Journal Articles
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Item Impact of thermosonication at neutral pH on the structural characteristics of faba bean protein isolate dispersions and their physicochemical and techno-functional properties(Elsevier Ltd, 2024-09) Hu Y; Cheng L; Gilbert EP; Lee SJ; Yang ZThe effect of thermosonication (TS) (90 °C, 10–30 min) on faba bean protein isolate (FPI) at pH 7 was investigated. The microstructural and techno-functional properties of TS-treated FPI were compared with native FPI or FPI treated with conventional prolonged heating (CH, up to 8 h) at 90 °C. TS treatment effectively converted FPI to amorphous aggregates containing predominant β-sheet secondary structures, as determined by Thioflavin T (ThT) fluorescence and circular dichroism (CD). According to sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), these amorphous aggregates could be formed by disulfide bonds. Additionally, TS treatment is efficient in disrupting large protein aggregates of FPI, thus improving their solubility. Both TS and CH treatments induced formation of viscoelastic FPI hydrogels, whose gel strength depends on the type and time of treatment. Hydrogels formation is likely to arise from the entanglement and interaction of protein aggregates as revealed by small angle neutron scattering (SANS) and scanning electron microscopy (SEM). TS-treated FPI was also used to prepare O/W emulsions and whose structural and physical properties were compared with those stabilised by untreated FPI. At all oil volume fractions (φ = 0.2, 0.5, and 0.7) and FPI concentrations (1, 3, and 5 wt %), emulsions stabilised by TS-treated FPI exhibited smaller oil droplet size, greater mechanical strength and superior stability compared to those stabilised by untreated FPI. The study suggests that TS treatment is promising in improving techno-functional properties of FPI; further studies are needed to exploit TS-treated plant proteins as a novel food ingredient in food product development.Item Formation of by high power ultrasound aggregated emulsions stabilised with milk protein concentrate (MPC70)(Elsevier BV, 2021-12-03) Zhang R; Luo L; Yang Z; Ashokkumar M; Hemar YIn this work, oil-in-water emulsions stabilised by milk protein concentrate (MPC70) were investigated. The MPC70 concentration was kept constant at 5% (close to the protein content found in skim milk) and the oil volume fraction was varied from 20 to 65%. Sonication was performed at 20 kHz and at a constant power of 14.4 W for a total emulsion volume of 10 mL. Under certain oil concentration (≥35%) and sonication times (≥3s) the emulsion aggregated and formed high-viscosity pseudo plastic materials. However, the viscosity behaviour of the emulsion made with 35% oil reverted to that of a liquid if sonicated for longer times (≥15 s). Confocal laser scanning microscopy showed clearly that the oil droplets are aggregated under the sonication conditions and oil concentrations indicated above. An attempt to explain this behaviour through a simple model based on the bridging of oil droplets by the MPC70 particles and, taking into account the oil droplet and MPC70 particle sizes as well as the oil volume fraction, was made. The model fails to describe in details the aggregation behaviour of these emulsions, likely due to the inhomogeneous protein layer, where both free caseins and casein micelles are adsorbed, and to the packing of the oil droplets at concentrations ≤55%. Nonetheless, this work demonstrates the potential of ultrasound processing for the formation of dairy emulsions with tailored textures.Item Limited Alcalase hydrolysis improves the thermally-induced gelation of quinoa protein isolate (QPI) dispersions(Elsevier BV, 2022-11-01) Wang X; Cheng L; Wang H; Yang ZGelation is critical in many food applications of plant proteins. Herein, limited hydrolysis by Alcalase was used to promote thermally induced gelation of quinoa protein isolates (QPI). Mechanical properties of various QPI gels were characterised by small and large oscillatory shear deformation rheology while the microstructural features were observed by confocal laser scanning microscopy (CLSM). Both the gel strength and microstructure are strongly related to the hydrolysis time. The maximum gel strength (∼100 Pa) was achieved after Alcalase hydrolysis for 1 min, which was ∼20 folds higher than that of untreated QPI. Extended hydrolysis up to 5 min progressively decreased the gel strength. A string-like interconnected protein network was formed after proteolysis. The change of gel strength with hydrolysis time correlated well to the Gʹ 20°C/Gʹ 90°C value and results of intrinsic fluorescence and surface hydrophobicity. The Gʹ 20°C/Gʹ 90°C value is sensitive to hydrogen bonds formation while the intrinsic fluorescence and surface hydrophobicity are associated with protein unfolding and exposure of hydrophobic groups. Therefore, both hydrogen bonding and hydrophobic interactions are critical in improving the gel strength of QPI hydrolysates. Finally, FTIR analysis revealed that protein secondary structures are affected by the proteolysis and formation of inter-molecular hydrogen bonds between polypeptides. This study provides an efficient strategy for improving thermally induced gelation of QPI and enables a deep understanding of QPI gelation mechanism induced by Alcalase hydrolysis.Item Comparative study on the rheological properties of myofibrillar proteins from different kinds of meat(Elsevier Ltd, 2022-01) Wang H; Yang Z; Yang H; Xue J; Li Y; Wang S; Ge L; Shen Q; Zhang MIn this study, the gel properties of myofibrillar proteins (MPs) from four meat sources (fish, beef, sheep, and pork) were compared. Oscillatory rheology measurements including temperature sweep, frequency sweep, and strain sweep were conducted to characterise the small and large deformation rheological properties of the MPs. In addition, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and scanning electron microscopy (SEM) were used to evaluate differences in the molecular weight distribution as well as the microstructures in gel among different MPs. Frequency sweep measurements showed that all MP gels were weak gels. MPs extracted from pork exhibited the highest gel strength and most compact gel structure, whereas those from fish exhibited the lowest gel strength and loosest gel structure. In addition, the MP extracted from pork (PSM) had the highest content of myosin heavy chain (MHC) and actin. In conclusion, the MPs extracted from fish source and mammalian sources varied significantly in terms of rheological properties and microstructural characteristics. These results provided useful information for developing mixed gel products with different gel strengths.Item Impact of incorporations of various polysaccharides on rheological and microstructural characteristics of heat-induced quinoa protein isolate gels(Springer Science+Business Media, LLC, 2022-09) Patole S; Cheng L; Yang ZThis study aimed to investigate the properties of heat-induced gels (85 °C for 30 min) of quinoa protein isolate (QPI) in the presence and absence of various polysaccharides including guar gum (GG), locust bean gum (LBG), and xanthan gum (XG) at pH 7. For this purpose, samples with three gum concentrations (0.05, 0.1, and 0.2 wt%) at a fixed QPI concentration (10 wt%) and a fixed ionic strength (50 mM NaCl) were studied in terms of their gelation behaviour, small and large deformation rheological properties, water holding capabilities, and microstructural characteristics. Rheological measurements revealed that all polysaccharides incorporation could improve gel strength (complex modulus, G*) and breaking stress, accelerate gel formations, and more stiffer gels were obtained at greater polysaccharide concentrations. The XG exhibited the most gel strengthening effect followed by LBG and GG. Incorporation of 0.2 wt% XG led to a 15 folds increase in G* compared to the control. Confocal laser scanning microscopy observation revealed that the polysaccharides also altered gel microstructures, with the gels containing XG showing the most compact gel structures. The findings of this study may provide useful information for the fabrication of novel QPI based food gel products with improved texture.