Comparison of Different Electrophoretic Separations of Hen Egg White Proteins

Abstract

The hen egg white protein composition has not yet been fully defined. To improve the knowledge of this biological fluid, the most usual and recently developed electrophoretic methods have been used: SDS-PAGE, native-PAGE, isoelectric focusing (IEF), and 2-dimensional electrophoresis (2DE). Seven of the major known proteins were thus identified in at least one electrophoretic system. Isoforms of ovotransferrin, ovalbumin, and ovomucoid were visualized when pI was used for the separation. Two-dimensional electrophoresis allowed separation of a very large number of spots. In each of the four systems, some components were revealed but not identified, and unknown spots were particularly numerous with 2DE. With this technique, many spots corresponding to small acidic proteins were highlighted, among which was the Ch21 protein, whose presence in hen egg white was thus confirmed. This study thus constitutes, to our knowledge, the first proteomic investigation of hen egg white.

Single-step purification of ovalbumin from egg white using aqueous biphasic systems

“…Nevertheless, the high amount of salt used can lead to the proteins irreversible unfolding. Nowadays, proteins from egg white are typically separated by electrophoresis, ion-exchange chromatography, size exclusion liquid chromatography, ultrafiltration, adsorption, among others [11][12][13][14][15][16][17][18]. However, some of these methods currently employed are multi-stage and with high equipment and operating costs.…”

Structural and Physicochemical Characteristics of Novel Basic Proteins Isolated from Duck Egg White

“…1,2) Even though the amounts of both proteins in EW were sufficient to be detected, there is no report about the presence of dBPS 1 and dBPS 2 . [8][9][10] This may be due to the extremely low molecular masses of dBPS 1 and dBPS 2 . This group of small basic proteins, consisting of dBPS 1 , dBPS 2 , cygnin, meleagrin, and ''similar to meleagrin,'' showed close phylogenetic relationships to each other.…”

“…5,6) To date, many minor proteins have not been identified. [7][8][9][10] Among the referenced proteins in avian EW, most are acidic proteins, having pI < 7, while only two are identified as basic proteins, proteins that have pI > 7, lysozyme (pI ¼ 10:7) and avidin (pI ¼ 10). 1,2) Both proteins have been sequenced and are well characterized.…”

Study of short-wave ultraviolet treatments (UV-C) as a non-thermal preservation process for liquid egg products

“…In egg white, ovomucoid, ovotransferrin, and ovalbumin represent approximately 80% of the protein content (54, 13, and 11%, respectively) (Desert et al, 2001), showing highest intensities in the gels, especially ovalbumin at 45.0 kDa. In LEY, 13 bands were identified: apolipoprotein CII, apolipoprotein CII apovitellenin I, apovitellenin I, apovitellin 8, β-livetin, β-livetin, R-livetin/apovitellenin III, apovitellenin IIIa/ apovitellenin IV, apovitellin 5 + 6/ apovitellenin V, apovitellenin Vb, apovitellin 3 + 4 and apovitellenin Va, in accordance to Guilmineau, Krause and Kulozik (2005).…”