Journal Articles
Permanent URI for this collectionhttps://mro.massey.ac.nz/handle/10179/7915
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Item Self-assembly and hydrogelation of a potential bioactive peptide derived from quinoa proteins(Elsevier BV, 2024-02) Cheng L; De Leon-Rodriguez L; Gilbert EP; Loo T; Petters L; Yang ZIn this work the identification of peptides derived from quinoa proteins which could potentially self-assemble, and form hydrogels was carried out with TANGO, a statistical mechanical based algorithm that predicts β-aggregate propensity of peptides. Peptides with the highest aggregate propensity were subjected to gelling screening experiments from which the most promising bioactive peptide with sequence KIVLDSDDPLFGGF was selected. The self-assembling and hydrogelation properties of the C-terminal amidated peptide (KIVLDSDDPLFGGF-NH2) were studied. The effect of concentration, pH, and temperature on the secondary structure of the peptide were probed by circular dichroism (CD), while its nanostructure was studied by transmission electron microscopy (TEM) and small-angle neutron scattering (SANS). Results revealed the existence of random coil, α-helix, twisted β-sheet, and well-defined β-sheet secondary structures, with a range of nanostructures including elongated fibrils and bundles, whose proportion was dependant on the peptide concentration, pH, or temperature. The self-assembly of the peptide is demonstrated to follow established models of amyloid formation, which describe the unfolded peptide transiting from an α-helix-containing intermediate into β-sheet-rich protofibrils. The self-assembly is promoted at high concentrations, elevated temperatures, and pH values close to the peptide isoelectric point, and presumably mediated by hydrogen bond, hydrophobic and electrostatic interactions, and π-π interactions (from the F residue). At 15 mg/mL and pH 3.5, the peptide self-assembled and formed a self-supporting hydrogel exhibiting viscoelastic behaviour with G' (1 Hz) ~2300 Pa as determined by oscillatory rheology measurements. The study describes a straightforward method to monitor the self-assembly of plant protein derived peptides; further studies are needed to demonstrate the potential application of the formed hydrogels in food and biomedicine.Item Formation and properties of highly concentrated oil-in-water emulsions stabilized by emulsion droplets(Elsevier Ltd, 2023-12) Cheng L; Ye A; Yang Z; Hemar Y; Singh H70% (v/v) concentrated emulsion has been prepared using Ca2+-cross-linked sodium caseinate particles (Ca-CAS) or Ca-CAS coated nano-sized primary emulsion droplets as emulsifiers. The primary droplet-stabilised emulsion (DSE) was compared with the conventional Ca-CAS stabilised-emulsion (PSE) in terms of viscoelasticity as affected by aging (30 days) and heating (80 °C, 30 min) at pH 5.8 and 7.0. DSE at pH 5.8 showed the highest complex modulus (G* = 1174 ± 39 Pa), approximately was six-times higher than other emulsions (G* ≤ ∼250 Pa) due to the thick emulsifier layer consisting of primary droplet increasing the effective volume faction of core droplets by a factor of ∼1.21. After aging, G* of DSE at pH 5.8 increased to 1685 ± 68 Pa, while G* of other three emulsions were ∼400 Pa. After heating, G* of DSE reached 1801 ± 69 Pa and 1312 ± 205 Pa at pH 5.8 and pH 7.0, respectively, while G* of PSE were ∼600 Pa at both pHs. The possible mechanism for aging-induced gelation was the gravity-driven microphase separation, in which the droplets flocculate together with the entrapped aqueous phase increasing the effective volume fraction. The heat-induced gelation was attributed to the increase in droplet interactions through protein aggregates and/or primary droplets forming three-dimensional networks at elevated temperature. This study suggests that the mechanical strength of food-grade concentrated emulsions can be effectively improved using nano-sized primary emulsions as emulsifying agent and can be further modulated by aging orItem Kinetics of pepsin-induced hydrolysis and the coagulation of milk proteins(Elsevier Inc and the Federation of Animal Science Societies on behalf of the American Dairy Science Association, 2022-02) Yang M; Ye A; Yang Z; Everett DW; Gilbert EP; Singh HHydrolysis-induced coagulation of casein micelles by pepsin occurs during the digestion of milk. In this study, the effect of pH (6.7–5.3) and pepsin concentration (0.110–2.75 U/mL) on the hydrolysis of κ-casein and the coagulation of the casein micelles in bovine skim milk was investigated at 37°C using reverse-phase HPLC, oscillatory rheology, and confocal laser scanning microscopy. The hydrolysis of κ-casein followed a combined kinetic model of first-order hydrolysis and putative pepsin denaturation. The hydrolysis rate increased with increasing pepsin concentration at a given pH, was pH dependent, and reached a maximum at pH ~6.0. Both the increase in pepsin concentration and decrease in pH resulted in a shorter coagulation time. The extent of κ-casein hydrolysis required for coagulation was independent of the pepsin concentration at a given pH and, because of the lower electrostatic repulsion between para-casein micelles at lower pH, decreased markedly from ~73% to ~33% when pH decreased from 6.3 to 5.3. In addition, the rheological properties and the microstructures of the coagulum were markedly affected by the pH and the pepsin concentration. The knowledge obtained from this study provides further understanding on the mechanism of milk coagulation, occurring at the initial stage of transiting into gastric conditions with high pH and low pepsin concentration.