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A modified procedure for caseinophosphopeptide analysis
1Graduate Institute of Food Science and Technology, National Taiwan University, Taipei, Republic of China.
Abstract:
A modified procedure is established for analyzing caseinophosphopeptides. The sodium caseinate hydrolysate is first treated by immobilized metal ion affinity chromatography to enrich the phosphopeptides. Because of the formation of Fe(3+)-peptide complexes, ethylenediaminetetraacetic acid is added to the bound fraction eluted with the immobilized metal ion affinity chromatography to disintegrate the complexes. Thus, the subsequent high-performance liquid chromatographic analysis is facilitated. A stepwise gradient elution is also suggested to enhance the resolution of caseinophosphopeptides during high-performance liquid chromatographic analysis.