Abhiram Arunkumar - Chromatographic purification and characterization of whey protein dextran glycation products

Document created by Abhiram Arunkumar on Aug 22, 2014
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  Publication Details (including relevant citation   information):

  T. Bund, S. Allelein, A. Arunkumar, J.A. Lucey, M.R. Etzel   (2012), J. Chrom. A., 1244, 98.


  A process for the food-grade preparative-scale production and   chromatographic purification of whey protein isolate   (WPI)–dextran glycates was developed in this work. The Maillard   reaction was used to produce the glycates in aqueous solution. A   5 mL cation exchange column and salt step gradients were utilized   to elute the glycated protein at low salt and unreacted protein   at high salt. The process was scaled-up 160-fold to an 800 mL   column. Glycated products were analyzed by SDS-PAGE, BCA protein   assay and glycoprotein carbohydrate estimation kit, MALDI-TOF and   static and dynamic light scattering. Glycated protein was   relatively pure, containing only traces of beta-lactoglobulin,   and it was heterogeneous due to oligo-glycation. It had a   molecular mass of 26–35 kDa by static light scattering, and 22–67   kDa by MALDI-TOF. Mono-glycated protein would have been 23.8 kDa   from beta-lactoglobulin (18.6 kDa) and dextran (5.2 kDa). This   work demonstrated the utility of cation exchange chromatography   for the large-scale purification of glycated proteins using   food-grade chemicals and procedures.

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