structural unfolding, increased hydrophobic group exposure and free sulfhydryl content, and reduced aggregation. Notably, compared to individual protein samples, a 1:1 (w/w) mixture of native and moderately heat-treated SLP jointly promoted protein adsorption at the interface, and facilitated the conformational evolution of the modified protein to form a mechanically robust and dense composite film, thereby substantially improving overall foaming capacity and stability. Conversely, 60-min heat treatment induced large, ordered aggregates that hindered interfacial adsorption and the development of a stable film, compromising the overall foaming performance. These findings offer new insights into the strategic application of SLP in aerated food systems.
Native soybean lipophilic protein (SLP) readily forms compact aggregates through strong hydrophobic interactions, impairing its water solubility and interfacial adsorption capacity. This study investigated the effects of high-speed shearing followed by genipin crosslinking on the structural and functional properties of...
Xumei Feng, Li-Jia Li, Yan-Wei Zou et al.· Food Chemistry· 0 citations
This study investigated the effects of water activity () and pH on the properties of hot‐pressed soy protein isolate (SPI) sheets. SPI and glycerol (1:1 mass ratio) were equilibrated under various (~0–0.75) prior to fabrication. Transparent sheets were obtained at , whereas they became opaque at . Differential scanni...
Mio Kurata, Airi Sonokawa, Aoi Yanagihara et al.· Journal of Applied Polymer S...· 0 citations
Oil separation limits peanut butter quality and shelf life. This study investigated the effect of heat-induced aggregation of peanut protein isolate (PPI) at 60–100 °C on its structural, functional properties, and evaluated its application as a stabilizer in peanut butter. Thermal treatment altered PPI conformation—mos...
The utilization of jack bean protein isolate (Canavalia ensiformis) and its modification as an emulsifier for stabilizing red fruit oil (Pandanus conoideus) emulsions remains underexplored. This study investigated the effects of pH-shifting, heat treatment, ultrasonication, and their combinations on the structural, int...
David Agusta Chandra, V. Armetha, Nadine Kurniadi et al.· Food Research International· 0 citations
While the bioactivity of pulse protein hydrolysates is widely studied, the holistic impact of unit operations from flour to final powder remains unexamined. This study produced black bean hydrolysate powders using enzyme‐assisted extraction, direct steam injection (low temperature, LT: 130°C/15 s, or high temperature,...
Jasmin S. Yang, Mayara Kuasnei, T. B. Pessato et al.· Sustainable Food Proteins· 0 citations
Achieving long-term stability of oil-in-water emulsions through robust interfacial films remains challenging. This study aimed to address this challenge by using hydrolyzed soy protein isolate-tannic acid-citrus pectin (HSPI-TA-CP) ternary complexes as stabilizers and investigating the effects of complex concentration...
Ying-Ying Zhang, Rui Shi, Jia-Ling Long et al.· Food Chemistry· 0 citations
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