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    Development of composite electrospun films utilizing soy protein amyloid fibrils and pullulan for food packaging applications
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    Abstract:
    Electrospun films (ESF) are gaining attention for active delivery due to their biocompatibility and biodegradability. This study investigated the impact of adding soy protein amyloid fibrils (SAFs) to ESF. Functional ESF based on SAFs/pullulan were successfully fabricated, with SAFs clearly observed entangled in the electrospun fibers using fluorescence microscopy. The addition of SAFs improved the mechanical strength of the ESF threefold and increased its surface hydrophobicity from 24.8° to 49.9°. Moreover, the ESF demonstrated antibacterial properties against Escherichia coli and Staphylococcus aureus. In simulated oral disintegration tests, almost 100% of epigallocatechin gallate (EGCG) dissolved within 4 min from the ESF. In summary, the incorporation of SAFs into ESF improved their mechanical strength, hydrophobicity, and enabled them to exhibit antibacterial properties, making them promising candidates for active delivery applications in food systems. Additionally, the ESF showed efficient release of EGCG, indicating their potential for controlled release of bioactive compounds.
    Keywords:
    Pullulan
    Biocompatibility
    Gallate
    Following oral administration of (-)-epigallocatechin gallate to rats, the presence of (-)-epigallocatechin gallate was examined in the portal blood. A compound present in the blood was identified as (-)-epigallocatechin gallate by HPLC and mass spectrometry analysis. The results clearly demonstrate that (-)-epigallocatechin gallate is absorbed, at least in part, into rat portal blood.
    Gallate
    Citations (33)
    Three new compounds, in addition to previously reported compounds, were isolated from a product mixture obtained on incubating (-)-epigallocatechin gallate (EGCG) in neutral solution. The products were two monomeric (EGCG-MOx-M3 and EGCG-MOx-M4) and one dimeric (EGCG-MOx-D4) structure involving the flavan skeleton. Possible oxidation-reduction pathways producing drastic changes in the structure of EGCG were presented based on the structures of the breakdown products.
    Gallate
    Flavan
    Citations (5)
    Soy protein isolate (SPI) has promising applications in various food products because of its excellent functional properties and nutritional quality. The structural and emulsifying properties of covalently modified SPI by (-)-epigallocatechin-3-gallate (EGCG) were investigated.SPI was covalently modified by EGCG under alkaline conditions. SDS-PAGE analysis revealed that EGCG modification caused crosslinking of SPI proteins. Circular dichroism spectra demonstrated that the secondary structure of SPI proteins was changed by EGCG modification. In addition, the modifications resulted in the perturbation of the tertiary structure of SPI as evidenced by intrinsic fluorescence spectra and surface hydrophobicity measurements. Oil-in-water emulsions of modified SPI had smaller droplet sizes and better creaming stability compared to those from unmodified SPI.The covalent modification by EGCG improved the emulsifying property of SPI. This study therefore provided an innovative approach for improving the emulsifying properties of proteins. © 2018 Society of Chemical Industry.
    Gallate
    Creaming
    Chemical modification
    Citations (52)
    A semi-synthetic route to the D-ring analogs of (–)-epigallocatechin gallate (EGCG) from the relatively abundant (–)-epigallocatechin (EGC), isolated from green tea leaves, is described. A natural product (13), found in Cistus salvifolius, its acetate (14) and analog (17) were synthesized by this method. Their inhibitory activities against proteasomes were investigated.Key words: green tea, (–)-epigallocatechin gallate (EGCG), (–)-epigallocatechin (EGC), proteasome inhibition.
    Gallate
    Natural product
    Green tea extract
    Ingredient
    Citations (12)
    Abstract BACKGROUND Traditional soy protein isolate (SPI)‐based gel products, such as tofu, are generally produced by heating and by addition of metal salt ions to adjust the hydrophobicity and electrostatic force of soybean protein to facilitate the formation of a uniform network structure. However, the gelation rate of the soy protein gel network structure is difficult to control. Theoretically, epigallocatechin‐3‐gallate (EGCG) could be used to alter the surface hydrophobicity of thermally induced SPI to improve its gelation rate and form a more uniform network structure, thus improving SPI‐based gel properties (hardness, water holding capacity and rheological properties). RESULTS An SPI‐EGCG complex (SPIE) was prepared, and properties of the resulting gel, following induction of transglutaminase (TG), were evaluated. Results showed that EGCG is bound to thermally induced SPI primarily via hydrophobic and hydrogen bonding, thus altering the secondary structure composition and reducing surface hydrophobicity of proteins in thermally induced SPI. Furthermore, the optimum amount of EGCG required to improve the gel strength, water holding capacity and rheological properties was ≤0.04:1 (SPI 1 g L −1 ; EGCG:SPI, w/w). Thermal stability analysis further indicated that EGCG in SPIE was more stable than free EGCG after heating. CONCLUSION This study demonstrated that EGCG can improve the gel properties of TG‐crosslinked SPIE, while EGCG in SPIE exhibits enhanced thermal stability. Additionally, the results of this study provide a novel strategy for the development of SPI‐based gel foods with improved gel properties and that are enriched with bioactive compounds. © 2020 Society of Chemical Industry
    Gallate
    Thermal Stability
    Tissue transglutaminase
    Hydrophobic effect
    Network Structure
    Citations (22)