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 sho...

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Bibliographic Details
Published in:Biotechnology letters 2000-03, Vol.22 (5), p.413-416
Main Authors: NAKANO, T, OZIMEK, L
Format: Article
Language:English
Subjects:
Amino acids
Biological and medical sciences
Biotechnology
Food industries
Fundamental and applied biological sciences. Psychology
glycomacropeptide
Methods. Procedures. Technologies
Others
phenyl-agarose
Proteins
Research and development. New food products, dietetic foods and beverages
Sodium chloride
Various methods and equipments
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Summary: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^sup -1^ of sweet whey.[PUBLICATION ABSTRACT]
ISSN:0141-5492
1573-6776
DOI:10.1023/A:1005649415447