화학공학소재연구정보센터
Biotechnology Letters, Vol.22, No.5, 413-416, 2000
Purification of glycomacropeptide from non-dialyzable fraction of sweet whey by hydrophobic interaction chromatography on phenyl-agarose
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.