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Characterization of Egg White Proteins

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Student
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General public
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biology
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Monash...

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documents in English
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case study
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28 pages
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  1. Introduction
  2. Methods and Materials
  3. Isolation of lysozyme
  4. Activity and Assay of Lysozyme
  5. Iron binding Capacity of Conalbumin II
  6. Conclusion

Egg white or albumin is the biggest fraction of whole egg and contains 88% water, 11% proteins, 0.2% fats and 0.2% minerals. The major constituent of egg white proteins are 60% of ovalbumin, 12% of conalbumin, 11% of ovomucoid, and 3.5% of lysozyme. It also contains small amount of ovoinhibitor, ovoglycoprotein, flavoprotein, avidin and ovoglobulins (Brown 2010).

Ovalbumin is the most abundant egg white protein with isoelectric point of 4.58. It has molecular weight of 44.5kDa (Coultate 2009). Ovalbumin is found to have antimicrobial effect, due to its ability to bind iron. This causes deprivation of irons essential for growth of microorganisms (Abdou et al. 2013). It is also suggested that the hydrophobicity and its positive charge contributes to ovalbumin's bactericidal actions against Gram-negative bacteria (Belitz et al. 2009). It also acts as a storage proteins and major nutrient source of amino acids for embryo in late developing stage (Mine & Yang 2008). In food industry, the amphilic behavior of ovalbumin makes it suitable to be used as foaming agent. It is used mainly as stabilizer in bakery products where their texture and structure have to be maintained during and after processing (Du et al. 2002). In medical field, ovalbumin is administered when there is suspected heavy metal poisoning to chelate the metal ions, preventing them to be further absorbed through digestive system.

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