Co-extraction of egg white proteins using ion-exchange chromatography from ovomucin-removed egg whites.
Efficient isolation of egg white components is desired due to its potential uses. Existing methods mainly targeted on one specific protein; an attempt has been made in the study to co-extract all the valuable egg white components in a continuous process. Ovomucin was first isolated by our newly developed two-step method; the resultant supernatant obtained after ovomucin isolation was used as the starting material for ion-exchange chromatography. Anion-exchange chromatography of 100 mM supernatant yielded a flow-through fraction and three other fractions representing ovotransferrin, ovalbumin and flavoproteins. The flow-through fraction was further separated into ovoinhibitor, lysozyme, ovotransferrin and an unidentified fraction which represents 4% of total egg white proteins. Chromatographic separation of 500 mM supernatant resulted in fractions representing lysozyme, ovotransferrin and ovalbumin. This co-extraction protocol represents a global recovery of 71.0% proteins.
Omana
Dileep A
DA
Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Alberta, Canada T6G 2P5.
Wang
Jiapei
J
Wu
Jianping
J
D000818:Animals; D000838:Anions / Q000737:chemistry; D002412:Cations / Q000737:chemistry; D002645:Chickens; D002852:Chromatography, Ion Exchange / Q000379:methods*; D004527:Egg Proteins / Q000737:chemistry / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D010059:Ovomucin / Q000737:chemistry / Q000302:isolation & purification
D000838:Anions; D002412:Cations; D004527:Egg Proteins; D010059:Ovomucin