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This investigation aimed to assess the effects of whey protein hydrolysate (WPH) on the oxidative stability of protein and the ability of Scomberomorus niphoniu surimi balls to retain water after repeated freeze–thaw (F–T) cycles. Ten percent natural whey peptides (NWP), 5% WPH, 10% WPH, 15% WPH, 0.02% butyl hydroxyl anisole (BHA), and a control group that did not receive any treatment were the six groups that were employed in the experiment. The cooking loss, water retention, total sulfhydryl content, and carbonyl content of each group were all measured. Notably, it was found that the surimi balls’ capacity to hold onto water and fend off oxidation was enhanced in a dose-dependent manner by the addition of WPH. Furthermore, the results showed that the 15% WPH added to the surimi balls effectively decreased protein oxidation in the F–T cycles and ameliorated the texture deterioration of surimi balls induced by repeated F–T, laying a theoretical foundation for the industrial application of WPH in surimi products.

Repeated freeze–thaw (FT) cycles can have an impact on surimi quality. In this study, we used 0.02% BHA as a positive control group. We examined the effects of different concentrations (0%, 5%, 10%, and 15%) of whey protein hydrolysate (WPH) on surimi, focusing on alterations in color metrics (L* for brightness, a* for red–green, b* for yellow–blue, and overall whiteness), textural characteristics, and antioxidant capacity during various freeze–thaw (FT) cycles. The results showed that the lipid oxidant values of surimi, as well as its a* and b* values, rose as the number of FT cycles increased; whereas the adhesiveness, resilience, gumminess, and shear force dropped, as did L* and the whiteness values, leading to an overall darkening of color and gloss. By contrast, the study found that the addition of WPH could effectively slow down the decrease of surimi textural stability after repeated freeze–thawing, with the textural stability of the group with 15% WPH being significantly superior to those of the other groups (p < 0.05). Under the same number of cycles, adding 15% WPH to the experimental group could successfully lower total volatile basic nitrogen (TVB-N) and effectively increase the antioxidant activity of surimi. This finding suggested that 15% WPH had the greatest effect on increasing surimi FT stability. To conclude, it was proved that WPH can be added to frozen surimi and improve its quality.

Whey protein hydrolysate (WPH) has made a breakthrough in inhibiting oxidative deterioration and improving the quality of meat products during storage. Based on our previous study of extracting the most antioxidant active fraction I (FI, the molecular weight < 1 kDa) from whey protein hydrolysates of different molecular weights, the present study continued to delve into the effects of WPH with fraction I on the structure and function of myofibrillar proteins (MP) in ground pork during the freeze–thaw (F-T) cycles. With the number of F-T cycles raised, the total sulfhydryl content, the relative contents of α-helix, Ca2+-ATPase activity, K+-ATPase activity, solubility, emulsion activity index (EAI), and emulsion stability index (ESI) of MP gradually decreased. Conversely, the carbonyl content and the relative content of random curl showed an increasing trend. In particular, the damage to the structure and the function of MP became more pronounced after three F-T cycles. But, during F-T cycles, FI stabilized the structure of MP. Compared to the control group, the 10% FI group showed a remarkable improvement (p < 0.05) in the total sulfhydryl content, Ca2+-ATPase activity, K+-ATPase activity, solubility, EAI and ESI after multiple F-T cycles, suggesting that 10% FI could effectively inhibit protein oxidation and had the influence of preserving MP function properties. In conclusion, WPH with fraction I can be used as a potential natural antioxidant peptide for maintaining the quality of frozen processed meat products.

The effects of whey protein hydrolysates (WPH) on myofibrillar protein (MP) oxidative stability and the aggregation behavior and the water-holding capacity of pork patties during freeze–thaw (F–T) cycles were investigated. During F–T cycles, the total sulfhydryl content and zeta potential of MP decreased, while peroxide value, surface hydrophobicity, particle size, pressure loss and transverse relaxation times increase. The oxidative stability and the water-holding capacity of pork patties were enhanced by the addition of WPH in a dose-dependent manner, whereas the MP aggregation decreased. The addition of 15% WPH had the most obvious effects on the pork patties, which was similar to that of the 0.02% BHA. After nine F–T cycles, the POV, surface hydrophobicity, particle size and pressure loss of the pork patties with 15% WPH were reduced by 17.20%, 30.56%, 34.67% and 13.96%, respectively, while total sulfhydryl content and absolute value of zeta potential increased by 69.62% and 146.14%, respectively. The results showed that adding 15% WPH to pork patties can be an effective method to inhibit lipid and protein oxidation, reducing protein aggregation and improving the water-holding capacity of pork patties during F–T cycles.

Pb3Nb4O13 semiconductor films were prepared on fluorine-doped tin oxide (FTO) substrates by an electrophoretic deposition method. Their phase and morphology were revealed by X-ray diffraction (XRD) and scanning electron microscopy (SEM) respectively. Their photoelectrochemical (PEC) properties were carefully studied on the obtained multiple metal oxide Pb3Nb4O13 electrodes. The energy band structure of Pb3Nb4O13 was analyzed from the Mott-Schottky experimental plot. The results indicate that the energy band structure satisfies the requirements for photoelectrochemical water splitting. The designed material produced a photocurrent density of ~46.5 µA/cm² under the illumination of a full arc Xe light. Electrochemical impedance spectroscopy was performed to investigate the kinetics of the electrolyte-electrode interface. The monochromatic incident photon-to-electron current conversion efficiency (IPCE) was measured. Interfacing with the water-oxidation electrocatalyst Co-Pi enhanced the IPCE. [ABSTRACT FROM AUTHOR]