Journal
JOURNAL OF CHROMATOGRAPHY A
Volume 1090, Issue 1-2, Pages 58-67Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.chroma.2005.06.083
Keywords
hen egg white fractionation; ion exchange chromatography; electrophoresis; reverse-phase chromatography; LC-MS-MS; ovalbumin; ovotransferrin; lysozyme; flavoprotein; ovalbumin gene X; ovalbumin gene Y; ovoglycoprotein; ovomucoid
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Major hen egg white proteins have been widely studied for their functional properties but these studies still are unable to explain, alone, all of the biological properties of hen egg white. Hence, it is still interesting to produce pure and non-altered proteins to improve our knowledge on the biological properties of hen egg white. Presently, identification and characterization of both bioactive peptides and minor proteins from hen egg white is essential work for progressing in the understanding of hen egg white biological properties. With this objective in mind, a new process for a complete mucin free hen egg white fractionation based on ion exchange chromatography is proposed. Mucin free egg white is fractionated into six different fractions. Four of them are high-recovery yield purified fractions of lysozyme, ovotransferrin, ovalbumin and flavoprotein. The two other fractions are enriched in recently detected minor proteins in hen egg white. (c) 2005 Elsevier B.V. All rights reserved.
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