The functional properties of heat-induced egg white gels were investigated at five pH values. Textural characteristics were determined using the Instron Universal Machine. Hardness, elasticity, cohesiveness, chewiness, and fracturability were maximum at pH 11. Hunter L values were maximum at pH 5 and 7. Microstructure studied with electron microscopy was distinctly different at the five pH values. Alkaline gels showed a fine ordered network that might have contributed to excellent textural characteristics. Water-holding capacity (WHC) was high at alkaline pH, but decreased with addition of 2-mercaptoethanol, suggesting that disulfide bonds were important in egg white gels. Sodium dodecyl sulfate (SDS) improved WHC at pH 7 and 9. No significant correlation was observed between textural profiles and WHC.

The effects of the Maillard reaction on the functional properties of dried egg white (DEW) were investigated. Maillard-reacted DEW (M-DEW) was prepared by storing sugar-preserved DEW (SP-DEW) at 55 degrees C and 35% relative humidity for 0-12 days. The M-DEW developed an excellent gelling property, and hydrogen sulfide production from heat-induced M-DEW gels decreased. Surface sulfhydryl (SH) group content of M-DEW increased while total SH group and alpha-helix contents decreased with increasing heating time in the dry state. Breaking strength, breaking strain, water-holding capacity, and hydrogen sulfide of heat-induced M-DEW gels significantly correlated with surface and total SH group contents in M-DEW. SDS-PAGE revealed that M-DEW proteins were polymerized in which covalent bonds were involved. The present study demonstrated that the Maillard reaction partially unfolds and polymerizes proteins of SP-DEW and, consequently, improved gelling property of SP-DEW under certain controlled conditions.

Films plasticized with polyethylene glycol were cast from alkaline (pH 10.5, 11.0, or 11.5), aqueous egg white (EW) solutions with or without heating (40°C for 30 min). Prior to casting, concentration of surface sulfhydryl (SH) groups was determined and they increased (P < 0.05) (3.81-19.45 mM/g protein) with both pH and heating, presumably due to protein denaturation and cleavage of disulfide (S-S) bonds. Concentration of surface SH groups correlated (P < 0.05) with film tensile strength (r = 0.70), elongation at break (r = 0.86), and film total soluble matter (r = -0.94). Most likely, surface SH groups formed S-S bonds through air oxidation and/or sulfhydryl/disulfide interchange, thus contributing to EW film formation. SDS-PAGE patterns in presence or absence of 2-mercaptoethanol confirmed occurrence of S-S bonding in dried EW films.

The relationship between protein structure and aggregation, as well as heat-induced gelling properties, of seven dried egg white (DEW) products was investigated. Strong correlations were found between average molecular weight and hydrophobicity plus surface SH groups of DEW-soluble protein aggregate (SPA). This suggests that hydrophobic interactions and disulfide bond formation between protein molecules were involved in the aggregation. The average molecular weight of DEW products with alkaline pHs was relatively higher than those with neutral pHs and the same degree of protein unfolding, probably because of more disulfide bond formation between protein molecules. In addition, strong correlations were found between hydrophobicity, surface SH groups plus average molecular weight of DEW-SPA, and physical properties of the gels from DEW products. These data indicated that controlling the aggregation of DEW proteins in the dry state is crucial to controlling the gelling properties of DEW.

Polyethylene glycol-plasticized films were cast from alkaline (pH 11.25), heated (45 °C for 20 min), aqueous egg white (EW) solutions, with or without (10% or 20% w/w of EW) milkfat (two fractions), oleic acid, or egg yolk lysophospholipid (LPL). The lipids did not reduce (P > 0.05) film water vapor permeability. Oleic acid increased (P < 0.05) tensile strength and elongation, and surface sulfhydryl group (SH) concentrations in EW solutions. Oleic acid probably increased negative charges on EW proteins, unfolding protein chains, and exposing SH groups. LPL also slightly increased (P < 0.05) surface SH concentrations in non-heated mixtures. Electrophoretic patterns suggested oleic acid interactions with ovalbumin, ovotransferrin, and lysozyme. No lysinoalanine was in film-forming mixtures based on lysine measurements.