Chicken egg yolk antibody (IgY) raised against Salmonella enteritidis or Salmonella typhimurium was found in highly specific activity levels by ELISA. S. enteritidis- and S. typhimurium-specific IgY powder, prepared by freeze-drying the egg yolk water-soluble fraction, contained 15.5 and 10.0% of specific IgY, respectively. Anti-S. enteritidis IgY cross-reacted 55.3% with S. typhimurium. The cross-reactivity of anti-S. typhimurium IgY with S. enteritidis was 42.4%. Salmonella-specific IgY was demonstrated to inhibit Salmonella growth in liquid medium. The growth rate of S. enteritidis incubated with S. enteritidis-specific IgY was fourfold less than that of the control group during a 4-to-6-h incubation. Cell counts of S. typhimurium incubated with S. typhimurium-specific IgY were reduced by 1.6 log cfu/mL in comparison to that of the control group after 6 h of incubation. The specific binding activity of IgY was further evaluated by using immunofluorescence and immunoelectron microscopy. It was found that Salmonella-specific IgY could bind to the antigens expressed on the Salmonella surface, resulting in structural alterations of the bacterial surface.

Escherichia coli O157:H7-specific antibodies (immunoglobulin Y [IgY]) were isolated by the waterdilution method from the egg yolk of chickens that were immunized with E. coli O157:H7 whole cells. The specificbinding activity of IgY against E. coli O157:H7 as determined by the enzyme immuno assay showed high levels of activity against bacterial whole cells. IgY binding activity was further demonstrated to have an inhibitory effect on E. coli O157:H7 growth in a liquid medium. The antibacterial function of IgY appeared to result from the interaction of IgY with surface components of E. coli O157:H7, as proven from observation of immunofluorescence and immunoelectron microscopy.

Casein-derived peptides are shown to possess radical scavenging and metal chelating properties. The objective of this study was to evaluate novel anti-inflammatory properties of casein hydrolysates (CH) produced by an eco-friendly process that combines high hydrostatic pressure with enzymatic hydrolysis (HHP-EH). Casein was hydrolysed by different proteases, including flavourzyme (Fla), savinase (Sav), thermolysin (Ther), trypsin (Try), and elastase (Ela) at 0.1, 50, 100, and 200 MPa pressure levels under various enzyme-to-substrate ratios and incubation times. Casein hydrolysates were evaluated for the degree of hydrolysis (DH), molecular weight distribution patterns, and anti-inflammatory properties in chemical and cellular models. Hydrolysates produced using HHP-EH exhibited higher DH values and proportions of smaller peptides compared to atmospheric pressure-enzymatic hydrolysis (AP-EH). Among five enzymes, Fla-digested HHP-EH-CH (HHP-Fla-CH) showed significantly higher antioxidant properties than AP-Fla-CH. The anti-inflammatory properties of HHP-Fla-CH were also observed by significantly reduced nitric oxide and by the suppression of the synthesis of pro-inflammatory cytokines in lipopolysaccharide (LPS)-stimulated RAW 264.7 macrophage cells. Liquid chromatography with tandem mass spectrometry (LC-MS/MS) revealed that 59% of the amino acids of the peptides in HHP-Fla-CH were composed of proline, valine, and leucine, indicating the potential anti-inflammatory properties. In conclusion, the HHP-EH method provides a promising technology to produce bioactive peptides from casein in an eco-friendly process.

Four different methods (direct-methylation, saponification, chloroform-methanol extraction, and postextraction saponification) were compared to determine the fatty acids in egg yolk. About 50 mg of pooled egg yolk samples, with C23:0 as an internal standard, was used for all assays. No difference (P > 0.05) was observed among the four methods for C17:0, C18:0, C18:1, C20:1, C18:2n-6, and C22:6n-3 content of egg yolk. Direct saponification resulted in a lower (P < 0.05) content of C14:0, C16:1, C18:3n-3, and C20:4n-6. Fatty acids at less than 0.5%, such as C15:0 and C14:1, were not detectable in the direct saponification method. The total saturated, monounsaturated, or polyunsaturated fatty acids did not differ (P > 0.05) among the four methods. Direct methylation of egg yolk resulted in lower variability than other methods and is fast and economic for determining egg fatty acid composition.

Immunization of chickens with whole bacteria results in the production of antibodies specific to lipopolysaccharide (LPS), a major constituent of the outer membrane of Gram-negative bacteria. However, there is relatively limited information available concerning immune response of purified LPS in this species. In the present study, immune responses were examined in serum and egg yolk from two groups of chickens injected with entire LPS from Escherichia coli and lipid A free LPS from Salmonella typhimurium. The results demonstrated that the increase of antibody activity occurs first in serum, and then in egg yolk with a lag in time of 1 to 3 wk in both groups of chickens. However, the time of elevated levels of antibodies activity was much shorter in chickens immunized with S. typhimurium LPS (< 1 wk) than in those immunized with E. coli LPS (4 wk). A lack of lipid A is the S. typhimurium antigen may be a factor related to this difference.