Author:
Tran Khoa Nguyen,Vo Van Song Toan
Abstract
Phosvitin from chicken egg yolk, known as a phosphoglycoprotein, owns a very strong metal chelating property due to its polyanionic character. This study aimed to evaluate the factors affecting the purification process and suitable conditions to increase phosvitin’s purity. Phosvitin was separated from yolk granules by using 10% of NaCl solution in 0.05 M NaOH solution and heat treatment which removes lipoprotein from the extracted solution. The highest phosphorus content (58.14 mg) and phosphorus recovery rate (32.4%) were obtained at thermal treatment of 30℃ for 30 minutes. In addition, phosvitin was purified using anion-exchange chromatography (AEC) and gel-filtration chromatography (GFC). The fraction 1 (F1) obtained from AEC using UNO-Sphere Q at pH 8 had the recovery rate of phosvitin approximately 72.73%. Furthermore, fraction F1 was separated on GFC to obtain two main sub-fractions (F1 and F2). Sub-fraction F1 from gel filtration was composed mostly of β-phosvitin with a high recovery rate (81.93%) while F2 was dominant with α-phosvitin in a lower phosvitin recovery rate (16.89%). These findings will provide useful information for further researches on other properties of phosvitin so that it can be applied widely in human needs.
Reference18 articles.
1. Fractionation and characterization of hen's egg yolk phosvitin;Abe;Journal of Food Science,1982
2. Anton, M., Castellani, O., & Guérin-Dubiard, C. (2007). Phosvitin: Bioactive Egg Compounds. Springer Press. Europe, pp. 17-24.
3. Bertrand, C. P. T. (2012). Development of antioxidant peptide fractions from egg yolk protein using enzymatic hydrolysis and ultrafiltration membranes. Science of Food and Nutrition Department of Agriculture and Food Faculty, Laval university.
4. A rapid and sensitive method for the quantitation of Mirogram quantities of protein utilizing the principle of protein - dye binding;Bradford;Analytical Biochemistry 72(1-2),1976
5. Burgess, R. R. (2009). Protein precipitation techniques. In: Methods in Enzymology: Guide to protein purificaion. Academic Press. USA, pp. 331-342.