Thermoreversible mechanical properties of peanut protein isolate gels induced by ethanol

A novel thermoreversible plant protein hydrogel was fabricated using peanut protein and ethanol. Ethanol-induced protein denaturation enabled peanut protein to form hydrogels at low concentrations (3–7% w/v) through hydrogen bonding and β-sheet interactions. Rheological analysis revealed a reversible sol-gel-sol transition when the temperature was increased and then decreased, with shear modulus values recovering after repeated heating and cooling cycles. Data from Fourier transform infrared and urea disruption analyses suggested that hydrogen bonds were the primary stabilizing forces in these gels, which could be tuned by the presence of ethanol. Cryo-scanning electron microscopy and small angle X-ray scattering analyze highlighted ethanol-dependent microstructural transitions in the samples from uniform dispersions to particulate networks. The system was extended to soy gels, demonstrating its versatility for food applications. The findings advance the development of functional, eco-friendly plant-based protein gels for diverse industrial applications. • A thermal-reversible gel was prepared from peanut proteins and ethanol. • Ethanol enables gel formation at lower protein concentrations. • Thermo-reversibility persisted over 5 heating-cooling cycles. • Hydrogen bonding drives reversible physical crosslinking.