In order to investigate the changes in fatty acid compounds and volatile compounds during the processing of sea buckthorn whole fruit powder, this study used sea buckthorn as the research object and employed targeted metabolomics combined with gas chromatography-ion mobility spectrometry (GC-IMS) technology, along with principal component analysis (PCA), correlation analysis (CorrA) and other chemometric methods to preliminarily investigate the dynamic changes and correlations of fatty acids and volatile components during the processing of sea buckthorn whole fruit powder. The results showed that 34 fatty acid compounds in sea buckthorn whole fruit powder were identified from sea buckthorn whole fruit powder by ultra-performance liquid chromatography-triple quadrupole mass spectrometry (UPLC-QQQ-MS), among which Linoleic acid (0.48~10.78 ng/mg) and palmitoleic acid (0.03~5.91 ng/mg) were the main fatty acid compounds. The total fatty acid content (2.48~114.84 ng/mg) in sea buckthorn whole fruit powder showed an overall decreasing trend during processing, with particularly significant decreases during the pulping and drying stages (P<0.05). These decreases represent reductions of 40.67% and 62.6%, respectively, compared to the raw material thawing stage. A total of 41 volatile compounds were identified by GC-IMS, showing an overall trend of first decreasing and then increasing. Based on VIP values>1, 12 key volatile compounds were screened, including hexanal, aromatic alcohols, and butyl 2-methylbutyrate. Combined with ROVA analysis, hexanal was identified as the primary characteristic volatile compound. Correlation analysis revealed that oxidized linalool was positively correlated with all fatty acid compounds. Further KEGG pathway analysis of the production pathways of major volatile compounds clarified that degraded lipids are primarily enriched in the fatty acid metabolism pathway, and fatty acid compounds derived from the unsaturated fatty acid biosynthesis pathway contribute to the formation of characteristic volatile flavor compounds such as hexanal, 2-pentanone, and 2-hexanone in sea buckthorn whole fruit powder. This study lays the foundation for improving the quality of sea buckthorn whole fruit powder.

This study involved the thermal-induced covalent conjugation of soy protein isolate (soy protein isolate, SPI, 2%, w/v) with different concentrations of rutin (0%, 0.5%, 1%, 1.5%, 2%, 2.5%, 3%, w/v) to prepare rutin-soy protein isolate (rutin-soy protein isolate, R-SPI) complex particles. These R-SPI particles were used as stabilizers to prepare high internal phase emulsions (high internal phase emulsions, HIPEs) with soy oil by one-pot homogenization. The effects of different rutin addition amounts on the particle size, zeta potential, rheological properties, interface protein adsorption rate, thermodynamic properties and microstructure of R-SPI composite HIPEs systems were investigated. The storage stability, thermal stability, acid-base stability, ionic stability, oxidation stability and digestive properties of the emulsion system were also studied. It was found that as the rutin concentration increased, the storage modulus (G') and loss modulus (G'') of HIPEs increased. When the rutin addition amount was 2.5%, the G' and G'' of HIPEs reached the maximum, and at this time, the particle size (1494.23±54.05 nm) and potential (−59.23±1.82 mV) of HIPEs reached the minimum values. At this time, the interface protein adsorption rate and free fatty acid release amount of HIPEs were the highest compared to other treatment groups (P<0.05). Further analysis of the stability of HIPEs revealed that after heating at 100 ℃ for 15 minutes, all treatment groups showed oil precipitation, while the HIPEs stabilized by R-SPI had stronger thermal stability, manifested by higher storage modulus (G'). Moreover, with the increase in rutin concentration, the acid-base stability, ionic stability and centrifugal stability of HIPEs increased. When the rutin concentration was 2.5%~3%, the alkaline stability, ionic stability and centrifugal stability of other treatment groups were better, and HIPEs with this concentration range showed stronger antioxidant capacity after accelerated oxidation. These findings will provide theoretical basis and experimental guidance for the development of new functional food-grade HIPEs.

To promote the development and utilization of β-conglycinin (7S) in the food industry, this study employed β-conglycinin and Auricularia auricula polysaccharide (AAP) as raw materials to prepare 7S-AAP non-covalent and covalent complexes via physical mixing and glycosylation reactions. The generation of 7S-AAP non-covalent/covalent complexes was verified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared spectroscopy (FT-IR). Furthermore, the physicochemical properties of the 7S-AAP non-covalent and covalent complexes were evaluated by assessing their solubility, surface hydrophobicity, emulsifying capacity, foaming capacity, and antioxidant activity. Results demonstrated that there was no significant difference in molecular composition between the 7S-AAP non-covalent complex and the native 7S protein. In contrast, the covalent complex formed a soluble macromolecular structure through the reaction of carbonyl and amino groups, confirming the occurrence of glycosylation and the successful synthesis of 7S-AAP non-covalent and covalent complexes. When the AAP concentration was 1%, the 7S-AAP covalent complex had the highest solubility (69.26%±2.98%), foaming capacity (149.00%±5.57%), foam stability (88.06%±2.59%), emulsifying activity (81.05±1.00 m²/g), emulsifying stability (64.53±0.50 min), DPPH radical scavenging rate (45.83%±1.99%), and ABTS⁺ radical scavenging rate (50.77%±1.44%). Compared with the 7S group, the surface hydrophobicity of the 7S-AAP covalent complex was significantly reduced (P<0.05). This study revealed that the physicochemical properties of 7S-AAP complexes improved with increasing AAP concentration, and the covalent complex outperformed the non-covalent complex in terms of functional properties. These findings provide theoretical support for the processing of 7S protein and the application of protein-polysaccharide systems in the food industry.

To systematically investigate the dynamic changes and underlying mechanisms of physicochemical properties and volatile compounds in potatoes during cooking, samples subjected to five cooking durations were comprehensively characterized using multidimensional techniques, including texture analyzers, rheometers, low-field nuclear magnetic resonance (LF-NMR), gas chromatography-ion mobility spectrometry (GC-IMS), and scanning electron microscopy (SEM), to assess texture properties, water migration, microstructure, and volatile profiles. It was revealed that cooking time had no significant effect on total moisture content (P>0.05). However, a decrease in the transverse relaxation time (T₂) at the core was observed, indicating partial conversion of bound water to free water. Chromaticity parameters (L^*, a^*, b^*) were significantly reduced (P<0.05), reflecting progressive darkening. Hardness, chewiness, and gumminess decreased significantly between 16.5 min and 20.5 min of boiling (P<0.05) and then remained stable with no significant changes between 20.5 min and 24.5 min (P>0.05). Rheological studies revealed that the viscosity versus frequency trends became increasingly similar for samples boiled between 18.5 min and 24.5 min, and the curves for 22.5 min and 24.5 min almost completely overlapped. Microstructural examination revealed that starch granules underwent swelling, rupture, and fragmentation, accompanied by progressive disintegration of the core matrix. Additionally, 67 volatile compounds were identified, among which aldehydes and pyrazines were enhanced by cooking. Prolonged cooking (>20.5 min) led to the formation of off-flavor compounds (e.g., 1-propanethiol, propanol, butyric acid, nonanoic acid). A critical threshold was identified at 20.5 min of boiling, with stabilized color parameters, water distribution, textural properties, and rheological characteristics, accompanied by elevated levels of characteristic flavor compounds and superior overall quality.

To address the issues of poor stability and degradation of antimicrobial peptides in food preservation and pharmaceutical applications, liposome encapsulation technology was employed to enhance the stability and bioavailability of antimicrobial peptide W1. The antimicrobial peptide W1 was extracted and purified from Bacillus subtilis SNBS-3 using ammonium sulfate precipitation, Sephadex-G25 gel chromatography, and high-performance liquid chromatography (HPLC). Its molecular sequence was identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS). Subsequently, W1-loaded liposomes were prepared using the film dispersion method, and optimal preparation conditions were determined through single-factor experiments and response surface methodology. The physicochemical properties of the liposomes were evaluated through particle size, Zeta potential, encapsulation efficiency, and microscopic structural analysis. The stability and antibacterial activity of the liposomes were tested under different temperature, pH, and enzyme treatment conditions. Additionally, cell experiments assessed the cytotoxicity of W1 liposomes on human liver cells (LO2). The results indicated that a highly active fraction was obtained by Sephadex-G25 purification, further purified by HPLC to obtain the core antibacterial peak, and the antimicrobial peptide W1 sequence was identified as IGLFGGAGVGK by LC-MS/MS. The optimal preparation conditions were determined to be a mass ratio of soybean phosphatidylethanolamine (SPE) to β-sitosterol of 5.94:1, a mass ratio of SPE to W1 of 5.18:1, and an ultrasonication time of 6.75 minutes. Under these conditions, W1-loaded liposomes were obtained with a particle size of 105.88±6.35 nm and an encapsulation efficiency of 68.2%±1.5%. Good physicochemical stability was exhibited by the resulting liposomes. Antibacterial tests revealed that the minimum inhibitory concentration (MIC) of W1 liposomes against Staphylococcus aureus was 32 mg/mL. Cytotoxicity assays demonstrated that W1 liposomes maintained LO2 cell viability above 90% at concentrations below 512 mg/mL (P>0.05), indicating favorable biocompatibility. These findings suggest that liposomal encapsulation significantly enhances the stability and antimicrobial efficacy of W1, providing a promising strategy for its application in the food and pharmaceutical industries.

To systematically investigate the structural features and anti-inflammatory activity of neutral polysaccharide (USP-N) from Orchis chusua D. Don, a medicinal and edible plant was selected. The structure of USP-N was comprehensively elucidated through partial acid hydrolysis, Smith degradation, methylation analysis, and 2D-NMR spectroscopy. Its anti-inflammatory effects were evaluated using a zebrafish inflammation model. Structural analysis revealed that the main chain of USP-N was composed of alternating β-1,4-linked glucose (38.5%) and mannose (33.8%), forming a glucomannan backbone. The side chains contained small amounts of rhamnose, arabinose, and galactose, with some mannose residues featuring 2-O-acetyl groups. Bioactivity assays demonstrated that USP-N treatment significantly suppressed LPS-induced nitric oxide (NO) release (P<0.0001) and inhibited neutrophil migration to the tail injury site in zebrafish (P<0.0001). Furthermore, dose-dependent reductions in neutrophil and macrophage recruitment to the caudal region following mechanical injury were observed. This study provides a theoretical foundation for applying Orchis chusua D. Don polysaccharides in functional foods and pharmaceutical development.

In order to improve the high-value utilization of sunflower seed protein, composite particles were prepared using sunflower seed protein (SSP) and xanthan gum (XG) as raw materials and used to stabilize Pickering emulsions. SSP-XG was characterized using Fourier transform infrared spectroscopy, contact angle measurement, and scanning electron microscopy to investigate the effect of the mass ratio of SSP to XG on the properties of SSP-XG particles. Particle size, Zeta potential, emulsifying activity index (EAI), and emulsion stability index (ESI) as indicators, this study analyzed the effects of different SSP-XG mass ratios and oil phase volume fractions on the microstructure, rheological properties and stability of Pickering emulsions. The results showed that hydrogen bonds, electrostatic interactions, and hydrophobic interactions existed between SSP and XG. The addition of XG made the SSP-XG surface smoother and increased the contact angle measurement value. The mass of SSP to XG ratio was 5:1, and the Pickering emulsion with an oil phase volume fraction of 70% exhibited the smallest particle size (6.65 μm), the highest Zeta potential (28.82 mV), and the highest EAI and ESI (1.26 m²/g, 154.81 min), the droplets were evenly distributed, forming a well developed gel network structure, and demonstrated excellent emulsification and stability. Additionally, it showed a lower emulsification index when stored at 4 ℃. They also had high pH, ionic stability and heat stability. The shear thinning behavior of rheology indicated that the emulsion was a non-Newtonian fluid. Laser confocal microscopy showed composite particles surrounding oil phase droplets, forming an oil-in-water (O/W) type emulsion. This study provides useful reference for the development of new green food-grade Pickering emulsions.

The potential of cold plasma (CP) treatment to promote the formation of amyloid fibrils of pea protein isolate (PPI) was evaluated relative to acidic heat fibrillation condition. The changes of ThT fluorescence intensity, microstructure, molecular structure, particle size distribution, Zeta potential, surface hydrophobicity, surface free sulfhydryl, free sulfhydryl, total sulfhydryl, and disulfide bonds content, emulsifying activity and foaming capacity of PPI amyloid fibrils were determined. Results indicated that the formation of PPI amyloid fibrils was significantly accelerated by CP treatment. Compared to acidic heat-induced PPI amyloid fibrils (A-PF), CP-mediated fibrils (CP-PF) showed higher ThT fluorescence intensity, relative content of β-fold, and shorter maturation time. After 60 min of heating, CP-PF formed longer fibrils (961.35 nm) than A-PF (219.84 nm). Hydrophobicity, free sulfhydryl groups, and disulfide bond analyses revealed that hydrophobic interactions and disulfide bonds were the primary driving forces for the self-assembly and ordered stacking of β-sheet structures during fibrillation process. Furthermore, fibrillization markedly improved the functional properties of PPI. The emulsifying activity and foaming capacity of A-PF and CP-PF were significantly enhancing. Notably, CP-PF exhibited superior emulsifying (improved by 9.1%) and foaming properties (improved by 6.8%) compared to A-PF. This study demonstrated that CP was an effective technique for promoting PPI amyloid fibril formation and improving its functionality.

To explore the effect of heating temperature on myosin functional properties, this study systematically analyzed the correlation between its functional properties (solubility, turbidity, emulsifying activity, and flavor binding capacity) and structural changes of tilapia myosin at different temperatures (40~90 ℃). Results demonstrated that with increasing temperature, myosin solubility significantly decreased (51.91% reduction at 90 ℃ vs 40 ℃) (P<0.05), while turbidity and emulsifying activity exhibited a V-shaped trend (initial decline followed by increase). Conversely, flavor-binding capacity displayed an inverted V-shaped pattern, with critical transition points concentrated at 50~60 ℃. Temperature-mediated functional changes were closely associated with structural transitions. In the low-temperature phase (40~50 ℃), partial denaturation induced structural unfolding, characterized by reduced α-helix (5.44% decrease) and β-sheet (42.08% decrease) contents, alongside a 102.64% increase in random coils. This exposed internal hydrophobic groups (0.30% increase in surface hydrophobicity) and active sulfhydryl groups (10.23% increase), enhancing hydrophobic interactions and providing additional flavor-binding sites. However, weakened electrostatic repulsion reduced emulsifying activity. In the medium-temperature stage (50~60 ℃), the unfolding of myosin structure intensified, leading to a 19.59% increase in surface hydrophobicity. The exposed active sites of myosin enhanced flavor-binding capacity, reduced the solubility and increased emulsifying activity and turbidity. In the high-temperature phase (60~90 ℃), irreversible denaturation promoted dense aggregate formation via hydrophobic interactions and disulfide bonds, evidenced by increased β-sheet (19.85%) and β-turn (4.72%) contents. Aggregation led to turbidity increase (6.21% increase at 90 ℃ vs. 40 ℃) (P<0.05), reduced surface hydrophobicity (26.95% reduction), and diminished active sulfhydryl content (76.27% reduction). Although the network formed between myosin molecules enhanced the emulsifying activity (29.68% increase at 80 ℃ vs 60 ℃), it masked flavor-binding sites, decreasing flavor retention. The research results provided theoretical references for the regulation of heat treatment parameters in fish meat product processing.

To investigate the inducing effect of dielectric barrier discharge cold plasma (DBD-CP) technology (treatment voltages: 30, 90, 150 kV, treatment times: 30, 60, 90 s) on the conformational changes of whey protein isolate (WPI)-chitosan (CS) composite particles and its regulatory effect on the loading performance of anthocyanins (ACNs), this study employed a two-factor full factorial experimental design. By systematically evaluating the encapsulation efficiency (EE), loading capacity (LC), ζ-potential, and particle size distribution of the composite particles for ACNs, the optimal DBD-CP treatment parameters were screened. Fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), scanning electron microscopy (SEM), fluorescence spectroscopy (FS), and circular dichroism (CD) were utilized as multi-scale characterization techniques to deeply analyze the DBD-CP-induced molecular conformational changes in WPI-CS. Based on the results of the above systematic evaluation, the optimal DBD-CP treatment parameters were screened and determined as voltage 90 kV and time 60 s. Under this optimal parameter set, the EE and LC of ACNs increased to 91.93% and 4.59%, respectively, significantly higher than those of the untreated group (P<0.05). The ζ-potential increased, enhancing electrostatic repulsion between particles and significantly improving system stability. Particle size analysis showed that distribution uniformity and particle dispersibility were improved. Structural characterization revealed that: Reactive species (e.g., electrons, ions) in DBD-CP promoted the exposure of hydrophobic groups in WPI and decreased the deacetylation degree of CS through oxidative modification, thereby enhancing the formation of hydrogen bonding and electrostatic cross-linking networks, simultaneously, the plasma etching effect optimized the pore uniformity of the complex, forming a dense encapsulation structure. DBD-CP treatment effectively modulated the structure of WPI-CS composite particles through synergistic effects (oxidative modification induced by reactive species and the etching effect), significantly improving their loading performance for ACNs and the system stability. This provides a theoretical basis for the application of cold plasma technology in stabilized delivery systems for bioactive components.