Abstract
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.
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