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Ultrasound-assisted phosphorylation of goose myofibrillar proteins: improving protein structure and functional properties

Zhou Y, Sun Y, Pan D, Xia Q, Zhou C

J Sci Food Agric, 2023 Aug 30;103(11):5412-5421.
PMID: 37038882 DOI: 10.1002/jsfa.12616

BACKGROUND: Goose meat is rough and embedded with dense connective tissue, impairing protein solubility. Therefore, to improve the functional properties of goose myofibrillar protein (GMP), ultrasound was used to assist the phosphorylation of GMP.
RESULTS: The fact that GMP attached covalently with the phosphate group of sodium tripolyphosphate (GMP-STP) was disclosed directly by Fourier transform infrared spectroscopy. Furthermore, ultrasound significantly improved the hydrophobicity and solubility of GMP-STP, which could be attributed to the conversion of α-helix to β-sheet, β-turns, and random coils by sonication. The spatial stabilization of the protein phosphorylation process was boosted by ultrasound, making the droplets more dispersed, and thus an improvement in the functional properties of GMP-STP was observed. Water-holding capacity, oil-binding capacity, and emulsifying and foaming properties were best at an ultrasound power of 400 W.
CONCLUSION: Ultrasound-assisted phosphorylation has great potential to modulate the structure-function relationship of proteins. © 2023 Society of Chemical Industry.
TMT-labeled quantitative proteomic reveals the mechanism of proteolysis and taste improvement of dry-cured bacon with Staphylococcus co-inoculation

Zhou C, Wu X, Pan D, Xia Q, Sun Y, Geng F, et al.

Food Chem, 2024 Mar 15;436:137711.
PMID: 37839122 DOI: 10.1016/j.foodchem.2023.137711

To understand the mechanism of co-inoculation of Staphylococcus xylosus and Staphylococcus vitulinus (SX & SV) on structural protein degradation and taste enhancement of dry-cured bacon, protease activities, protein degradation, surface morphology of proteins and taste parameters of dry-cured bacon with Staphylococcus inoculation were investigated. The dry-cured bacon with co-inoculation of Staphylococcus xylosus and Staphylococcus vitulinus showed the best taste attributes. High residual activities in cathepsin B + L (more than 1.6-fold) and alanyl aminopeptidase (more than 1.4-fold) accelerated structural protein degradation in SX & SV. 32 down-regulated proteins were identified in SX & SV by TMT-labeled quantitative proteomic compared with control group; myosin and actin showed the most intense response to the accumulation of sweet and umami amino acids, and atomic force microscopy confirmed structural proteins breakdown by morphological changes. The accumulation of glutamic acid, alanine and lysine was mainly responsible for taste improvement of dry-cured bacon with Staphylococcus co-inoculation.
Fulltext Investigation into the characteristic volatile flavor of old duck

Duan M, Xu L, Gu T, Sun Y, Xia Q, He J, et al.

Food Chem X, 2023 Dec 30;20:100899.
PMID: 38144818 DOI: 10.1016/j.fochx.2023.100899

In order to explore the characteristic aroma flavor and its formation mechanism of old ducks, two ages (30 days and 60 days) of young ducks and three ages of old ducks (300 days, 900 days, and 1500 days) were selected and studied. An electronic nose was applied to evaluate the overall aroma flavor, and the result showed significant differences between the five duck samples. By gas chromatography-mass spectrometry (GC-MS), forty-eight volatile flavor compounds were detected, including seven aldehydes, six esters, five alcohols, five nitrogen compounds, twenty-one hydrocarbons, and four others. Among these compounds, twelve components, such as hexanal and dimethyl anthranilate, were considered as the characteristic flavor compounds along with duck aging. Furthermore, correlation analysis indicated that meat's unsaturated free fatty acids, especially linoleic acid (C18:2), were responsible for the duck's characteristic flavor formation. These data contribute to the flavor research and identification of old ducks.
Fulltext Efficacy of Forsythia suspensa (Thunb.) Vahl on mouse and rat models of inflammation-related diseases: a meta-analysis

Zhou C, Xia Q, Hamezah HS, Fan Z, Tong X, Han R

Front Pharmacol, 2024;15:1288584.
PMID: 38500762 DOI: 10.3389/fphar.2024.1288584

Objective: To evaluate the efficacy of the fruits of the medicinal plant Forsythia suspensa (Thunb.) Vahl (FS), in treating inflammation-associated diseases through a meta-analysis of animal models, and also probe deeply into the signaling pathways underlying the progression of inflammation. Materials and methods: All data analyses were performed using Review Manager 5.3 and the results are presented as flow diagrams, risk-of-bias summaries, forest plots, and funnel plots. Summary estimates were calculated using a random- or fixed-effect model, depending on the value of I2. Results: Of the 710 records identified in the initial search, 11 were selected for the final meta-analysis. Each study extracted data from the model and treatment groups for analysis, and the results showed that FS alleviated the inflammatory cytokine levels in serum; oxidant indicator: reactive oxygen species; enzymes of liver function; endotoxin and regulatory cells in blood; and improved the antioxidant enzyme superoxide dismutase. Conclusion: FS effectively reversed the change in acute or chronic inflammation indicators in animal models, and the regulation of multiple channel proteins in inflammatory signaling pathways suggests that FS is a good potential drug for inflammatory disease drug therapy.
Fulltext Combining thermosonication microstress and pineapple peel extract addition to achieve quality and post-acidification control in yogurt fermentation

Zhang X, Zheng Y, Zhou C, Cao J, Zhang Y, Wu Z, et al.

Ultrason Sonochem, 2024 May;105:106857.
PMID: 38552299 DOI: 10.1016/j.ultsonch.2024.106857

This work investigated the effects of the combined use of thermosonication-preconditioned lactic acid bacteria (LAB) with the addition of ultrasound-assisted pineapple peel extracts (UU group) on the post-acidification potential, physicochemical and functional qualities of yogurt products, aimed at achieving prolonged preservation and enhancing functional attributes. Accordingly, the physical-chemical features, adhesion properties, and sensory profiles, acidification kinetics, the contents of major organic acids, and antioxidant activities of the differentially processed yogurts during refrigeration were characterized. Following a 14-day chilled storage process, UU group exhibited acidity levels of 0.5-2 oT lower than the control group and a higher lactose content of 0.07 mg/ml as well as unmodified adhesion potential, indicating that the proposed combination method efficiently inhibited post-acidification and delayed lactose metabolism without leading to significant impairment of the probiotic properties. The results of physicochemical analysis showed no significant changes in viscosity, hardness, and color of yogurt. Furthermore, the total phenolic content of UU-treated samples was 98 μg/mL, 1.78 times higher than that of the control, corresponding with the significantly lower IC50 values of DPPH and ABTS radical scavenging activities of the UU group than those of the control group. Observations by fluorescence inverted microscopy demonstrated the obvious adhesion phenomenon with no significant difference found among differentially prepared yogurts. The results of targeted metabolomics indicated the proposed combination strategy significantly modified the microbial metabolism, leading to the delayed utilization of lactose and the inhibited conversion into glucose during post-fermentation, as well as the decreased lactic acid production and a notable shift towards the formation of relatively weak acids such as succinic acid and citric acid. This study confirmed the feasibility of thermosonication-preconditioned LAB inocula, in combination with the use of natural active components from fruit processing byproducts, to alleviate post-acidification in yogurt and to enhance its antioxidant activities as well as simultaneously maintaining sensory features.
Research advance of non-thermal processing technologies on ovalbumin properties: The gelation, foaming, emulsification, allergenicity, immunoregulation and its delivery system application

Chen Q, Dong L, Li Y, Liu Y, Xia Q, Sang S, et al.

Crit Rev Food Sci Nutr, 2024;64(20):7045-7066.
PMID: 36803106 DOI: 10.1080/10408398.2023.2179969

Ovalbumin (OVA) is the most abundant protein in egg white, with excellent functional properties (e.g., gelling, foaming, emulsifying properties). Nevertheless, OVA has strong allergenicity, which is usually mediated by specific IgE thus results in gut microbiota dysbiosis and causes atopic dermatitis, asthma, and other inflammation actions. Processing technologies and the interactions with other active ingredients can influence the functional properties and allergic epitopes of OVA. This review focuses on the non-thermal processing technologies effects on the functional properties and allergenicity of OVA. Moreover, the research advance about immunomodulatory mechanisms of OVA-mediated food allergy and the role of gut microbiota in OVA allergy was summarized. Finally, the interactions between OVA and active ingredients (such as polyphenols and polysaccharides) and OVA-based delivery systems construction are summarized. Compared with traditional thermal processing technologies, novel non-thermal processing techniques have less damage to OVA nutritional value, which also improve OVA properties. OVA can interact with various active ingredients by covalent and non-covalent interactions during processing, which can alter the structure or allergic epitopes to affect OVA/active components properties. The interactions can promote OVA-based delivery systems construction, such as emulsions, hydrogels, microencapsulation, nanoparticles to encapsulate bioactive components and monitor freshness for improving foods quality and safety.
Unlocking the molecular modifications of plasma-activated water-induced oxidation through redox proteomics: In the case of duck myofibrillar protein (Anas platyrhynchos)

Rao W, Ju S, Sun Y, Xia Q, Zhou C, He J, et al.

Food Chem, 2024 Nov 15;458:140173.
PMID: 38943955 DOI: 10.1016/j.foodchem.2024.140173

Plasma-activated water (PAW) contains multiple active species that alter the structure of myofibrillar protein (MP) to enhance their gel properties. This work investigated the impact of PAW on the oxidation of cysteine in MP by label-free quantitative proteomics. PAW treatment caused the oxidation of 8241 cysteine sites on 2815 proteins, and structural proteins such as nebulin, myosin XVIIIB, myosin XVIIIA, and myosin heavy chain were susceptible to oxidation by PAW. Bioinformatics analysis, including Gene Ontology (GO), Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway, subcellular localization, and STRING analysis, indicated that these proteins with differential oxidation sites were mainly derived from the cytoplasm and membrane, and were involved in multiple GO terms and KEGG pathways. This is one of the first reports of the redox proteomic changes induced by PAW treatment, and the results are useful for understanding the possible mechanism of PAW-induced oxidation of MP.
Structural and gel property changes in chicken myofibrillar protein induced by argon cold plasma-activated water: With a molecular docking perspective

Li J, Rao W, Sun Y, Zhou C, Xia Q, He J, et al.

Food Res Int, 2024 Dec;197(Pt 1):115271.
PMID: 39593348 DOI: 10.1016/j.foodres.2024.115271

This study investigated the effects of plasma-activated water (PAW) generated with argon at discharge times of 0, 4, 8, 12, and 16 min on the gel properties and structures of chicken myofibrillar protein (MP). Under treatments of 8, 12, and 16 min, both the gel strength and water retention capacity of MP significantly improved, with the gel strength (0.53 N) peaking at 16 min and the lowest cooking loss（30.38 %）. As the treatment time increased from 0 to 16 min, the storage modulus also gradually increased. Results from low-field nuclear magnetic resonance indicated a slowing of water proton mobility, with the proportion of bound water rising from 0.26 % (0 min) to 0.52 % at 16 min. Fourier transform infrared spectroscopy, endogenous fluorescence spectroscopy and scanning electron microscopy confirmed PAW's alteration of MP's secondary and tertiary structures and gel microstructure. Additionally, this study explored the influence of argon PAW's primary active species on MP from a molecular docking perspective·H2O2 could form hydrogen bonds with MP, while O3 and NO2‾could interact via both hydrogen bonds and electrostatic interactions. Thus, PAW can alter protein structure and enhance MP's functional properties, providing insights for applying cold plasma in processing chicken gel products.
Contribution of process-induced molten-globule state formation in duck liver protein to the enhanced binding ability of (E,E)-2,4-heptadienal

Han C, Zheng Y, Wang L, Zhou C, Wang J, He J, et al.

J Sci Food Agric, 2023 May;103(7):3334-3345.
PMID: 36786016 DOI: 10.1002/jsfa.12499

BACKGROUND: Extracted proteins of alternative animal origin tend to present strong off-flavor perception due to physicochemical interactions of coextracted off-flavor compounds with proteins. To investigate the relationship between absorption behaviors of volatile aromas and the processes-induced variations in protein microstructures and molecular conformations, duck liver protein isolate (DLp) was subjected to heating (65/100 °C, 15 min) and ultra-high pressure (UHP, 100-500 MPa/10 min, 28 °C) treatments to obtain differential unfolded protein states.
RESULTS: Heat and UHP treatments induced the unfolding of DLp to varied degrees, as revealed by fluorescence spectroscopy, ultraviolet-visible absorption, circular dichroism spectra and surface hydrophobicity measurements. Two types of heating-denatured states with varied unfolding degrees were obtained, while UHP at both levels of 100/500 MPa caused partial unfolding of DLp and the presence of a molten-globule state, which significantly enhanced the binding affinity between DLp and (E,E)-2,4-heptadienal. In particular, significantly modified secondary structures of DLp were observed in heating-denatured samples. Excessive denaturing and unfolding degrees resulted in no significant changes in the absorption behavior of the volatile ligand, as characterized by observations of fluorescence quenching and analysis of headspace concentrations.
CONCLUSION: Defining process-induced conformational transition behavior of matrix proteins could be a promising strategy to regulate food flavor attributes and, particularly, to produce DLp coextracted with limited off-flavor components by modifying their interaction during extraction processes. © 2023 Society of Chemical Industry.
Tunability of Pickering particle features of whey protein isolate via remodeling partial unfolding during ultrasonication-assisted complexation with chitosan/chitooligosaccharide

Yu H, Zheng Y, Zhou C, Liu L, Wang L, Cao J, et al.

Carbohydr Polym, 2024 Feb 01;325:121583.
PMID: 38008470 DOI: 10.1016/j.carbpol.2023.121583

The potential of ultrasonication-driven molecular self-assembly of whey protein isolate (WPI) with chitosan (CS)/chitooligosaccharide (COS) to stabilize Pickering emulsions was examined, based on CS/COS ligands-induced partial unfolding in remodeling the Pickering particles features. Multi-spectral analysis suggested obvious changes in conformational structures of WPI due to interaction with CS/COS, with significantly higher unfolding degrees of WPI induced by COS. Non-covalent interactions were identified as the major forces for WPI-CS/COS conjugates. Ultrasonication enhanced electrostatic interaction between CS's -NH3 groups and WPI's -COO- groups which improved emulsification activity and storability of WPI-COS stabilized Pickering emulsion. This was attributed to increased surface hydrophobicity and decreased particle size compared to WPI-CS associated with differential unfolding degrees induced by different saccharide ligands. CLSM and SEM consistently observed smaller emulsion droplets in WPI-COS complexes than WPI-CS/COS particles tightly adsorbed at the oil-water interface. The electrostatic self-assembly of WPI with CS/COS greatly enhanced the encapsulation efficiency of quercetin than those stabilized by WPI alone and ultrasound further improved encapsulation efficiency. This corresponded well with the quantitative affinity parameters between quercetin and WPI-CS/COS complexes. This investigation revealed the great potential of glycan ligands-induced conformational transitions of extrinsic physical disruption in tuning Pickering particle features.
Exploring the binding mechanisms of thermally and ultrasonically induced molten globule-like β-lactoglobulin with heptanal as revealed by multi-spectroscopic techniques and molecular simulation

Han C, Zheng Y, Huang S, Xu L, Zhou C, Sun Y, et al.

Int J Biol Macromol, 2024 Apr;263(Pt 1):130300.
PMID: 38395276 DOI: 10.1016/j.ijbiomac.2024.130300

This work employed the model protein β-lactoglobulin (BLG) to investigate the contribution of microstructural changes to regulating the interaction patterns between protein and flavor compounds through employing computer simulation and multi-spectroscopic techniques. The formation of molten globule (MG) state-like protein during the conformational evolution of BLG, in response to ultrasonic (UC) and heat (HT) treatments, was revealed through multi-spectroscopic characterization. Differential MG structures were distinguished by variations in surface hydrophobicity and the microenvironment of tryptophan residues. Fluorescence quenching measurements indicated that the formation of MG enhanced the binding affinity of heptanal to protein. LC-MS/MS and NMR revealed the covalent bonding between heptanal and BLG formed by Michael addition and Schiff-base reactions, and MG-like BLG exhibited fewer chemical shift residues. Molecular docking and molecular dynamics simulation confirmed the synergistic involvement of hydrophobic interactions and hydrogen bonds in shaping BLG-heptanal complexes thus promoting the stability of BLG structures. These findings indicated that the production of BLG-heptanal complexes was driven synergistically by non-covalent and covalent bonds, and their interaction processes were influenced by processes-induced formation of MG potentially tuning the release and retention behaviors of flavor compounds.
Insights into the fabrication and antibacterial effect of fibrinogen hydrolysate-carrageenan loading apigenin and quercetin composite hydrogels

Wang Q, An J, Xia Q, Pan D, Du L, He J, et al.

Int J Biol Macromol, 2024 Sep 09.
PMID: 39260642 DOI: 10.1016/j.ijbiomac.2024.135517

Escherichia coli and Staphylococcus aureus are the most prevalent pathogenic bacteria, often resulting in the foodborne disease outbreaks through food spoilage and foodborne infections. To prevent and control food spoilage and foodborne infections induced by Escherichia coli and Staphylococcus aureus, the antibacterial hydrogels were fabricated using fibrinogen hydrolysate-carrageenan (AHs-C) and flavonoids (apigenin and quercetin), and the antibacterial effect of the composite hydrogels against Escherichia coli and Staphylococcus aureus was further investigated. The results of mechanical property exhibited that the composite hydrogels with 0.2 % of apigenin and quercetin (AHs-C-Ap/Que) showed the highest hardness and swelling property compared with the separate addition of apigenin or quercetin. Scanning electron microscopy and atomic force microscopy showed that the dense networks were formed in the hydrogels of AHs-C-Ap/Que., and the average roughness of AHs-C-Ap/Que. significantly increased to 30.70 nm compared with AHs-C. 1H NMR and FTIR spectra demonstrated that apigenin and quercetin were bound to AHs-C by hydrogen bond, hydrophobic interaction and Schiff base, where the interactions between Ap/Que. and AHs-C was stronger compared with the separate addition of apigenin or quercetin. The hydrogels of AHs-C-Ap/Que. showed the highest antibacterial capacity and antibacterial adhesion against Escherichia coli and Staphylococcus aureus. The antibacterial adhesion assay showed that 99 % removal ratios for E. coli and S. aureus were observed in AHs-C-Ap/Que. hydrogels, which showed a great potential to prevent food spoilage and foodborne infections.
Effect of pre-acidification induction on the physicochemical features, myofibrillar protein microstructure, and headspace volatiles of ready-to-cook goose meat

Cheng Y, Zheng Y, Cai X, Wang L, Zhou C, Cao J, et al.

Food Res Int, 2024 Dec;197(Pt 1):115166.
PMID: 39593377 DOI: 10.1016/j.foodres.2024.115166

This study examined the impact of pre-acidification induction on the quality attributes and flavor retention of ready-to-cook (RTC) goose meat products. The results demonstrated that pre-acidification could influence the eating qualities of RTC goose meat by effectively regulating the physicochemical properties of goose myofibrillar proteins (MP) including solubility and water-holding capacity. Elevated carbonyl contents indicated an enhanced gel-forming capacity in RTC goose meat during storage, accompanied with reduced total sulfhydryl contents from enhanced protonation pretreatment and augmented lipid oxidation. Structural characterization of MP via sodium dodecyl sulfate-polyacrylamide gel electrophoresis, circular dichroism spectroscopy, and intrinsic fluorescence revealed the formation of a dense protein matrix under highly acidic conditions. Furthermore, the headspace concentration of aldehydes increased by 3.23 times upon enhancing the pre-acidification intensity, resulting in the production of esters and acidic flavor compounds with favorable aromas. Correlation analysis demonstrated the dependence of headspace concentrations of volatile constituents on the acidification-enhanced surface hydrophobicity of MP, attributed to the modified binding sites of proteins after pre-acidification. Current results have indicated both the positive and negative influence of pre-acidulation induction on the eating quality of goose meat products, suggesting the necessity of introducing extra processes to modulate the quality of prefabricated products.

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