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

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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.

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Authors and Affiliations

  1. Alberta Dairy Association Research Unit, c/o Department of Agricultural, Food and Nutritional Science, Canada

    Takuo Nakano & Lech Ozimek

  2. University of Alberta, Edmonton, Alberta, T6G 2P5, Canada

    Takuo Nakano & Lech Ozimek

Authors
  1. Takuo Nakano
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  2. Lech Ozimek
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Nakano, T., Ozimek, L. Purification of glycomacropeptide from non-dialyzable fraction of sweet whey by hydrophobic interaction chromatography on phenyl-agarose. Biotechnology Letters 22, 413–416 (2000). https://doi.org/10.1023/A:1005649415447

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  • DOI: https://doi.org/10.1023/A:1005649415447

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