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A comprehensive UPLC-MS/MS-based lipidomics analysis of egg yolk at different storage periods was performed. Through the analysis, 836 lipid species from 27 subclasses were detected, including 159 significantly different lipid species. Glycerolipids (GL) and glycerophospholipids (GP) were the most abundant lipids, followed by fatty acyls (FA), sphingolipids (SP), sterol lipids (ST), and prenol lipids (PR). PCA and OPLS-DA showed that egg yolk lipids changed significantly with prolonged storage. Moreover, glycerophospholipid metabolism and glycerolipid metabolism were key metabolic pathways, as phosphatidic acid (PA), lysophosphatidic acid (LPA), and diglyceride (DG) were key lipid metabolites in the related metabolic pathways of egg yolk during storage. Furthermore, egg yolk quality changed the most when stored up to 21 days. Our study establishes a foundation for the quality control and the lipid oxidation mechanism of eggs during storage.

The present study attempted to investigate the interactive roles of protein oxidation (0-20 mM H

This study aimed to evaluate the effect of inclusion complexes (ICs) on the oxidative stability of myofibrillar proteins (MPs) and microstructures in lamb during frozen storage. The inclusion process between apple polyphenols (APs) and hydroxypropyl-β-cyclodextrin (HP-β-CD) was verified using Fourier transform infrared spectroscopy, thermogravimetric analysis, scanning electron microscopy, and the antioxidant activity of APs. Results showed that the sensitivity of MPs to oxidation improved after 40 weeks. The ICs (0.2-1.6 mg/mL) significantly reduced the carbonyl content, particle size aggregation, protein degradation, fluorescence quenching effect, and decreased the α-helix contents loss of MPs. Additionally, the changes in protein oxidation showed a correlation with the microstructure of muscles, and the addition of 1.6 mg/mL IC remarkably improved the structure of muscle tissues while that of 3.2 mg/mL IC was detrimental to the structural properties. Overall, the exertion of antioxidant activity significantly influenced the cryoprotective effect of ICs on frozen lamb meat.

Six key stages in the processing of dry-cured muton ham were selected, and changes in the main lipid metabolites as well as the major pathways involved were identified using a lipidic metabolomics approach based on UPLC-MS-MS. In total, 581 lipid metabolites from 22 subclasses were identified, including 521 significantly differential lipids (p 0.05, VIP 1). Glycerolipids (GL) were the most abundant lipids, followed by glycerophospholipids (GP), fatty acyls (FA), and sphingolipids (SL). PCA and OPLS-DA of metabolites showed that the quality of mutton ham changed the most during the P3 fermenting stage, including TG(18:1/18:2/18:3), PE(20:5/18:1), and TG(16:1/18:1/18:4) that were significantly downregulated, and CE(20:3), FFA(24:6), LPC(20:3/0:0), and FFA(18:4) that were significantly upregulated. Moreover, glycerophospholipid metabolism and sphingolipid metabolism were the key metabolic pathways involved in the processing of dry-cured mutton ham. Our results provide a basis for quality control and product improvement of dry-cured mutton ham.

In this study, the structural, interfacial, and emulsifying properties of high-intensity ultrasound (HUS)-treated pea protein isolate (PPIUS) were investigated. HUS at 50% amplitude and 57–60 W·cm−2 for 5 min markedly improved protein solubility (by 132%), surface hydrophobicity (by 173%), and reduced particle size (by 52%). These physicochemical changes in PPIUS led to more rapid protein adsorption at the oil–water interface, improved emulsifying activity (by 18–27%) and capacity (by 11%), and enhanced emulsion physical stability. The multilayer nature, albeit less elastic, of the interfacial membrane formed by PPIUS when compared to control protein (PPIC), based on dilatational testing, contributed to the above results. Moreover, PPIUS-stabilized emulsions exhibited a tendency of being less susceptible to lipid oxidation during storage. Thus, structure-modifying HUS may be a valuable processing technology for the manufacture of pea protein-based emulsion foods.

Phosphates are commonly included in meat processing, where oxidation is inevitable, to improve water binding. This present study attempted to reveal the interactive roles of protein oxidation and tetrasodium pyrophosphate (TSPP) on the crosslinking pattern of myosin mediated by transglutaminase (TGase). Mild oxidation at 1 mM H2O2 facilitated the TGase-initiated crosslinking, with the dominate crosslinking site shifted from S1 (in nonoxidized myosin) to Rod. The introduction of TSPP alleviated the oxidation stress on proteins, and was conductive to the crosslinking reaction notably at the LMM domain. The crosslinking sites in untreated myosin were identified as Gln-613 (S1) and Gln-1498 (LMM) by amino-acid sequence analysis, while strongly oxidation resulted in the loss of Gln-1498. Contrastively, four new reactive crosslinking sites were generated by TSPP, one (Gln-558/Gln-567) located on S1 and three (Gln-1362, Gln-1374, and Gln-1423/Gln-1426) on LMM. Yet, Gln-1362 was eliminated under strong oxidation at 50 mM H2O2.