Hu YCheng LGilbert EPLoo TSLee SJHarrison JYang Z2024-05-152024-05-152024-09Hu Y, Cheng L, Gilbert EP, Loo TS, Lee SJ, Harrison J, Yang Z. (2024). Fibrillisation of faba bean protein isolate by thermosonication for process efficacy: Microstructural characteristics, assembly behaviour, and physicochemical properties. Food Hydrocolloids. 154.0268-005Xhttps://mro.massey.ac.nz/handle/10179/69568The effect of thermosonication (TS) (90 °C, 10–30 min) on the fibrillisation of faba bean protein isolate (FPI) was studied. The self-assembly behaviour, microstructural characteristics and techno-functional (gelation and emulsification) properties of FPI fibrils obtained from TS treatment were compared with those obtained from conventional prolonged heating (CH) at 90 °C up to 8 h. Compared to CH treatment, TS treatment was shown to significantly accelerate the formation of FPI fibrils with prominent β-sheet structures as revealed by Thioflavin T (ThT) fluorescence, Fourier-transform infrared spectroscopy (FTIR) and circular dichroism (CD). The characteristics of fibril building blocks were analysed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and liquid chromatography linked to tandem mass spectrometry (LC-MS/MS) to obtain the differences between TS and CH induced fibrillisation of FPI. Transmission electron microscopy (TEM) and small-angle neutron scattering (SANS) showed that 4 h CH and 10 min TS treatments resulted in the fibrils with similar radius (from 5 to 10 nm). Furthermore, SANS indicated that TS treatment induced the formation of an entangled FPI fibrillar network, which could lead to the observed viscoelastic properties of FPI at a high concentration (10 wt%). Finally, high internal phase O/W emulsions (HIPE, φ = 0.75) stabilised by 30 min TS induced FPI fibrils (3 wt%) demonstrated a stronger gel strength and smaller oil droplet size compared to those prepared with untreated FPI, suggesting a superior emulsification capability of FPI fibrils. This finding demonstrates that TS treatment is a promising and efficient method for fibrillisation of plant proteins with the resultant fibrils generating excellent gelation and emulsification properties.(c) 2024 The Author/sCC BY-NC 4.0https://creativecommons.org/licenses/by-nc/4.0/ThermosonicationSelf-assembly fibrilsFaba bean protein isolatesSmall angle neutron scatteringHigh internal phase emulsionsMicrostructuresJournal article10.1016/j.foodhyd.2024.1101271873-7137journal-article110127S0268005X24004016