No abstract

The objective of this study was to evaluate the effects of an atmospheric pressure plasma (APP) jet on L. monocytogenes inactivation, quality characteristics, and genotoxicological safety of cooked egg white and yolk. APP treatment using He gas resulted in a 5 decimal reduction in the number of L. monocytogenes in cooked egg white, whereas that using He+O 2 , N 2 , and N 2 +O 2 decreased the number further, and to undetectable levels. All treatments of cooked egg yolk resulted in undetectable levels of inoculated L. monocytogenes. There were no viable cells of total aerobic bacteria after APP treatment on day 0 while the control showed approximately 3-4 Log CFU/g. On day 7, the numbers of total aerobic bacteria had increased by approximately 3 log cycles in cooked egg white, but there were no viable cells in cooked egg yolk after 2 min of APP jet. APP treatment decreased the L*-values of cooked egg white and yolk significantly on day 0. No significant sensory differences were found among the cooked egg white samples, whereas significant reductions in flavor, taste, and overall acceptability were found in cooked egg yolks treated with APP jets. SOS chromotest did not reveal the presence of genotoxic products following APP treatments of cooked egg white and yolk. Therefore, it can be concluded that APP jets can be used as a non-thermal means to enhance the safety and extend the shelf-life of cooked egg white and yolk.

No abstract

Molecular weights (MW) of major proteins in milk of 3 Korean dairy goat breeds were determined by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, after treatment of milk samples with the reduction buffer used in capillary electrophoresis. The MW of caprine milk proteins were compared with those of Holstein milk counterparts using commercial bovine milk protein standards. The MW of α-lactalbumin, β-lactoglobulin, and α- and β-casein standards were 14,197±3.4, 18,326±26.3, 23,591±13.0, and 23,967±12.8 m/z, respectively, whereas those of Holstein milk treated with the reduction buffer were 14,199±8.3, 18,397±25.9, 23,614±64.8, and 23,984±75.6 m/z, respectively. The respective MW of α-lactalbumin in Saanen, Toggenberg, and Alpine milk were 14,194±27.2, 14,266±105.9, and 14,241±13.2 m/z, which were not different from those of the bovine milk. The respective MW of β- lactoglobulin in corresponding caprine milk were 18,840±31.5, 18,856±26.3, and 18,857±21.3 m/z, which were higher than those in the bovine milk. The MW of β-casein in corresponding caprine milk were 23,860±27.2, 23,886±12.3, and 23,901±8.4 m/z, which were lower than those in the bovine milk. The results indicated that matrix-assisted laser desorption/ionization time-of-flight mass spectrometry could be used for rapid determination of MW of Korean caprine milk proteins without protein separation steps.