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Fibrillisation of faba bean protein isolate by thermosonication for process efficacy: Microstructural characteristics, assembly behaviour, and physicochemical properties

Yinxuan Hu, Lirong Cheng, Elliot P. Gilbert, Trevor S. Loo, Sung Je Lee, John A. Harrison, Zhi Yang

2024Food Hydrocolloids21 citationsDOIOpen Access PDF

Abstract

The 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 5-10 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.

Topics & Concepts

ThioflavinFourier transform infrared spectroscopyCircular dichroismChemistrySodium dodecyl sulfateDynamic light scatteringSmall-angle X-ray scatteringGel electrophoresisFibrilChromatographyAnalytical Chemistry (journal)CrystallographyMaterials scienceChemical engineeringScatteringBiochemistryNanoparticleNanotechnologyMedicineDiseaseEngineeringPhysicsAlzheimer's diseaseOpticsPathologyProteins in Food SystemsFood composition and propertiesFood Chemistry and Fat Analysis