Thermodynamics of hydrophobic interaction chromatography of acetyl amino acid methyl esters

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DOIResolve DOI: http://doi.org/10.1016/j.chroma.2007.09.031
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TypeArticle
Journal titleJournal of Chromatography A
Volume1177
Issue2
Pages243253; # of pages: 11
SubjectAcids; Adsorption; Amino Acids; analogs & derivatives; analysis; Biotechnology; chemistry; Chromatography; Chromatography,Liquid; Esters; Heat; Hydrogen Bonding; Hydrophobicity; methods; Models,Chemical; Polymers; Sepharose; Solubility; Thermodynamics; Hydrophobic interaction chromoatography; N-Acetyl amino acid methyl esters; bio; Temperature
AbstractThermodynamic analysis of hydrophobic interaction chromatography of amino acid methyl esters showed entropy-driven adsorption, consistent with solvophobic theory, except for phenyl ester on the Toyopearl resins. All esters adsorbed more strongly to the Toyopearl resins, including the polymethacrylate base matrix, than to Butyl Sepharose. Enthalpy changes were more favorable with the former, explaining the retention difference between Toyopearl Butyl and Butyl Sepharose. An enthalpy change versus heat capacity change plot showed Van derWaals interactions predominantly with the resin matrix. Literature data revealed the same effect for dansylamino acids, shown by isothermodynamic temperature analysis to adsorb more entropically than the esters.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada; NRC Biotechnology Research Institute
Peer reviewedNo
NRC number52722
NPARC number12401003
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Record identifier181b34cb-8fde-4b2a-a05c-796d146f53a7
Record created2009-10-26
Record modified2016-05-09
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