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Animal Products
Asian-Australasian Journal of Animal Sciences 2009;22(4): 591-597.
DOI: https://doi.org/10.5713/ajas.2009.80363    Published online March 4, 2009.
Improvement of Functional Properties of Egg White Protein through Glycation and Phosphorylation by Dry-heating
Hirofumi Enomoto, Shiho Nagae, Yoko Hayashi, Can-Peng Li, Hisham R. Ibrahim, Yasushi Sugimoto, Takayoshi Aoki*
Correspondence:  Takayoshi Aoki,
Abstract
Egg white protein (EWP) was glycated with maltopentaose (MP) through the Maillard reaction and subsequently phosphorylated by 85??C dry-heating at pH 4.0 for 1 d in the presence of pyrophosphate. The functional properties of glycated, phosphorylated EWP were compared with those of native EWP and with EWP which was phosphorylated by dry-heating in the presence of pyrophosphate under the same conditions. The phosphorus content of EWP was increased to ~0.60% by phosphorylation, and to ~0.74% by glycation with MP and subsequent phosphorylation. The electrophoretic mobility of EWP increased through phosphorylation. The stability of EWP against heat-induced insolubility at pH 7.0 was considerably improved by phosphorylation alone and further by phosphorylation after glycation. The anti-ovalbumin antibody response was reduced significantly by glycation and phosphorylation, and further reduced by phosphorylation after glycation. The anti-ovomucoid antibody response was reduced significantly by glycation, phosphorylation and phosphorylation after glycation. The calcium phosphate-solubilizing ability of EWP was enhanced by both phosphorylation methods.
Keywords: Egg White Protein; Phosphorylation; Dry-heating; Maillard Reaction; Functional Property


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