Simple rapid procedure for preparation of large quantities of ovalbumin.
A simple rapid procedure for preparation of large quantities of highly purified homogeneous ovalbumin from egg white by using an anion exchanger is described. It is based on the principle of frontal chromatography. The volume of "mucin-free" egg white loaded onto the column was determined in order to exceed resin capacity. Thus, competition between proteins for resin sites was created. Owing to its high negative charge density, ovalbumin drives other egg white proteins from the column progressively. Two hundred and fifty milliliters of Q-Sepharose FF gel eluted isocratically with 0. 5 M NaCl extracted 9.55 g of ovalbumin with a purity rate of 83%. A 6.75 g amount of ovalbumin, with a purity rate of 94%, was recovered with an isocratic elution program using 0.14 M NaCl. Purified ovalbumins were compared by electrophoresis and analytical chromatography with other ovalbumin preparations.
Croguennec
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T
UMR INRA-ENSA Physico-Chimie et Technologie des Ovoproduits CS 84215 65, Rue de St. Brieuc, 35042 Rennes Cedex, France.
Nau
F
F
Pezennec
S
S
Brule
G
G
D002852:Chromatography, Ion Exchange; D004529:Egg White / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D009077:Mucins / Q000737:chemistry; D010047:Ovalbumin / Q000302:isolation & purification*
D009077:Mucins; D010047:Ovalbumin