Modification of functional properties of egg‐white proteins

Abstract

Egg-white proteins are extensively utilised as food ingredients due to their unique functional properties. Several attempts have been made in order to improve the functional properties of egg-white proteins and to identify the optimal formulations for unique food products. Experimental data proves that controlled denaturation of egg-white proteins can have a beneficial impact on various functional applications in the food industry such as emulsifying ability, heat stability, and gelation. This review describes the effect of heat-induced denaturation on protein structure and functionality. Studies on the impact of Maillard reaction, which aim to elucidate the structure-function relationship of egg-white proteins, are presented. A novel approach which could be the basis for the development of new methods aiming to improve the functional properties of egg-white proteins is also discussed.

Kinetics of hydrolysis of egg white protein by pepsin

“…On the other hand, there is a distinct relationship between the degree of hydrolysis (DH) and functional properties such as the distribution of molecular weights, surface hydrophobicity, solubility, foaming and emulsifying properties (Campbell et al 2003;Cigić & Zelenik-Blatnik 2004;Behnke et al 2006). However, the relationship between the DH and bioactivity of the peptides derived from egg white protein is not clear.…”

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

“…High disulfide bonds containing compact-shaped protein requires fairly high thermal energy to disrupt the sulfhydryl linkages and unfold the molecule. 28) Moreover, the high content of proline (three residues) in both proteins might be attributable to heat stability, as it was mentioned to stabilize protein conformation in previous studies. 32,33) A report of Zscherp 33) revealed a pronounced loss of thermal stability by tendamist, a small -sheet protein containing three prolines after it was mutated into proline-free tendamist.…”

“…Denaturation of globular proteins can lead to a great variety of properties, such as gelling, clotting, emulsifying, and the water binding property, each of which can affect food products. 28) EW protein begins to denature when heated to 60 C, according to CD spectra of native and denatured EW protein. 29) In spite of that, individual proteins of chicken EW have different denaturation temperatures: ovotransferrin (61 C), lysozyme (75 C), ovalbumin (84 C), ovomucoid (79 C), G2 globulin (92.5 C), and avidin (85 C).…”

Changes in activity during storage and characteristics of superoxide dismutase from hen eggs (Gallus gallus domesticus)

“…Mann & Mann identified 119 proteins in hen egg yolk by use of 1D electrophoresis, LC-MS/MS, and MS 3 . Out of this number, 86 fractions were described for the first time.…”

“…Eggs are often used as coagulants, reducing the surface tension, emulsifying and foaming agents, also fit the nutritional value and taste of food [3,4].…”