Partitioning of α-lactalbumin and β-lactoglobulin in aqueous two-phase systems of polyvinylpyrrolidone and potassium phosphate

J Chromatogr B Analyt Technol Biomed Life Sci. 2011 Apr 1;879(11-12):721-6. doi: 10.1016/j.jchromb.2011.02.007. Epub 2011 Feb 24.

Abstract

In the present study, the partitioning of α-lactalbumin, β-lactoglobulin, and cheese whey proteins in aqueous two-phase system of polyvinylpyrrolidone-potassium phosphate is investigated. The partitioning of proteins in this system depends on the polymer and salt weight percents in feed, temperature, and pH. The orthogonal central composite design is used to study the effects of different parameters on partitioning of α-lactalbumin and β-lactoglobulin. A second order model is proposed to determine the impact of these parameters. The results of the model show that the weight percent of the salt in feed has a large effect on the protein partitioning. The weight percent of polyvinylpyrrolidone in the feed increases the partitioning coefficients. By increasing the temperature, the viscosity of polyvinylpyrrolidone is reduced and the protein can easily be transferred from one phase to the other phase. The pH of the aqueous two phase system can alter the protein partitioning coefficient through the variation of the protein net charge.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chemical Fractionation / methods*
  • Hydrogen-Ion Concentration
  • Lactalbumin / isolation & purification*
  • Lactoglobulins / isolation & purification*
  • Milk Proteins / chemistry
  • Phosphates / chemistry*
  • Potassium Compounds / chemistry*
  • Povidone / chemistry*

Substances

  • Lactoglobulins
  • Milk Proteins
  • Phosphates
  • Potassium Compounds
  • Lactalbumin
  • potassium phosphate
  • Povidone