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Separation of Native and Acylated Egg White Proteins with Gel Chromatography and DEAE‐Cellulose Ion Exchange
Author(s) -
PALLADINO D. K.,
BALL H. R.,
SWAISGOOD H. E.
Publication year - 1981
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1981.tb15346.x
Subject(s) - egg white , chemistry , ovalbumin , chromatography , lysozyme , succinic anhydride , ion chromatography , acylation , acetic anhydride , cellulose , biochemistry , organic chemistry , biology , catalysis , immune system , immunology
Chemical modification of egg white has been shown to improve its functional properties. In order to fully understand the changes in functionality it is necessary to separate the proteins and study their corresponding structural changes. This paper describes two chromatographic techniques applied to the separation of native and acylated egg white. A molified DEAE—cellulose ion exchange methodology was developed which reduced separation time and expense. It was found that increases in net charge introduced by acylation with succinic or acetic anhydride changed the ionic state of the proteins, limiting their separation by ion‐exchange chromatography. Using Sephacryl S‐200, a gel chiomatographic technique was developed which separated over 80% of the total succinylated egg white proteins; viz., ovomucin, ovalbumin, conalbumin, ovomacroglobulin, and lysozyme. Most proteins of native and acetylated egg white were separated with S‐200 chromatography, but required rechromatography of the ovalbumin‐conalbumin fractions for complete resolution.