In this study, the effects of pH and NaCl concentrations on the structure of golden pompano myosin and emulsion gel were analyzed using SEM in combination with molecular dynamics simulations (MDS). The microscopic morphology and spatial structure of myosin were investigated at different pH (3.0, 7.0, and 11.0) and NaCl concentrations (0.0, 0.2, 0.6, and 1.0 M), and their effects on the stability of emulsion gels were discussed. Our results show that pH had a greater effect on the microscopic morphology of myosin than NaCl. The MDS results show that under the condition of pH 7.0 and 0.6 M NaCl, the myosin expanded and experienced significant fluctuations in its amino acid residues. However, NaCl showed a greater effect on the number of hydrogen bonds than pH. Although changes in pH and NaCl concentrations only slightly altered the secondary structures in myosin, they, nevertheless, significantly influenced the protein spatial conformation. The stability of the emulsion gel was affected by pH changes but not NaCl concentrations, which only affect the rheology. The best elastic modulus G″ of the emulsion gel was obtained at pH 7.0 and 0.6 M NaCl. Based on the results, we conclude that pH changes have a greater influence than NaCl concentrations on the spatial structure and conformation of myosin, contributing to the instability of its emulsion gel state. The data from this study would serve as a valuable reference for emulsion gel rheology modification in future research.

In this study, the physicochemical properties, functional properties and N-glycoproteome of tilapia myofibrillar protein (TMP), golden pompano myofibrillar protein (GPMP) and skipjack tuna myofibrillar protein (STMP) were assessed. The microstructures and protein compositions of the three MPs were similar. TMP and GPMP had higher solubility, sulfhydryl content and endogenous fluorescence intensity, lower surface hydrophobicity and β-sheet contents than STMP. The results showed that the protein structures of TMP and GPMP were more folded and stable. Due to its low solubility and high surface hydrophobicity, STMP had low emulsifying activity and high foaming activity. By N-glycoproteomics analysis, 23, 85 and 22 glycoproteins that contained 28, 129 and 35 N-glycosylation sites, were identified in TMP, GPMP and STMP, respectively. GPMP had more N-glycoproteins and N-glycosylation sites than STMP, which was possibly the reason for GPMP’s higher solubility and EAI. These results provide useful information for the effective utilization of various fish products.

Free, conjugated, and bound phenolic fractions of peel and pulp in four wampee varieties from South China were analyzed for their contents, composition, antioxidant capacities, and inhibitory activities against α-glucosidase. We found that there were significant differences in phenolic/flavonoid contents among diverse varieties and different parts (peel and pulp), and the contents were highest in the peel’s bound form. The results of UHPL-Q-Exactive HF-X and HPLC showed that chlorogenic acid, gentisic acid, and rutin were abundantly distributed over the three phenolic fractions in peel and pulp of all wampee samples, while isoquercitrin was the most abundant in the conjugated form of peel/pulp and myricetin had the richest content in the free form of peel/pulp. Wampee peel had stronger antioxidant capacities of ABTS+, DPPH, ·OH, and FRAP than the pulp, and the bound phenolic fraction of the peel/pulp had much higher antioxidant activities than FP and CP fractions. It is interesting that the same phenolic fraction of the wampee peel displayed roughly close IC₅₀ values of α-glucosidase inhibition to those from the pulp samples. The relationship between individual phenolic and TPC/TFC/the bio-activities and the similarity among the free, conjugated, and bound phenolic fractions in peel and pulp samples were explored by using Pearson correlation analysis, principal component analysis, and hierarchical cluster analysis. This work provides a systematic and comprehensive comparison of the three phenolic fractions of diverse wampee varieties and different parts, and a rationale for applying phenolics from wampee fruits.

This study employed a multi-technique approach to investigate the structural and conformational changes in proteins in Meretrix lyrata (M. lyrata) adductor, foot, and siphon tissues during boiling. Data-independent acquisition (DIA) quantitative proteomics was utilized to identify differentially expressed proteins (DEPs) in six temporal comparison groups (20–0 s, 40–20 s, 60–40 s, 80–60 s, 100–80 s, and 120–100 s). The results showed that key myofibrillar proteins, including myosin heavy chain, paramyosin, and actin, exhibited tissue-specific expression patterns, while low-molecular-weight degradation fragments (<17 kDa) appeared with prolonged heating. Turbidity measurements peaked in adductor and siphon tissues at 60 s and in foot tissue at 80 s. Heating resulted in a narrowed particle size distribution (100–1000 nm), and a decreased zeta potential, indicating a reduction in protein surface charge. Fourier transform infrared spectroscopy revealed hydrogen bond disruption and secondary structure transitions, marked by a reduction in α-helix content with a corresponding increase in β-sheet and random coil structures. In total, 6527 proteins were identified, and Gene Ontology (GO) enrichment analysis highlighted the DEPs’ involvement in biological regulation and metabolic processes. Collectively, these results provide comprehensive characterization of protein denaturation, degradation, and structural reorganization in M. lyrata tissues during the boiling process.