Journal Articles
Permanent URI for this collectionhttps://mro.massey.ac.nz/handle/10179/7915
Browse
Search Results
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 Impacts of sonication and high hydrostatic pressure on the structural and physicochemical properties of quinoa protein isolate dispersions at acidic, neutral and alkaline pHs(Elsevier BV, 2022-12) Luo L; Yang Z; Wang H; Muthupandian A; Hemar YHerein, 1 wt% quinoa protein isolate (QPI) was exposed to sonication using a 20 kHz ultrasonicator equipped with a 6 mm horn (14.4 W, 10 mL, up to 15 min) or high hydrostatic pressure (HHP, up to 600 MPa, 15 min) treatments at pH 5, pH 7, and pH 9. The changes to physicochemical properties were probed by SDS-PAGE, FTIR, free sulfhydryl group (SH), surface hydrophobicity (H0), particle size and solubility. As revealed by SDS-PAGE, substantial amounts of 11S globulin participated in the formations of aggregates via Ssingle bondS bond under HHP, particularly at pH 7 and pH 9. However, protein profiles of QPI were not significantly affected by the sonication. Free SH groups and surface hydrophobicity were increased after the sonication treatment indicating protein unfolding and exposure of the embedded SH and/or hydrophobic groups. An opposite trend was observed in HHP treated samples, implying aggregation and reassociation of structures under HHP. HHP and sonication treatments induced a decrease in ordered secondary structures (random coil and β-turn) accompanied with an increase in disordered secondary structures (α-helix and β-sheet) as probed by FTIR. Finally, the sonication treatment induced a significant improvement in the solubility (up to ∼3 folds at pH 7 and ∼2.6 folds at pH 9) and a reduction in particle sizes (up to ∼3 folds at pH 7 and ∼4.4 folds at pH 9). However, HHP treatment (600 MPa) only slightly increased the solubility (∼1.6 folds at pH 7 and ∼1.2 folds at pH 9) and decreased the particle size (∼1.3 folds at pH 7 and ∼1.2 folds at pH 9). This study provides a direct comparison of the impacts of sonication and HHP treatment on QPI, which will enable to choose the appropriate processing methods to achieve tailored properties of QPI.