Hen egg white fractionation by ion-exchange chromatography

被引:103
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
收藏
页码:58 / 67
页数:10
相关论文
共 47 条
[1]  
ALDERTON G, 1946, J BIOL CHEM, V164, P1
[2]  
ANTONINI E, 1977, Patent No. 4029771
[3]   2-STEP CHROMATOGRAPHIC PROCEDURE FOR THE PURIFICATION OF HEN EGG-WHITE OVOMUCIN, LYSOZYME, OVOTRANSFERRIN AND OVALBUMIN AND CHARACTERIZATION OF PURIFIED PROTEINS [J].
AWADE, AC ;
MOREAU, S ;
MOLLE, D ;
BRULE, G ;
MAUBOIS, JL .
JOURNAL OF CHROMATOGRAPHY A, 1994, 677 (02) :279-288
[4]   THE MECHANICAL PROPERTIES OF THE THICK WHITE OF THE HENS EGG [J].
BROOKS, J ;
HALE, HP .
BIOCHIMICA ET BIOPHYSICA ACTA, 1959, 32 (01) :237-250
[5]   Simple rapid procedure for preparation of large quantities of ovalbumin [J].
Croguennec, T ;
Nau, F ;
Pezennec, S ;
Brule, G .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2000, 48 (10) :4883-4889
[6]   Two-step chromatographic procedure for the preparation of hen egg white ovotransferrin [J].
Croguennec, T ;
Nau, F ;
Pezennec, S ;
Piot, M ;
Brulé, G .
EUROPEAN FOOD RESEARCH AND TECHNOLOGY, 2001, 212 (03) :296-301
[7]   SINGLE-STEP PURIFICATION OF AVIDIN FROM EGG WHITE BY AFFINITY CHROMATOGRAPHY ON BIOCYTIN-SEPHAROSE COLUMNS [J].
CUATRECASAS, P ;
WILCHEK, M .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1968, 33 (02) :235-+
[8]   Comparison of different electrophoretic separations of hen egg white proteins [J].
Desert, C ;
Guérin-Dubiard, C ;
Nau, F ;
Jan, G ;
Val, F ;
Mallard, J .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2001, 49 (10) :4553-4561
[9]   Potentiation of the antihypertensive activity of orally administered ovokinin, a vasorelaxing peptide derived from ovalbumin, by emulsification in egg phosphatidylcholine [J].
Fujita, H ;
Sasaki, R ;
Yoshikawa, M .
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, 1995, 59 (12) :2344-2345
[10]   ISOLATION AND CHARACTERIZATION OF OVOKININ, A BRADYKININ B-1 AGONIST PEPTIDE DERIVED FROM OVALBUMIN [J].
FUJITA, H ;
USUI, H ;
KURAHASHI, K ;
YOSHIKAWA, M .
PEPTIDES, 1995, 16 (05) :785-790