AbstractBovine κ-casein glycomacropeptide (GMP) found in cheese whey is a sialylated phosphorylated peptide which is thought to be a potential ingredient for functional food as well as dietetic food. This study was undertaken to determine whether high purity GMP can be isolated from soluble whey fraction (SWF) using column chromatography on food grade anion exchange resin and chitin as an adsorbent. Samples of commercially available anion exchange resin (resin A, resin B and resin C) and those of chitin (chitin A, chitin B and chitin C) were examined in this experiment. The GMP fraction obtained from each column was analyzed for amino acid composition which reflects the purity of the peptide. Major findings for commercial anion exchange resin were that: (1) the proportion of GMP monitored as sialic acid in total recovered sialic acid was similar among the three samples of resin accounting for average 78% of recovered sialic acid; (2) the GMP fraction from resin A or resin B contained undetectable level of contaminating amino acids including phenylalanine, histidine, arginine and tyrosine; (3) the GMP fraction from resin C contained small amounts (<1 mol%) of contaminating amino acids, arginine, phenylalanine and tyrosine; and (4) the GMP binding capacity expressed as mg/100 mg dry weight of resin was more than 2.5 times higher in resin C (average 22.9) than in resin A or resin B with no difference between resin A and resin B averaging 8.7. Results obtained for chitin A, chitin B and chitin C were in general similar to those found with resin A and resin B. Since chitin has a remarkable GMP binding capacity averaging 8.6 mg/100 mg dry weight of chitin, it may be a useful adsorbent for whey fractionation. Further research is needed to develop an efficient inexpensive method to purify GMP.
Separation of O-Phosphorylated Amino Acids and Peptides on Anion Exchange Resin.