Partitioning behavior of amino acids in aqueous two-phase systems with recyclable volatile salts

Mos Van Berlo, Marcel Ottens, Karel Ch A.M. Luyben, Luuk A.M. Van Der Wielen

Research output: Contribution to journalArticlepeer-review

Abstract

As part of an ongoing research effort on aqueous two-phase systems (ATPSs) with volatile salts, this work describes the partitioning behavior of a series of amino acids, namely L-serine, glycine, L-alanine, L-valine, L- methionine, L-isoleucine, and L-phenylalanine, in these systems. The results show that amino acids partition in a similar way in polymer-volatile salt ATPSs and in traditional polymer-salt ATPSs. Increasing amino acid hydrophobicities lead to increasing partition coefficients. Moreover, the common linear relationship between the logarithm of the partition coefficient and the tie line length is observed here as well. Furthermore, the relation between relative partition coefficients and relative hydrophobicities of amino acids in the extraction systems investigated in this work is comparable to that in other extraction systems. (C) 2000 Elsevier Science B.V.

Original languageEnglish
Pages (from-to)317-325
Number of pages9
JournalJournal of Chromatography B: Biomedical Sciences and Applications
Volume743
Issue number1-2
DOIs
Publication statusPublished - 23 Jun 2000
Externally publishedYes

Keywords

  • Amino acids
  • Aqueous two-phase systems
  • Partitioning
  • Volatile salts

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