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Purification of glycomacropeptide from non-dialyzable fraction of sweet whey by anion-exchange chromatography

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Biotechnology Techniques

Abstract

Glycomacropeptide (GMP) was purified from non-dialyzable fraction of sweet whey by anion-exchange chromatography on DEAE-Sephacel at two pHs 6.4 and 3.0. Chromatography at pH 3.0 (but not pH 6.4) gave a GMP fraction of high purity with its yield (1 g from every litre of whey) being approximately 100 times higher than that shown in the previous report. It was concluded that DEAE-Sephacel chromatography at pH 3.0 is a simple useful method to separate GMP from most whey proteins. It may be applicable to a large scale production of GMP.

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Authors and Affiliations

  1. Alberta Dairy Association Research Unit, c/o Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Alberta, T6G 2P5, Canada

    Takuo Nakano & Lech Ozimek

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  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 anion-exchange chromatography. Biotechnology Techniques 13, 739–742 (1999). https://doi.org/10.1023/A:1008957928446

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  • DOI: https://doi.org/10.1023/A:1008957928446

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