Asian-Australasian Journal of Animal Sciences

Asian Australasian Association of Animal Production Societies (아세아태평양축산학회)
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Improvement of Functional Properties of Egg White Protein through Glycation and Phosphorylation by Dry-heating

  • Enomoto, Hirofumi (United Chair of Applied Resource Chemistry, Kagoshima University) ;
  • Nagae, Shiho (Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University) ;
  • Hayashi, Yoko (United Chair of Applied Resource Chemistry, Kagoshima University) ;
  • Li, Can-Peng (Department of Food and Pharmacy Engineering, Yunnan University) ;
  • Ibrahim, Hisham R. (Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University) ;
  • Sugimoto, Yasushi (United Chair of Applied Resource Chemistry, Kagoshima University) ;
  • Aoki, Takayoshi (Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University)
  • Received : 2008.06.30
  • Accepted : 2008.12.04
  • Published : 2009.04.01
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Abstract

Egg white protein (EWP) was glycated with maltopentaose (MP) through the Maillard reaction and subsequently phosphorylated by $85^{\circ}C$ 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

References

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