Purification of glycomacropeptide from non-dialyzable fraction of sweet whey by hydrophobic interaction chromatography on phenyl-agarose

Author: Nakano T.  

Publisher: Springer Publishing Company

ISSN: 0141-5492

Source: Biotechnology Letters, Vol.22, Iss.5, 2000-03, pp. : 413-416

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Abstract

Non-dialyzable fraction of sweet whey was chromatographed on a column of phenyl-agarose equilibrated with 0.01 M sodium phosphate buffer, pH 6.8 containing 5 M NaCl. Most whey proteins were adsorbed on the column, while the glycomacropeptide (GMP) was not. Amino acid analysis of the GMP fraction showed presence of traces (each < 1="" residue/peptide)="" of="" arginine,="" histidine="" and="" phenylalanine="" which="" are="" not="" found="" in="" gmp.="" the="" estimated="" yield="" of="" gmp="" fraction="" was="" approximately="" 1.6 g l^−1="" of="" sweet="" whey.="">