Egg yolk lecithin is a natural animal-derived phospholipid complex, primarily composed of phosphatidylcholine, phosphatidylethanolamine, sphingomyelin, lysophosphatidylcholine, and lysophosphatidylethanolamine, and has multiple bioactivities such as neuroprotection, hepatoprotection, anti-aging, and immunomodulation. Techniques such as solvent extraction, supercritical fluid extraction, membrane separation and column chromatography can effectively isolate lecithin from egg yolk, and the lecithin can be precisely characterized by mass spectrometry (MS)-based lipidomics. Egg yolk lecithin, a unique amphiphilic substance containing a hydrophilic polar phosphate head and a hydrophobic tail consisting of fatty acid chains, can form bilayer vesicles, making it suitable for encapsulating sensitive active substances or small molecule drugs to improve their bioavailability. The application scope of egg yolk lecithin has expanded from traditional foods to high-value-added pharmaceuticals, health foods and cosmetics, showing significant development potential. This article systematically reviews the structural characteristics, extraction and identification methods, bioactivities, and applications of egg yolk lecithin, with a view to providing a theoretical reference for its future research and high-value-added application.

3,5,6,7,8,3′,4′-Heptamethoxyflavone (HMF), one of the highest O-methyl numbers in the polymethoxyflavones, possesses various significant health benefits. However, the in vivo metabolic profile of HMF remains largely unexplored. In this study, a systematic identification and relative quantitation of HMF and its metabolites in rats were performed using UHPLC-LTQ-Orbitrap mass spectrometry combined with enzymatic hydrolysis. A total of 56 metabolites were tentatively identified, including 37 demethylated metabolites and 19 glucuronide conjugates of these demethylated products. Notably, all seven mono-demethylated metabolites of HMF were simultaneously detected and structurally discriminated for the first time in rats, along with other di-, tri-, tetra-, and penta-demethylated metabolites. Semi-quantitative analysis revealed that HMF underwent predominant biotransformation into mono-demethylated metabolites in rats, followed by progressive sequential demethylation of these metabolites to generate more di-, tri-, tetra-, and penta-demethylated metabolites. Demethylation and glucuronidation are the primary metabolic pathways of HMF in vivo. This study presents the first comprehensive elucidation of the in vivo metabolic profile of HMF, which is helpful for further understanding of its in vivo potential effective components and pharmacological mechanism.

The antioxidant and anti-aging activities of a sleep-promoting peptide from bovine milk were evaluated in this study. Four in vitro methods, namely 1,1-diphenyl-2-picrylhydrazyl (DPPH), 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), hydroxyl, and superoxide anion radical scavenging assays, were used to evaluate its antioxidant activity. Caenorhabditis elegans was used as a model organism to evaluate its anti-oxidant and anti-stress capacity in vivo. The results showed that the peptide scavenged 44.27% of DPPH, 18.37% of superoxide anion, 37.22% of hydroxyl radical and 24.83% of ABTS radical at 0.1 mg/mL. In addition, the sleep-promoting peptide obviously extended the life span of Caenorhabditis elegans, protected against oxidative stress and heat stress, improved the mobility of Caenorhabditis elegans without damaging its reproductive ability, significantly increased the activity of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px), and significantly reduced malondialdehyde (MDA) content (P < 0.05, P < 0.01). In conclusion, the sleep-promoting peptide has good antioxidant and anti-stress effects both in vivo and in vitro, and thus shows promise for wide application.

As one of the major sources of protein in the human diet, chicken is characterized by high protein and low fat. Fresh chicken is susceptible to spoilage by microorganisms and enzymes during storage. Freezing is an effective way to extend the storage period of chicken, but ice crystals formed during the freezing process can negatively impact the chemical quality attributes of chicken, thereby affecting its eating quality. This article reviews traditional, modern, and emerging chicken freezing techniques, and elucidates the effects of freezing rate, freezing method, freezing temperature, freezing time, and freeze-thaw cycle on the quality of frozen chicken, with a focus on the changes in the eating quality (color, waterholding capacity, tenderness, and flavor) and chemical quality attributes (moisture, proteins, lipids, and pH) of chicken during freezing and frozen storage. It is our hope that this review will provide a theoretical reference for improving the key quality attributes of frozen chicken and extending its storage period.