Feibai Zhou

Effect of Oxidation on the Emulsifying Properties of Myofibrillar Proteins

The aim of this work was to investigate the effect of chemical oxidation on the emulsifying properties of myofibrillar proteins. Myofibrillar proteins were oxidized by a hydroxyl radical generating system (Fenton reaction). Structural changes of oxidized or non-oxidized myofibrillar proteins were determined using surface hydrophobicity (H0) and Fourier transform infrared (FTIR) spectroscopy. The results suggested that H0 increased (p < 0.05) after treatment with oxidizing agent. Result from FTIR suggested that protein aggregation occurred and there was an increase in β-sheet structure accompanied by a decrease in turns, alpha helix, and random structures with the increase of oxidizing agent. Changes in zeta potential of the test emulsions suggested that protein oxidation could alter the electric charge of myofibrillar proteins. The analysis of the emulsions showed that protein oxidation had a negative effect on the emulsifying properties of myofibrillar proteins due to changes in electric charge, surface active properties, and protein molecular flexibility.

Physicochemical changes of myofibrillar proteins during processing of Cantonese sausage in relation to their aggregation behaviour and in vitro digestibility

The physicochemical changes of myofibrillar proteins, especially oxidation behaviour, were measured to determine their mechanism of action on in vitro protein digestibility during Cantonese sausage processing. The results indicated that the carbonyl level significantly increased (p<0.05) during the process. The SH group level decreased, while S-S group level increased gradually. Protein aggregation was induced by oxidation and heat treatment. Result from Fourier transform infrared (FTIR) spectroscopy confirmed protein aggregation occurred. The analysis of in vitro digestibility showed a highly significant (p<0.05) correlation between pepsin activity and carbonyl group formation, S-S group level, protein surface hydrophobicity, D4,3. A negative and highly significant correlation between trypsin, α-chymotrypsin activity and carbonyl group formation was measured, while no significant correlation with S-S groups, protein surface hydrophobicity, D4,3 was observed. It indicated that not only protein oxidation and aggregation but also degradation by pepsin would influence proteolysis with trypsin and α-chymotrypsin.

Changes in lipid composition, fatty acid profile and lipid oxidative stability during Cantonese sausage processing

Lipid composition, fatty acid profile and lipid oxidative stability were evaluated during Cantonese sausage processing. Free fatty acids increased with concomitant decrease of phospholipids. Total content of free fatty acids at 72 h in muscle and adipose tissue was 7.341 mg/g and 3.067 mg/g, respectively. Total amount of saturated, monounsaturated and polyunsaturated fatty acids (SFA, MUFA, and PUFA) in neutral lipid exhibited a little change during processing, while the proportion of PUFA significantly decreased in the PL fraction. The main triacylglycerols were POO+SLO+OOO, PSO (P = palmitic acid, O = oleic acid, L = linoleic acid, S = stearic acid), and a preferential hydrolysis of palmitic, oleic and linoleic acid was observed. Phosphatidylcholines (PC) and phosphatidylethanolamines (PE) were the main components of phospholipids and PE exhibited the most significant degradation during processing. Thiobarbituric acid values (TBARS) increased while peroxide values and hexanal contents varied during processing.

Binding of Aroma Compounds with Myofibrillar Proteins Modified by a Hydroxyl-Radical-Induced Oxidative System

The objective of this study was to investigate the influence of oxidation-induced structural modifications of myofibrillar protein on its binding ability with aroma compounds such as 2-methyl-butanal, methional, 2-pentanone, 2-heptanone, and nonanal. A method using solid-phase microextraction (SPME) combined with gas chromatography/mass spectrometry (GC/MS) was used to determine the corresponding binding ability. The binding with aroma compounds was found to be strongly affected by the oxidation levels of proteins, probably due to the varying modifications in protein structure and surface. Incubation with oxidants around or below 1 mM mainly caused the refolding of protein structure and accelerated the protein aggregation, which reduced the affinity of the aroma compounds, thus decreasing the binding ability. Nevertheless, treatment with oxidants over 2.5 mM would cause protein reaggregation and partial degradation, and thus, the subsequent modification of protein surface properties. The aggregated protein with wrinkled surfaces favored the hydrophobic interactions with aroma compounds, forming the protein-aroma compound complex, thus enhancing the resultant binding ability as evidenced by fluorescence quenching and SPME-GC/MS analysis.

Iron(II) Initiation of Lipid and Protein Oxidation in Pork: The Role of Oxymyoglobin

Iron(II), added as FeSO4·7H2O, was found to increase the rate of oxygen depletion as detected electrochemically in a pork homogenate from Longissimus dorsi through an initial increase in metmyoglobin formation from oxymyoglobin and followed by formation of primary and secondary lipid oxidation products and protein oxidation as detected as thiol depletion in myofibrillar proteins. Without added iron(II), under the same conditions at 37 °C, oxygen consumption corresponded solely to the slow oxymyoglobin autoxidation. Long-lived myofibrillar protein radicals as detected by ESR spectroscopy in the presence of iron(II) were formed subsequently to oxymyoglobin oxidation, and their level was increased by lipid oxidation when oxygen was completely depleted. Similarly, the time profile for formation of lipid peroxide indicated that oxymyoglobin oxidation initiates both protein oxidation and lipid oxidation.

Surface Characterization of Oxidized Myofibrils Using X-ray Photoelectron Spectroscopy and Scanning Electron Microscopy

The functional properties of myofibrils depend largely on their surface characteristics. Changes in surface characteristics of myofibrils after chemical oxidation were elucidated using X-ray photoelectron spectroscopy (XPS) and scanning electron microscopy. Myofibrils were oxidized by a hydroxyl radical generating system. Lipid oxidation and phospholipid distribution were altered during the oxidative processing. Results from particle size analysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and salt solubility indicated that protein cross-linking and fragmentation occurred during the oxidation of myofibrils. XPS analysis of C 1s, N 1s, and O 1s spectra suggested that surface chemical function concentrations changed significantly because of the modification of amino acid side chains that rendered protein cross-links and fragmentation and phospholipid alteration. Analysis of the correlation between the surface chemical composition and parameters of particle size distributions confirmed that protein carbonylation and phospholipid alteration were involved in protein surface modification. Results of the microstructure analysis were in agreement with those of particle size and XPS analysis.

Protective Effect of Bovine Elastin Peptides against Photoaging in Mice and Identification of Novel Antiphotoaging Peptides

This study aimed to investigate the protective effects of bovine elastin hydrolysates on UV-induced skin photoaging in mice and to identify the potent antiphotoaging peptides. Results showed that the ingestion of elastin peptides could obviously ameliorate epidermis hyperplasia and fibroblast apoptosis, and increase the content of hydroxyproline and water in photoaging skin in vivo ( p < 0.05). Furthermore, four peptides with elastase inhibitory activity were purified and identified, including GLPY, PY, GLGPGVG, and GPGGVGAL. Interestingly, GLPY and GPGGVGAL exhibited the highest inhibition activity with 58.77% and 42.91% at 10 mΜ, respectively. This might be attributed to the N-terminal Gly, C-terminal Leu, and Pro at the third position of the N-terminus, which showed stronger affinity and interaction with elastase. Moreover, GLPY and GPGGVGAL could also inhibit the apoptosis of fibroblasts effectively at 50 μΜ ( p < 0.01). It suggested that elastin peptides had great potential to prevent and regulate skin photoaging.

Development of a Sono-Assembled, Bifunctional Soy Peptide Nanoparticle for Cellular Delivery of Hydrophobic Active Cargoes

Soy proteins are prone to aggregate upon proteolysis, hindering their sustainable development in food processing. Here, a continuous work on the large insoluble peptide aggregates was carried out, aiming to develop a new type of soy peptide-based nanoparticle (SPN) for active cargo delivery. Sono-assembled SPN in spherical appearance and core-shell structure maintained by noncovalent interactions was successfully fabricated, exhibiting small particle size (103.95 nm) in a homogeneous distribution state (PDI = 0.18). Curcumin as a model cargo was efficiently encapsulated into SPN upon sonication, showing high water dispersity (129.6 mg/L, 104 higher than its water solubility) and storage stability. Additionally, the pepsin-resistant SPN contributed to the controlled release of curcumin at the intestinal phase and thus significantly improved the bioaccessibility. Encapsulated curcumin was effective in protecting glutamate-induced toxicity in PC12 cells, where the matrix SPN can simultaneously reduce lipid peroxidation and elevate antioxidant enzymes levels, innovatively demonstrating its bifunctionality during cellular delivery.

Interaction of β-conglycinin with catechin-impact on physical and oxidative stability of safflower oil-in-water emulsion

The study aimed at improving the antioxidant activity of β-conglycinin to enhance the oxidative and physical stabilities of safflower oil-in-water emulsion stabilized by β-conglycinin. Heating promoted binding affinity and antioxidant activity of β-conglycinin. Catechin and chlorogenic acid showed higher binding affinities towards unheated (or heated) β-conglycinin than caffeic acid and quercetin. The enhancement efficiencies of the phenolics on the antioxidant activity of unheated (or heated) β-conglycinin decreased in the order of catechin > quercetin > chlorogenic acid > caffeic acid. Hydrophobic force and hydrogen bonding were the important binding forces for the selected phenolics to β-conglycinin. The complexation with catechin has no side effect on interfacial behavior and emulsifying property of β-conglycinin. The use of heated β-conglycinin-catechin complex as an emulsifier for preparing safflower oil emulsion effectively improved the oxidative and physical stabilities of the emulsion treated with lipoxygenase through inhibition of lipid oxidation, protein carbonyl formation and sulfhydryl loss.

Particulate nanocomposite from oyster (Crassostrea rivularis) hydrolysates via zinc chelation improves zinc solubility and peptide activity

An oyster protein hydrolysates-zinc complex (OPH-Zn) was prepared and investigated to improve zinc bioaccessibility. Zinc ions chelating with oyster protein hydrolysates (OPH) cause intramolecular and intermolecular folding and aggregation, homogeneously forming the OPH-Zn complex as nanoclusters with a Z-average at 89.28 nm (PDI: 0.16 ± 0.02). The primary sites of zinc-binding in OPH were carboxyl groups, carbonyl groups, and amino groups, and they were related to the high number of charged amino acid residues. Furthermore, formation of the OPH-Zn complex could significantly enhance zinc solubility both under specific pH conditions as well as during simulated gastrointestinal digestion, compared to the commonly used ZnSO4. Additionally, after digestion, either preserved or enhanced antioxidant activity of OPH was found when chelated with zinc. These results indicated that the OPH-Zn complex could be a potential functional ingredient with improved antioxidant bioactivity and zinc bioaccessibility.