Journal Articles
Permanent URI for this collectionhttps://mro.massey.ac.nz/handle/10179/7915
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Item A Study of the Interaction, Morphology, and Structure in Trypsin-Epigallocatechin-3-Gallate Complexes(MDPI (Basel, Switzerland), 2021-07-28) Liu J; Ghanizadeh H; Li X; Han Z; Qiu Y; Zhang Y; Chen X; Wang A; Tresserra-Rimbau A; Bresciani LUnderstanding the interaction between proteins and polyphenols is of significance to food industries. The aim of this research was to investigate the mode of aggregation for trypsin-EGCG (Epigallocatechin-3-gallate) complexes. For this, the complex was characterized by fluorescence spectroscopy, circular dichroism (CD) spectra, small-angel X-ray scattering (SAXS), and atomic force microscope (AFM) techniques. The results showed that the fluorescence intensity of trypsin-EGCG complexes decreased with increasing the concentration of EGCG, indicating that the interaction between trypsin and EGCG resulted in changes in the microenvironment around fluorescent amino acid residues. The results of CD analysis showed conformational changes in trypsin after binding with EGCG. The results from SAXS analysis showed that the addition of EGCG results in the formation of aggregates of trypsin-EGCG complexes, and increasing the concentration of EGCG resulted in larger aggregates. AFM images showed that the trypsin-EGCG complex formed aggregates of irregular ellipsoidal shapes with the size of about 200 × 400 × 200 nm, with EGCG interconnecting the trypsin particles. Overall, according to these results, it was concluded that the large aggregates of trypsin-EGCG complexes are formed from several small aggregates that are interconnected. The results of this study shed some light on the interaction between digestive enzymes and EGCG.Item Delivery of Catechins from Green Tea Waste in Single- and Double-Layer Liposomes via Their Incorporation into a Functional Green Kiwifruit Juice(MDPI (Basel, Switzerland), 2023-01-06) Athirojthanakij W; Rashidinejad A; Tzen JTCGlobally, about one million tonnes of tea products, which contain high concentrations of catechins and their derivatives, are wasted annually. Therefore, green tea waste catechins (GTWCs) are worth extracting, processing, protection, and delivery to the human body. In this study, GTWCs were extracted using a green method and then encapsulated in both single- (SLLs) and double-layer liposomes (DLLs). The encapsulated extracts were subsequently incorporated into a fresh green kiwifruit juice. SLLs and DLLs containing GTWCs had a size of about 180 and 430 nm with a zeta potential of -35 and +25 mV, respectively. Electron microscopy illustrated the separation of the SLLs and fibre in kiwifruit juice and attraction of the DLLs to this fibre. Liposomal GTWCs were effectively maintained in the kiwifruit juice during the 28 days of storage (4 °C), demonstrating the effectiveness of this delivery system for high-value bioactives (i.e., catechins) from such a by-product (i.e., green tea waste).Item Assessment of Various Food Proteins as Structural Materials for Delivery of Hydrophobic Polyphenols Using a Novel Co-Precipitation Method(MDPI (Basel, Switzerland), 2023-04-19) Rashidinejad A; Nieuwkoop M; Singh H; Jameson GB; Papetti AIn this study, sodium caseinate (NaCas), soy protein isolate (SPI), and whey protein isolate (WPI) were used as structural materials for the delivery of rutin, naringenin, curcumin, hesperidin, and catechin. For each polyphenol, the protein solution was brought to alkaline pH, and then the polyphenol and trehalose (as a cryo-protectant) were added. The mixtures were later acidified, and the co-precipitated products were lyophilized. Regardless of the type of protein used, the co-precipitation method exhibited relatively high entrapment efficiency and loading capacity for all five polyphenols. Several structural changes were seen in the scanning electron micrographs of all polyphenol-protein co-precipitates. This included a significant decrease in the crystallinity of the polyphenols, which was confirmed by X-ray diffraction analysis, where amorphous structures of rutin, naringenin, curcumin, hesperidin, and catechin were revealed after the treatment. Both the dispersibility and solubility of the lyophilized powders in water were improved dramatically (in some cases, >10-fold) after the treatment, with further improvements observed in these properties for the powders containing trehalose. Depending on the chemical structure and hydrophobicity of the tested polyphenols, there were differences observed in the degree and extent of the effect of the protein on different properties of the polyphenols. Overall, the findings of this study demonstrated that NaCas, WPI, and SPI can be used for the development of an efficient delivery system for hydrophobic polyphenols, which in turn can be incorporated into various functional foods or used as supplements in the nutraceutical industry.