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Fractionation of Caseins by Anion‐exchange Chromatography Using Food‐grade Buffers
Author(s) -
Turhan K.N.,
Barbano D.M.,
Etzel M.R.
Publication year - 2003
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2003.tb12294.x
Subject(s) - chromatography , chemistry , casein , fractionation , dithiothreitol , elution , skimmed milk , ion exchange , ultrafiltration (renal) , ion chromatography , ion , food science , biochemistry , organic chemistry , enzyme
: Caseins prepared by microfiltration of bovine skim milk were fractionated using anion‐exchange chromatography. Laser densitometry of electrophoresis gels was shown to be sufficiently quantitative to perform accurate mass balance calculations detailing the fate of each casein fraction. L‐cysteine was successfully used as a reducing agent instead of traditional toxic agents, such as dithiothreitol or β‐mercaptoethanol, enabling development of the first food‐grade buffer system for casein fractionation. More salt was required for elution of the casein fractions having a greater charge: α s ‐casein > β‐casein > κ‐casein. Increasing flow rate decreased the extent of separation. Use of smaller beads was suggested as a method to maintain separation at increased flow rate.