Abstract
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 5mL 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 800mL 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 26–35kDa by static light scattering, and 22–67kDa by MALDI-TOF. Mono-glycated protein would have been 23.8kDa from beta-lactoglobulin (18.6kDa) and dextran (5.2kDa). 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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