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Purification of glycomacropeptide from dialyzed and non-dialyzed sweet whey by anion-exchange chromatography at different pH values

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Abstract

Glycomacropeptide (GMP) was purified from sweet whey dialyzed in water by anion-exchange chromatography on DEAE-Sephacel at pH 2.0–4.5. The optimum pH range was 2.5–4.0. The yield of purified GMP increased and its sialic acid concentration decreased with increasing pH value. The GMP had an apparent isoelectric point < 3.8. Dialysis of sweet whey was shown to be important to maximize the yield of GMP adsorbed to the anion-exchanger. Only highly sialylated GMP, accounting for approximately 55% of total sialic acid content, was adsorbed on the anion-exchanger from non-dialyzed sweet whey.

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Nakano, T., Ozimek, L. Purification of glycomacropeptide from dialyzed and non-dialyzed sweet whey by anion-exchange chromatography at different pH values. Biotechnology Letters 22, 1081–1086 (2000). https://doi.org/10.1023/A:1005618619167

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