FOOD SCIENCE ›› 2013, Vol. 34 ›› Issue (7): 82-85.doi: 10.7506/spkx1002-6630-201307018

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Effect of Glycosylation on Gelling and Physicochemical Properties of Egg White Powder

CHI Yu-jie1,XU Wei1,HONG Yu-miao2   

  1. 1. College of Food Science, Northeast Agricultural University, Harbin 150030, China; 2. College of Pharmacy, China Pharmaceutical University, Nanjing 210009, China
  • Received:2012-01-05 Revised:2013-01-31 Online:2013-04-15 Published:2013-03-20
  • Contact: Yujie Chi E-mail:yjchi323@126.com

Abstract: Molecular characteristics of glycosylated egg white proteins (GEWP), including gelling properties, the number of sulfhydryl groups, hydrophobicity, molecular flexibility and Zeta potential were investigated. The results showed that gel strength and water holding capacity of glycosylated egg white proteins increased by 112.51% and 18.89%, respectively, when compared to control. After glycosylation, the protein molecules were partially unfolded, thus exposing the internal hydrophobic groups. At the same time, inter- and intra-protein disulfide bonds were formed, resulting in decreased total sulfhydryl content. In addition, glycosylation decreased the number of free ε-NH2 on the surface of egg white protein molecules, reducing the positive charges, and thus, the isoelectric point of egg white proteins.

Key words: egg white powder, glycosylation, gelling properties, hydrophobicity, molecular flexibility

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