Gelling Properties and Stability of Glycated Egg White Protein

Abstract

Abstract: The changes of texture, water-holding capacity and microstructure of native (EWP) and glycated (GWP) egg white proteins during storage were comparatively studied. The results showed that glycation resulted in an increase in the hardness, elasticity, cohesiveness, water-holding capacity of egg white proteins by 146%, 7%, 24% and 61% respectively. After storage at 4 ℃ for 180 days, both the gel hardness and cohesiveness of GWP decreased by 2%, and the springiness and water holding capacity of GWP increased by 1.3% and 0.6%, while the gel hardness of EWP decreased by 9%, and the springiness, cohesiveness and water-holding capacity of EWP increased by 0.6%, 3% and 5.2% respectively. A compact and more uniform network with constant stability in the course of storage was observed in GWP gels under SEM (×500 ), while gaps in EWP gel network were larger and the gel texture became looser with increasing storage time. These findings demonstrate that glycation is an effective method to improve the gelling properties and stability of EWP.

Key words: egg white proteins, glycation, gelling properties, gel structure

CLC Number:

S879.3

Wei Xu. Gelling Properties and Stability of Glycated Egg White Protein[J]. FOOD SCIENCE, 2012, 33(15): 15-18.

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