scholarly journals PEPTIC AND PANCREATIC DIGESTIBILITY OF RAW AND HEAT-COAGULATED HEN'S EGG WHITE PROTEINS

1999 ◽  
Vol 13 (1) ◽  
pp. 36-42 ◽  
Author(s):  
Kentaro Sakai ◽  
Yu Ushiyama ◽  
Sachinobu Manabe
Keyword(s):  
Egg White ◽  
Egg White Proteins ◽  
Hen’S Egg

Peptic digestibility of raw and heat-coagulated hen's egg white proteins at acidic pH range

2004 ◽  
Vol 55 (8) ◽  
pp. 635-640 ◽  
Author(s):  
Kenji Yoshino ◽  
Kentaro Sakai ◽  
Yoko Mizuha ◽  
Ayako Shimizuike ◽  
Shigeru Yamamoto
Keyword(s):  
Egg White ◽  
Acidic Ph ◽  
Egg White Proteins ◽  
Hen’S Egg ◽  
Ph Range

Microbial Contamination of the Hen's Egg: A Review

1983 ◽  
Vol 46 (12) ◽  
pp. 1092-1098 ◽  
Author(s):  
FRANCIS J. MAYES ◽  
MUSTAFA A. TAKEBALLI
Keyword(s):  
Microbial Contamination ◽  
Egg White ◽  
Shell Membrane ◽  
Egg White Proteins ◽  
Hen’S Egg ◽  
Bactericidal Properties ◽  
Bacterial Penetration ◽  
Physical And Chemical ◽  
Microbial Attack

The hen's egg is susceptible to microbial attack in a number of ways. The yolk or the albumen may be contaminated before the egg is laid. After the egg has been laid the possibility exists of microbial penetration from the outside. In this review, both these possibilities are discussed together with the defences, both physical and chemical, that the egg has against microbial contamination. Most eggs contain no bacteria when they are laid and only become contaminated subsequently. The shell membrane offers the best protection against bacterial penetration, but once inside the egg their growth and multiplication is slowed due to the viscous nature of the egg white proteins, their pH, and the bactericidal properties of lysozyme and conalbumen.

scholarly journals Extractability, Stability, and Allergenicity of Egg White Proteins in Differently Heat-Processed Foods

2007 ◽  
Vol 90 (2) ◽  
pp. 427-436 ◽  
Author(s):  
Christiane K Fste ◽  
Kjersti E Lvberg ◽  
Helene Lindvik ◽  
Eliann Egaas
Keyword(s):  
Egg White ◽  
Food Samples ◽  
Processed Foods ◽  
Heat Treated ◽  
Extraction Buffer ◽  
Egg White Proteins ◽  
Hen’S Egg ◽  
Study Results ◽  
The Stability ◽  
Protein Extractability

Abstract Hen's egg white protein is a major cause of food allergy, and a considerable number of countries have introduced labeling directions for processed food products. To control compliance with these regulations, analytical assays for the detection of egg in manufactured foods have been developed. In this study, we have tested the performance of 3 commercially available kits for quantitative egg analysis using 6 model heat-processed foods. The 3 assays worked well under standard conditions with soluble egg white proteins, but only the kit using a denaturing-reducing extraction buffer detected egg in complex heat-treated food matrixes. The differently extracted food samples were further used to evaluate the stability and allergenicity of the egg white allergens ovalbumin, ovomucoid, ovotransferrin, and lysozyme with polyclonal anti-egg antibodies and sera of 6 patients with egg allergy. It could be shown that differences in egg protein extractability have a significant impact on the interpretation of study results.

Identification of Egg White Proteins and Divergence in the Regulatory Region of the Ovalbumin Gene in Avians

2016 ◽  
Vol 24 (1) ◽  
pp. 12-25 ◽  
Author(s):  
Jindong Ren ◽  
Jianhong Hu ◽  
Li Chen ◽  
Yali Liu ◽  
Xiaoqin Xu ◽  
...  
Keyword(s):  
Regulatory Region ◽  
Egg White ◽  
Egg White Proteins

scholarly journals EGG WHITE PROTEINS

1950 ◽  
Vol 184 (1) ◽  
pp. 377-383 ◽  
Author(s):  
Richard H. Forsythe ◽  
Joseph F. Foster
Keyword(s):  
Egg White ◽  
Egg White Proteins
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