Phosvitin
Phosvitin is one of the egg (commonly hen's egg) yolk[1][2] phosphoproteins known for being the most phosphorylated protein found in nature.[3][4][5] Phosvitin isolation was first described by Mecham and Olcott in the year 1949.[3][6] Recently it has been shown that phosvitin orchestrates nucleation and growth of biomimetic bone like apatite.[7]
Structure
[edit]As the most phosphorylated natural protein, phosvitin contains 123 phosphoserine residues accounting for 56.7% of its total 217 amino acid residues.[3][8] The structure of phosvitin at large consists of 4-12 base pair stretches of serines, interspersed with amino acid residues lysine (6.9%), histidine (6.0%), and arginine (5.1%), among others in smaller quantities.[9] Phosvitin’s structure (right) is adapted from the protein vitellogenin (Gene: VTG2; Uniprot: P02845; residues 1-1850) generated by AlphaFold, where all the possible phosphorylated serine residues are highlighted in red. Phosvitin is one of four proteins cleaved from vitellogenin and is unstructured at neutral pH.[3] Despite phosvitin only accounting for 16% of total proteins in egg yolk, it alone accounts for 60% of the total yolk phosphoproteins as well as 90% of the total yolk phosphorus.[10][8]
Function
[edit]Due to phosvitin’s polyanionic activity, the protein performs functionalities such as metal chelation, emulsification, and nutrition sequestration for a growing embryo.[3] Additionally, in recent research it has been shown that the disordered secondary structure of phosvitin orchestrates nucleation and growth of biomimetic bone like apatite.[7]
References
[edit]- ^ Joubert, F. J.; Cook, W. H. (1958). "Preparation And Characterization Of Phosvitin From Hen Egg Yolk". Canadian Journal of Biochemistry and Physiology. 36 (4): 399–408. doi:10.1139/o58-045. PMID 13511246.
- ^ Clark, Richard C. (1980). "Relative and total abundance of constituent phosphoproteins from hen phosvitin in egg yolk". International Journal of Biochemistry. 12 (4): 651–653. doi:10.1016/0020-711x(80)90021-x. PMID 7428998.
- ^ a b c d e Samaraweera, Himali (Sep 2011). "Egg Yolk Phosvitin and Functional Phosphopeptides—Review". Journal of Food Science. 76 (7): R143–R150. doi:10.1111/j.1750-3841.2011.02291.x. PMID 21806612.
- ^ Taborsky, George (1963). "Interaction Between Phosvitin and Iron and Its Effect on a Rearrangement of Phosvitin Structure". Biochemistry. 2 (2): 266–271. doi:10.1021/bi00902a010. PMID 13980103.
- ^ Jung, Samooel; et al. (Dec 2012). "The functional property of egg yolk phosvitin as a melanogenesis inhibitor". Food Chemistry. 135 (3): 993–998. doi:10.1016/j.foodchem.2012.05.113. PMID 22953815.
- ^ Allerton, Samuel E.; Perlmank, Gertrude E. (Oct 1965). "Chemical Characterization of the Phosphoprotein Phosvitin". The Journal of Biological Chemistry. 240 (10): 3892–3898. doi:10.1016/S0021-9258(18)97126-7. PMID 5891575.
- ^ a b Sarem, Melika; Lüdeke, Steffen; Thomann, Ralf; Salavei, Pavel; Zou, Zhaoyong; Habraken, Wouter; Masic, Admir; Shastri, V. Prasad (2017-07-17). "Disordered Conformation with Low Pii Helix in Phosphoproteins Orchestrates Biomimetic Apatite Formation". Advanced Materials. 29 (35): 1701629. Bibcode:2017AdM....2901629S. doi:10.1002/adma.201701629. ISSN 0935-9648. PMID 28714191.
- ^ a b Chang, Chang; Lahti, Todd; Tanaka, Takuji; Nickerson, Michael T (2018-03-23). "Egg proteins: fractionation, bioactive peptides and allergenicity". Journal of the Science of Food and Agriculture. 98 (15): 5547–5558. Bibcode:2018JSFA...98.5547C. doi:10.1002/jsfa.9150. ISSN 0022-5142. PMID 29797412.
- ^ Chay Pak Ting, B.P.; Pouliot, Y.; Gauthier, S.F.; Mine, Y. (2013), "Fractionation of egg proteins and peptides for nutraceutical applications", Separation, Extraction and Concentration Processes in the Food, Beverage and Nutraceutical Industries, Elsevier, pp. 595–618, doi:10.1533/9780857090751.2.595, ISBN 978-1-84569-645-0, retrieved 2024-04-26
- ^ Yilmaz, Birsen; Ağagündüz, Duygu (2020-09-23). "Bioactivities of hen's egg yolk phosvitin and its functional phosphopeptides in food industry and health". Journal of Food Science. 85 (10): 2969–2976. doi:10.1111/1750-3841.15447. ISSN 0022-1147. PMID 32966601.
Further reading
[edit]- SI, Ishikawa; et al. (Aug 2007). "Egg yolk protein and egg yolk phosvitin inhibit calcium, magnesium, and iron absorptions in rats". Journal of Food Science. 72 (6): S412–S419. doi:10.1111/j.1750-3841.2007.00417.x. PMID 17995699.
- Mecham, Dale K.; Olcott, Harold S. (1949). "Phosvitin, the principal phosphoprotein of egg yolk". Journal of the American Chemical Society. 71 (11): 3670–3679. doi:10.1021/ja01179a028.
- Ko, K. Y.; et al. (2011). "A simple and efficient method for preparing partially purified phosvitin from egg yolk using ethanol and salts" (PDF). Poultry Science. 90 (5): 1096–1104. doi:10.3382/ps.2010-01138. PMID 21489960.
- Huopalahti, Rainer; et al. Bioactive Egg Compounds. Springer.
- Anton, Marc; Castellani, Oscar; Guérin-Dubiard, Catherine (2007). Phosvitin. Springer Berlin Heidelberg. pp. 17–24. doi:10.1007/978-3-540-37885-3_4. ISBN 9783540378839.
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