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Food Chemistry Aug 2023Nicotinamide mononucleotide (NMN) has been recognized as a promising bio-active compound in relieving aging-related mitochondrial dysfunction. Self-assembled...
Nicotinamide mononucleotide (NMN) has been recognized as a promising bio-active compound in relieving aging-related mitochondrial dysfunction. Self-assembled nanoparticles were prepared based on interaction between ovalbumin (OVA) and fucoidan to improve the stability and bio-accessibility of NMN. The OVA-fucoidan nanoparticles (OFNPs) displayed outstanding thermal stability and entrapment ability of NMN. The reactive oxygen species (ROS) analysis and senescence-associated β-galactosidase (SA-β-gal) staining characterization indicated that NMN encapsulated by OFNPs could effectively alleviate the cellular senescence of d-galactose-induced senescent cells. In vivo Caenorhabitis elegans experiment demonstrated that NMN-loaded OFNPs caused less accumulation of lipofuscin and protected NMN from thermal damage. Compared with free NMN, the NMN-loaded OFNPs prolonged lifespan from 28 to 31 days, increased 26% reproductive ability, and improved 12% body length of Caenorhabitis elegans. The results indicated that the use of nanocarriers could be a good strategy to improve anti-oxidative stress and anti-aging ability of NMN.
Topics: NAD; Nicotinamide Mononucleotide; Ovalbumin; Polysaccharides; Nanoparticles
PubMed: 36996645
DOI: 10.1016/j.foodchem.2023.135982 -
Bioelectrochemistry (Amsterdam,... Aug 2021A novel, sensitive and selective electrochemical sensor based on epitope-imprinted polydopamine (PDA) was developed for ovalbumin (OVA) detection. Molecularly imprinted...
A novel, sensitive and selective electrochemical sensor based on epitope-imprinted polydopamine (PDA) was developed for ovalbumin (OVA) detection. Molecularly imprinted polydopamine was synthesized on an AuNP-coated screen-printed carbon electrode (SPCE) via electropolymerization in the presence of OVA IgE-binding epitope as the template. Key process parameters including template concentration, electropolymerization cycle, pH, time required for template removal and rebinding were optimized. Electrochemical detection of OVA was performed by differential pulse voltammetry (DPV) in 5 mM KFe(CN) and 0.1 M KCl as the supporting electrolyte. Under optimized conditions, the sensor demonstrated excellent sensitivity toward OVA with linear range from 23.25 to 232.50 nM (1 to 10 ppm), limit of detection (LOD) of 10.76 nM (0.46 ppm), and limit of quantification (LOQ) of 35.87 nM (1.54 ppm). The sensor also exhibited good selectivity against other proteins such as human serum albumin (HSA), bovine serum albumin (BSA), and lysozyme (LYZ). OVA in wine samples was detected with RSD of 5.63-10.82%, and recovery percentage of 104.74-105.96%. The developed method can be easily adapted to detect other allergic proteins in the food supply chain.
Topics: Animals; Carbon; Cattle; Electrochemistry; Electrodes; Epitopes; Humans; Indoles; Limit of Detection; Ovalbumin; Polymers
PubMed: 33838516
DOI: 10.1016/j.bioelechem.2021.107805 -
Food Chemistry Mar 2023Egg proteins, as one of the most abundant animal protein sources, have received considerable attention for developing delivery systems. Among all egg proteins, egg white... (Review)
Review
Egg proteins, as one of the most abundant animal protein sources, have received considerable attention for developing delivery systems. Among all egg proteins, egg white (ovalbumin) is the most promising encapsulant due to its excellent properties such as gelling, digestibility, self-assembly, amphiphilic nature. In this review paper, we focused particularly on egg protein-based delivery systems with superior encapsulation and delivery functions, including polymeric nanoparticles, emulsions, hydrogels and aerogels. Egg protein-based delivery systems across a wide range of geometry and dimensions have been applied to protect or control-release bioactive small molecules and macromolecules, probiotics and metal nanostructures. However, there are challenges that must be carefully addressed for advancing the practical applications of egg protein-based delivery system in foods, including allergenicity from ovalbumin and ovotransferrin, intolerance to environmental conditions, limited processing technologies. More efforts are warranted to fill knowledge gaps related to fabrication, utilization and digestive mechanisms of egg protein-derived delivery systems.
Topics: Animals; Ovalbumin; Egg Proteins; Egg White; Conalbumin; Hydrogels
PubMed: 36179637
DOI: 10.1016/j.foodchem.2022.134353 -
International Journal of Biological... Aug 2019The surface properties and foaming of ovalbumin and guar gum aqueous solutions was investigated in the presence of sucrose or sorbitol. All solutions had a broad...
The surface properties and foaming of ovalbumin and guar gum aqueous solutions was investigated in the presence of sucrose or sorbitol. All solutions had a broad particle size distribution (395.60 at 1137.50 nm). Higher ovalbumin concentrations had lower equilibrium surface tension and higher absolute values of the zeta potential, regardless the presence of sucrose or sorbitol. Mixtures containing ovalbumin and guar gum resulted in a predominantly elastic character of the air-water interface probably due to the formation of a complex (hydrogen bonding and/or hydrophobic interactions) between ovalbumin and guar gum. Besides, the increase in guar gum concentration enhanced the elasticity of the surface film. Higher concentrations of both polymers were required to provide higher kinetic stability to the system, although the increase in guar gum concentration reduced foam capacity due to the increase in the apparent viscosity. Foams formed in the presence of sucrose or sorbitol showed similar half-lives.
Topics: Galactans; Mannans; Ovalbumin; Particle Size; Plant Gums; Rheology; Sorbitol; Sucrose; Surface Properties; Surface Tension; Viscoelastic Substances
PubMed: 31128179
DOI: 10.1016/j.ijbiomac.2019.05.140 -
Cardiovascular Toxicology Aug 2022Clinical observations have shown the risk of cardiovascular disease during asthmatic changes. Whether and how asthma causes heart failure is the subject of debate. Here,...
Clinical observations have shown the risk of cardiovascular disease during asthmatic changes. Whether and how asthma causes heart failure is the subject of debate. Here, we aimed to investigate the possibility of cardiomyocyte mitophagy in a rat model of asthma. Twelve mature Wistar rats were randomly allocated into the Control and Asthmatic rats (n = 6). To induce asthma, ovalbumin was injected intraperitoneally on days 1 and 8 and procedure followed by nebulization from days 14 to 32. After 2 weeks, we performed the pathological examination of both lungs and heart using Hematoxylin-Eosin staining. Real-time PCR analysis was used to measure the expression of mitophagic factors, such as Optineurin, Pink1, and mitofusin 1 and 2. Typical changes like increased inter-alveolar septa thickness and interstitial pneumonia were evident in asthmatic lungs. In cardiac tissue, slight inflammatory response, and hydropic degeneration with an eosinophilic appearance were detected in the cytoplasm of cardiomyocytes. Real-time PCR analysis showed mitophagic response in pulmonary and cardiac tissues via upregulation of mitophagy-related genes like Optineurin and Pink-1 in asthmatic lungs and hearts compared to the control group (p < 0.05). Likewise, asthmatic changes increased the expression of genes associated with mitochondrial fusion in the lungs and heart. The expression of mitofusin1 and 2 was significantly increased following inflammatory response in pulmonary and cardiac tissues (p < 0.05). Our findings showed the expression of certain factors related to mitophagy during chronic asthmatic conditions. The findings open a new avenue in the understanding of cardiomyocyte injury during asthma.
Topics: Animals; Asthma; Lung; Mitophagy; Myocytes, Cardiac; Ovalbumin; Rats; Rats, Wistar
PubMed: 35687292
DOI: 10.1007/s12012-022-09757-3 -
International Journal of Biological... May 2024Contaminating microplastics can interact with food proteins in the food matrix and during digestion. This study investigated adsorption of chicken egg protein ovalbumin...
Contaminating microplastics can interact with food proteins in the food matrix and during digestion. This study investigated adsorption of chicken egg protein ovalbumin to polystyrene (PS, 110 and 260 μm) and polyethylene terephthalate (PET, 140 μm) MPs in acidic and neutral conditions and alterations in ovalbumin structure. Ovalbumin adsorption affinity depended on MPs size (smaller > larger), type (PS > PET) and pH (pH 3 > pH 7). In bulk solution, MPs does not change ovalbumin secondary structure significantly, but induces loosening (at pH 3) and tightening (at pH 7) of tertiary structure. Formed soft corona exclusively consists of full length non-native ovalbumin, while in hard corona also shorter ovalbumin fragments were found. At pH 7 soft corona ovalbumin has rearranged but still preserved level of ordered secondary structure, resulting in preserved thermostability and proteolytic stability, but decreased ability to form fibrils upon heating. Secondary structure changes in soft corona resemble changes in native ovalbumin induced by heat treatment (80 °C). Ovalbumin is abundantly present in corona around microplastics also in the presence of other egg white proteins. These results imply that microplastics contaminating food may bind and change structure and functional properties of the main egg white protein.
Topics: Ovalbumin; Polystyrenes; Microplastics; Polyethylene Terephthalates; Hydrogen-Ion Concentration; Adsorption; Animals; Chickens; Protein Structure, Secondary
PubMed: 38614174
DOI: 10.1016/j.ijbiomac.2024.131564 -
Frontiers in Cellular and Infection... 2023Helminth derived excretory/secretory molecules have shown efficacy in the treatment of allergic asthma in mice, but their roles in allergic rhinitis (AR) are little...
Helminth derived excretory/secretory molecules have shown efficacy in the treatment of allergic asthma in mice, but their roles in allergic rhinitis (AR) are little known. In this study, we aimed to determine the intervention effect of SJMHE1, a derived small molecular peptide, on ovalbumin (OVA)-induced AR mice and investigate its possible mechanism. AR was induced in BALB/c mice, following which the mice were treated with phosphate-buffered saline (PBS), OVA and SJMHE1 respectively. SJMHE1 treatment improved clinical symptoms (rubbing and sneezing), suppressed infiltrates of inflammatory cells and eosinophils in nasal mucosa, modulated the production of type-2 (IL-4 and IL-13) and anti-inflammatory (IL-10) cytokines in the nasal lavage fluids (NLF), spleen, and serum. To investigate the underlying mechanism, fluorescein isothiocyanate (FITC)-labeled SJMHE1 was subcutaneously injected into AR mice, and we found that the FITC-SJMHE1 could accumulate in spleen, but not in nasal mucosa. FITC-SJMHE1 mainly bound to CD19 positive cells (B cells), and the SJMHE1 treatment significantly increased the proportion of regulatory B cells (Bregs) and B10 cells, along with the enhancement of PR domain containing protein 1 (Prdm1) protein levels. SJMHE1 may alleviate AR by upregulating Bregs, and has great potential as a new avenue for the AR treatment.
Topics: Animals; Mice; Schistosoma japonicum; Fluorescein-5-isothiocyanate; Rhinitis, Allergic; Peptides; Cytokines; Nasal Mucosa; Ovalbumin; Mice, Inbred BALB C; Disease Models, Animal
PubMed: 37346033
DOI: 10.3389/fcimb.2023.1143950 -
ChemistryOpen Apr 2023As vaccine adjuvants, polyacrylate materials can induce a specific immune response in the body and have been widely studied in recent years due to their advantages, such...
As vaccine adjuvants, polyacrylate materials can induce a specific immune response in the body and have been widely studied in recent years due to their advantages, such as their safety, effectiveness, and low required dosage. In this study, a series of polyacrylates with hydrophobic physical crosslinking and chemical crosslinking were prepared using precipitation polymerization, and their structures were characterized by nuclear magnetic resonance spectroscopy and Fourier-transform infrared spectroscopy. The optimal reaction conditions were determined according to the effect of reaction time, azodiisobutyronitrile, Span 60, allyl pentaerythritol, and octadecyl methacrylate (OMA) contents on the viscosity of the polyacrylate microgel, combined with the effects of allyl pentaerythritol and OMA contents on the subcutaneous immune safety of the polyacrylate microgel in BALB/c mice. The polyacrylate microgels with different OMA contents showed good biological safety. In addition, in vivo immunity experiments were carried out in mice to analyze the adjuvant properties of ovalbumin as a model antigen. Based on the titer results of the IgG1 and IgG2a antibodies, with 1 wt % OMA content, the polyacrylate microgel vaccine could optimally induce the body to produce an immune response type dominated by Th2-type humoral immune response and supplemented by Th1-type cellular immune response.
Topics: Animals; Mice; Microgels; Ovalbumin; Th1 Cells; Th2 Cells; Adjuvants, Immunologic; Antigens; Adjuvants, Pharmaceutic
PubMed: 37009889
DOI: 10.1002/open.202200246 -
International Journal of Molecular... May 2023Exposure to methylglyoxal (MGO) increases the levels of receptor for advanced glycation end products (RAGE) and reactive-oxygen species (ROS) in mouse airways,...
Exposure to methylglyoxal (MGO) increases the levels of receptor for advanced glycation end products (RAGE) and reactive-oxygen species (ROS) in mouse airways, exacerbating the inflammatory responses. Metformin scavenges MGO in plasma of diabetic individuals. We investigated if amelioration by metformin of eosinophilic inflammation reflects its ability to inactivate MGO. Male mice received 0.5% MGO for 12 weeks together or not with 2-week treatment with metformin. Inflammatory and remodeling markers were evaluated in bronchoalveolar lavage fluid (BALF) and/or lung tissues of ovalbumin (OVA)-challenged mice. MGO intake elevated serum MGO levels and MGO immunostaining in airways, which were reduced by metformin. The infiltration of inflammatory cells and eosinophils and levels of IL-4, IL-5 and eotaxin significantly increased in BALF and/or lung sections of MGO-exposed mice, which were reversed by metformin. The increased mucus production and collagen deposition by MGO exposure were also significantly decreased by metformin. In MGO group, the increases of RAGE and ROS levels were fully counteracted by metformin. Superoxide anion (SOD) expression was enhanced by metformin. In conclusion, metformin counteracts OVA-induced airway eosinophilic inflammation and remodeling, and suppresses the RAGE-ROS activation. Metformin may be an option of adjuvant therapy to improve asthma in individuals with high levels of MGO.
Topics: Male; Mice; Animals; Ovalbumin; Metformin; Pyruvaldehyde; Reactive Oxygen Species; Magnesium Oxide; Inflammation; Lung; Bronchoalveolar Lavage Fluid; Receptor for Advanced Glycation End Products; Airway Remodeling; Mice, Inbred BALB C; Disease Models, Animal
PubMed: 37298498
DOI: 10.3390/ijms24119549 -
Food & Function Apr 2023This study was designed to investigate the influence and effect mechanism of the filler type on the physicochemical properties, microbial numbers, and digestibility of...
This study was designed to investigate the influence and effect mechanism of the filler type on the physicochemical properties, microbial numbers, and digestibility of ovalbumin emulsion gels (OEGs) during storage. Sunflower oil was emulsified with ovalbumin (20 mg mL) and Tween 80 (20 mg mL) separately to prepare ovalbumin emulsion gels (OEGs) that contained active and inactive fillers, respectively. The formed OEGs were stored at 4 °C for 0, 5, 10, 15, and 20 days. The active filler enhanced the gel hardness, water holding capacity, fat holding capacity, and surface hydrophobicity and decreased the digestibility and free sulfhydryl content during storage compared to control (unfilled) ovalbumin gel, whereas the inactive filler had the opposite effects. Protein aggregation diminished, lipid particle aggregation increased, and the amide A band shifted to a higher wavenumber for all three types of gel during storage, suggesting that the compact network structure of the OEG became rough and disordered with storage. The OEG with the active filler did not inhibit microbial growth, and the OEG with the inactive filler did not significantly promote the development of bacteria. In addition, the active filler delayed the digestion of the protein in the OEG throughout storage. Emulsion gels containing active filler facilitated the retention of the gel properties during storage, whereas emulsion gels containing inactive filler exacerbated the loss of the gel properties during storage.
Topics: Emulsions; Ovalbumin; Proteins; Polysorbates; Gels
PubMed: 36995104
DOI: 10.1039/d2fo03526j