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Isolation of hen egg white lysozyme, ovotransferrin and ovalbumin, using a quaternary ammonium bound to a highly
M C Vachier1, M Piot, A C Awadé
1Laboratoire de Recherches et de Technologie Laitière, Institut National de la Recherche Agronomique, Rennes, France.
Abstract:
A single-step anion-exchange chromatographic separation of egg white proteins was carried out using a Q Sepharose Fast Flow column. The separation resulted in the isolation of two lysozyme peaks with purities of ca. 99 and 88%, one peak of ovotransferrin purified to ca. 75% and two ovalbumin peaks with purities of ca. 54 and 98%. Recoveries were estimated to be ca. 60, 100 and 83% for lysozyme, ovotransferrin and ovalbumin, respectively. The amino acid compositions of all collected peaks have also been determined. This confirmed the identity of some of the proteins contained in these peaks.