Journal Articles

Permanent URI for this collectionhttps://mro.massey.ac.nz/handle/10179/7915

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    Fibrillisation of faba bean protein isolate by thermosonication for process efficacy: Microstructural characteristics, assembly behaviour, and physicochemical properties
    (Elsevier Ltd, 2024-09) Hu Y; Cheng L; Gilbert EP; Loo TS; Lee SJ; Harrison J; Yang Z
    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 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.
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    Impact of Ultrasound Emulsification on the Physicochemical Properties of Emulsions Stabilised by Quinoa Protein Isolates at Different pHs
    (Springer Science+Business Media, LLC, 2024-03) Yang Z; Cheng L
    Ultrasonication (20 kHz, 19.9 W/10 mL sample) was used to form O/W emulsions stabilised by quinoa protein isolate (QPI) particles at 3 wt%. Effects of pH (3, 5, 7, 9) and oil volume fractions (20%, 40%, and 60%) on rheological properties and microstructural characteristics of emulsions were investigated. All emulsions show viscoelastic behaviours and form a network structure comprising aggregated oil droplets and QPI particles. Emulsions stabilised by QPI at pH 5 showed largest droplet sizes and lowest gel strength due to extensive aggregation of proteins around the isoelectric point (pI ~ 4.5). The gel strength (G´(1 Hz)) were enhanced when the oil volume fraction increased and reached ~ 1100–1350 Pa at 60% oil volume fraction at different pH. This could be attributed to a tighter packing of oil droplets at 60% oil. Confocal laser scanning microscopy (CLSM) and transmission electron microscopy (TEM) revealed that interdroplets bridging and voids filling of QPI particles between oil droplets are critical in formation of aggregated emulsions network. Emulsions stabilised by QPI at pH 7 and 9 possessed thinner interfacial layers compared to those at pH 3 and 5. Finally, this study shows a potential of using ultrasonication to prepare gel-like emulsions stabilised by QPI, broadening applications of quinoa proteins in making dairy substitutes with semi-solid textural characteristics.
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    Formation and characterisation of concentrated emulsion gels stabilised by faba bean protein isolate and its applications for 3D food printing
    (Elsevier BV, 2023-08-20) Hu Y; Cheng L; Lee SJ; Yang Z
    Concentrated emulsions were prepared at a fixed oil concentration (50 wt%) using faba bean protein isolates (FPI) as an emulsifier and texturizer. Effects of FPI concentration (1, 3 and 5 wt%; at pH7), pH (pH 3, 5, 7, and 9; 3 wt%) and addition of salts (200 mM NaCl and 40 mM CaCl2; at 3 wt% FPI and pH 7) on the emulsion formation were studied. The oil droplet size and microstructural characteristics were examined by static light scattering and confocal laser scanning microscopy (CLSM), and the viscoelastic behaviours of emulsions were characterised by oscillatory rheology. At all different FPI concentrations, the emulsions formed viscoelastic gels with different gel strengths and stability due to network formation and interactions between jammed oil droplets and protein aggregates. The oil droplet size, rheological properties, and 3D printability of emulsions were not significantly changed by the presence of salts. The storage modulus G′ (1 Hz) values were higher at higher FPI concentrations, and higher pH values (i.e., pH 7 and 9) as the droplet size was smaller and the droplet packing was more compact, resulting in a better 3D printing performance. Furthermore, the heat treatment (90 °C for 30 min) remarkedly improved gel strength and the 3D printability because of protein denaturation and oil droplet aggregation. This finding demonstrated that the emulsion gel formed with FPI was tuneable for food 3D printing. Most of samples displayed high printing precision with great self-supporting capability, which may find potential applications in creating specialised diet.