Hen egg white fractionation by ion-exchange chromatography

被引:100
|
作者
Guérin-Dubiard, C
Pasco, M
Hietanen, A
del Bosque, AQ
Nau, F
Croguennec, T
机构
[1] INRA, UMR 1253, F-35042 Rennes, France
[2] MTT Agrifood Res Finland, Jokioinen 31600, Finland
[3] CSIC, Inst Fermentaciones Ind, E-28006 Madrid, Spain
关键词
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;
D O I
10.1016/j.chroma.2005.06.083
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
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页码:58 / 67
页数:10
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