The Relative Biochemical Studies of Avian Egg White Proteins
Sanjeev Kumar Shukla*, Shubhra Shukla and Jose MathewDepartment of Biotechnology, Bundelkhand University, Jhansi India.
Corresponding Authior E-mail:sanjeevcloning@gmail.com
Abstract: Avian egg whites are a rich source of protein inhibitors of proteinases. This work describes the use of different high resolution techniques to study egg white proteins from avian species. In addition to their nutritional importance, egg white proteins present multiple functional properties, such as foaming, emulsification and heat-setting. The egg whites of 20 different avian species or varieties were examined by specific biochemical and chemical analyses, by chromatographic separations of the constituent proteins, and by examinations of the properties of several of the purified proteins. The constituents studied included sulfhydryl groups, sialic acid, lysozyme, apoprotein-flavoprotein, conalbumin, and ovalbumin. Large differences were found in the amounts of these substances in the whites from the different birds. In the cases of lysozyme and sialic acid, differences as great as 30-fold were found. Differences in the properties of several of the purified proteins were also found. The significances and values of the results from the standpoints of comparative and genetic biochemistry were discussed.
Keywords: Egg white protein; Lysozyme; Poultry species Back to TOC