Effect of Conductivity, pH, and Elution Buffer Salinity on Glycomacropeptide Recovery from Whey Using Anion Exchange Chromatography |
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Authors: | Hatice N Tek Kamile N Turhan Mark R Etzel |
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Affiliation: | Authors Tek and Etzel are with Dept. of Food Science, 1605 Linden Drive, Univ. of Wisconsin, Madison, WI 53706.;Author Turhan is with Food Engineering Dept., Mersin Univ., Mersin, Turkey. Direct inquiries to author Etzel (E-mail: ). |
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Abstract: | ABSTRACT: The objective of this study was to investigate the effect of whey conductivity, pH, and the salt concentration of the elution buffer on glycomacropeptide recovery and its extent of contamination using anion exchange chromatography. Glycomacropeptide was isolated from Mozzarella whey. Samples were analyzed for glycomacropeptide and contaminating whey proteins. Mass balances and percent recoveries were calculated from these data. Glycomacropeptide recovery increased substantially with decreasing conductivity and increasing pH of the whey feed stream. Increasing the pH, but not increasing the conductivity, increased contamination of the glycomacropeptide by primarily beta-lactoglobulin. Salt concentration of at least 0.1 M was required for complete elution of bound glycomacropeptide. These data define conditions needed for glycomacropeptide recovery by a process chromatography system that uses food-grade buffers, operates at industrially relevant flow rates, and achieves up to 98% recovery. |
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Keywords: | ion exchange beta-lactoglobulin fractionation protein isolate |
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