Alleoni A C. 2006. Albumen protein and functional properties of gelation and foaming. Scientia Agricola. 63(3)291-299.
A review paper
• Hen egg white protein coagulation orchestrates the success of many cooked foods, such as bread, cakes, cookies and other bakery products, as they act to link ingredients together.
• The proteins depend on polymerization to make gel networks that allow for the incorporation, encapsulation and retaining of air that is important to maintain the texture of these foods.
• The authors present various pieces of evidence that suggest that an increase in s-ovalbumin decreases the stability of the foam formed in these baked products
Deleu L J, Wilderjans E, Haesendonck I V, Courtin …show more content…
Jones D R, Musgrove M T. 2007. Effects of extended storage on egg quality factors. Poultry Science. 84(11):1774-7.
A primary research paper
• The article aims to study the effects of long-term cold storage of shell eggs on the quality factors such as egg weight, shell strength, albumen height, Haugh units and vitelline membrane strength with the current standards of production, processing and storage.
• While shell and vitelline membrane strength did not change over time, there was an observed decrease in egg weight, albumen height and Haugh units with an increase in cold storage time.
• From the findings of the study, the authors conclude that refrigerating shell eggs does not compromise their quality factors but instead could extend their shelf life without affecting consumer product satisfaction.
Jones D R. 2007. Egg functionality and quality during long-term storage. International Journal of Poultry Science. 6(3):157-162.
A primary research …show more content…
Qun H, Mei-hu M, Xi H, Yong-guo J, Fang G. 2012. Effect of S-configuration transformation of ovalbumin on its molecular characteristics and emulsifying properties. Asian Journal of Chemistry. 24(4):1675-1679.
A primary research paper
• The authors aimed to study the how the transformation of natural ovalbumin to S-ovalbumin affects the emulsibility and molecular characteristics such as hydrophobicity and zeta potential of s-ovalbumin.
• After ovalbumin is converted to an s-configuration there is an observed increase in free amino groups, hydrophobicity and emulsifying activity while there is a decrease in zeta potential, emulsifying stability and emulsion droplet size suggesting a correlation between the molecular characteristics of S-ovalbumin and its emulsification properties.
• The authors conclude that although the emulsification activity improved by the transformation from natural ovalbumin to S-ovalbumin, the stability of the emulsifications declines, suggesting that perhaps the transformation leads to a decline in shell egg