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Egg Yolk Phosvitin and Functional Phosphopeptides—Review
Author(s) -
Samaraweera Himali,
Zhang Wangang,
Lee Eun Joo,
Ahn Dong U
Publication year - 2011
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1750-3841.2011.02291.x
Subject(s) - phosvitin , yolk , chemistry , casein , calcium , biomolecule , bioavailability , biochemistry , food science , phosphorylation , biology , organic chemistry , bioinformatics , protein kinase a
Phosphopeptides are among the most interesting biomolecules with characteristic molecular structure and functions. They usually contain clusters of phosphoserines, which can effectively bind calcium and iron, and inhibit formation of insoluble calcium phosphates or iron complexes. Therefore, phosphopeptides can increase calcium or iron bioavailability and prevent lipid oxidation in foods. Milk protein casein has been currently used by industry to produce phosphopeptides. Egg yolk phosvitin is considered as the most phosphorylated protein found in the nature. Phosvitin from egg yolk can be much better source for producing phosphopeptides with varying sizes and functions than casein because it contains much greater number of phosphates in the molecule than casein. However, still phosvitin has not been subjected to considerable attention with regard to bioactive peptides production.