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Improvement of Functional Properties of Egg White Protein through Glycation and Phosphorylation by Dry-heating
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 Title & Authors
Improvement of Functional Properties of Egg White Protein through Glycation and Phosphorylation by Dry-heating
Enomoto, Hirofumi; Nagae, Shiho; Hayashi, Yoko; Li, Can-Peng; Ibrahim, Hisham R.; Sugimoto, Yasushi; Aoki, Takayoshi;
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 Abstract
Egg white protein (EWP) was glycated with maltopentaose (MP) through the Maillard reaction and subsequently phosphorylated by 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;
 Language
English
 Cited by
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