Effects of ultrasonication on structure and gelation of plant proteins at different denaturation states
Year: 2026
Type: article
Abstract: Changing the functionality of plant proteins can improve their applicability in food formulations. In this study, we investigated the effects of ultrasound (US; 20 kHz, 1 h, 2250 J/cm 3 ) as a physical modification technique on faba bean protein isolate (FB, legumin-rich) and mung bean protein isolate (MB, vicilin-rich). The proteins were treated at different thermal states, including 70 °C-treated and 90 °C-treated, and the resulting structure changes (SDS-PAGE, size-exclusion chromatography (SEC), circular dichroism (CD), Fourier-transform infrared (FTIR) spectroscopy, differential scanning calorimetry (DSC), particle size and heat-induced gelation/rheological properties) were evaluated. Ultrasonication reduced particle size without causing protein degradation, but induced partial unfolding of the soluble protein fraction, altered intermolecular interactions, and decreased the denaturation enthalpy. Although G′ and G″ initially decreased after ultrasonication, subsequent heating promoted more effective structural reorganisation of the soluble protein fraction, which may have contributed to the recovery or enhancement of gel network formation, particularly in faba bean protein treated at 90 °C. Overall, these findings demonstrate that ultrasonication modulates the structure of the soluble protein fraction by promoting partial unfolding and reorganising non-covalent aggregates, with the extent of these changes depending on the protein composition and prior thermal state.
Source: Food Hydrocolloids
Authors: Minqian Zhu, Stefan Kasapis, Sushil Dhital
Institutions: Monash University, RMIT University
Language: English
Topic: Proteins in Food Systems
Subfield: Food Science
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $4,990
OpenAlex ID: W7203948425