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Corresponding Author(s)

陈树兴(1965—),男,河南科技大学教授,博士。E-mail:chenshuxing1@163.com

Abstract

[Objective] To improve the functional characteristics of egg white protein (EWP) by tagatose glycosylation. [Methods] Firstly, the differences in antioxidant activity, emulsifying property, emulsion stability, foaming ability, and foaming stability are compared among glycosylated EWP (G-EWP), heat-treated EWP (H-EWP), and EWP. Then, the mechanism underlying the structural changes of G-EWP is investigated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Fourier transform infrared spectroscopy, circular dichroism, scanning electron microscopy, and particle size analysis. [Results] Compared with EWP and H-EWP, G-EWP exhibits significantly improved antioxidant activity, emulsifying property, emulsion stability, foaming ability, and foaming stability (P<0.05). After glycosylation, the molecular weight increases. Tagatose is covalently grafted to egg white protein, with the content of α-helix, β-sheet, and β-turn changing and the morphology changing from spherical to large block-like complexes. The average particle size decreases from 153.53 nm to 129.33 nm (P<0.05), and the zeta potential value decreases from-22.68 mV to-31.83 mV (P<0.05). [Conclusion] Tagatose glycosylation can significantly improve the functional characteristics of EWP.

Publication Date

10-28-2025

First Page

8

Last Page

14

DOI

10.13652/j.spjx.1003.5788.2025.80324

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