Effects and mechanism of natural phenolic acids/fatty acids on copigmentation of purple sweet potato anthocyanins.

Anthocyanins are attractive alternatives to colorants; however, their low color stability hinders practical application. Copigmentation can enhance both the color intensity and color stability of complexes. Herein, we report an investigation of copigmentation reactions between purple sweet potato anthocyanins (PSA1) and phenolic acids (tannic, ferulic, and caffeic acids) or fatty acids (tartaric and malic acids) at pH 3.5. The effects of the mole ratios of the copigment and the reaction temperature were examined. In addition, quantum mechanical computations were performed to investigate molecular interactions. The optimum PSA:copigment molar ratio was found to be 1:100. The strongest bathochromic and hyperchromic effects were observed for copigmentation with tannic acid (Tan), which might be attributable to the fact that its HOMO-LUMO energy gap was the smallest among the investigated copigments, and because it has a greater number of phenolic aromatic and groups to form more van der Waals and hydrogen bond interactions. However, the formation of the PSA-caffeic acid (Caf) complex was accompanied by the greatest drop in enthalpy (-33.18 kJ/mol) and entropy (-74.55 kJ/mol), and this was the most stable complex at 90 °C. Quantum mechanical calculations indicated that hydrogen bonds and van der Waals force interactions contributed to the color intensification effect of copigmentation. These findings represent an advancement in our understanding of the properties of PSA, expanding the application scope of this natural product.

Preparation and Characterization of Yellow Peach Peel/Sodium Alginate/Glycerol Antioxidant Film Applicable for Oil Package.

This work was dedicated to improving the utilization rate of yellow peach peel (YPP), with the addition of sodium alginate (SA) and glycerol (G) to prepare a biodegradable antioxidant film. First, the formulation of the film was optimized via response surface methodology (RSM) combined with the multi-index comprehensive evaluation method, considering physical properties including tensile strength (TS), elongation at break (E%), water solution (WS) and light transmittance (T). The RSM results displayed the best process condition was 2.50% of YPP, 0.60% SA and 0.80% of G (based on water) and compared with pure YPP film and YPP-SA film, the optimized (YPP-SA-G) film presented excellent properties with TS of 21.52 MPa, E of 24.8%, T of 21.56% on 600 nm, and WS of 41.61%, the comprehensive evaluation score of the film was 0.700. Furthermore, the films were characterized by Fourier transform infrared (FTIR) spectroscopy, scanning electron microscope (SEM), X-ray diffraction (XRD), and thermogravimetric analysis (TGA). FTIR analysis showed the main interaction of hydrogen between YPP, SA and G make the film has excellent compatibility, and the SEM images displayed that the film was dense and compacted with a little roughness. In addition, the optimized film had excellent thermal stability, suggested by TGA and XRD showed that the film's crystal structure has been changed significantly when the SA and G were mixed in. The TPC and the ability of DPPH radical scavenging of the YPP-SA-G film was 17.68 mg·g-1 of GAE and 18.65%, then potential packaging applications were evaluated using soybean oil and the YPP-SA-G antioxidant film significantly decreased peroxide value (POV) to delay oil oxidation during storage. Therefore, the YPP-SA-G film is expected to provide a new theoretical basis for the use of food processing by-products and the packaging industry.

Ameliorative effects of L-arginine? On heat-induced phase separation of Aristichthys nobilis myosin are associated with the absence of ordered secondary structures of myosin.

This investigation aimed to study the potential mechanism of L-arginine (L-Arg) on the heat-induced phase separation phenomenon of myosin from the perspective of conformational changes of myosin. L-Arg ameliorated the phase separation of myosin after a two-step heating procedure via suppression of heat-induced aggregation of myosin. The effect of L-Arg on the heating of myosin at high temperatures (75-85 °C) was more pronounced than that in the setting stage (35-45 °C), suggesting that the ameliorative effects of L-Arg on the heat-induced phase separation of myosin are mainly attributed to the inhibition of rod-rod cross-linking between denatured myosin molecules. Additionally, L-Arg without pH modification exhibited an increased ability to suppress the gelation of myosin compared with pH modification, indicating that both pH effects and the particular structure of L-Arg play noticeable roles in the suppression of myosin gelation. Far-UV circular dichroism, intrinsic fluorescence spectroscopy and differential scanning calorimetry demonstrated that L-Arg induced the absence of ordered secondary structures of myosin molecules, especially ß-sheets, and thus generated a looser protein structure, which may represent the dominant suppression mechanisms of L-Arg on the heat-induced aggregation of myosin. This work provided support for the use of L-Arg as a food additive, and the results of this study will be attractive to the meat and beverage products.