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Updated: Feb 12, 2026

A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
Published on: October 1, 2009
Characterization and comparison of the structure and antioxidant activity of glycosylated whey peptides from two
Xinliu Zhang1, Hao Gao1, Chunyan Wang1
1Key Laboratory of Dairy Science (Northeast Agricultural University), Ministry of Education, Harbin 150030, PR China.
Abstract:
Glycosylated whey peptides (WPP-Gal A and WPP-Gal B) were formed from two pathways. WPP-Gal A showed higher browning intensity and fluorescence intensity than WPP-Gal B. Loss of amino groups and reducing sugar was heavier for WPP-Gal A than WPP-Gal B. Size exclusion chromatography revealed that WPP-Gal A and B had similar curves, but the molecular weight distribution of WPP-Gal B was more extensive than that of WPP-Gal A. Particle size was larger for WPP-Gal B than WPP-Gal A. Furthermore, WPP-Gal A showed greater antioxidant activity than WPP-Gal B. FT-IR analysis indicated that vibrations of several chemical bonds in amide I, II and III bands of WPP-Gal A were more obvious than those of WPP-Gal B. WPP-Gal A showed greater Caco-2 cell proliferation than WPP-Gal B. Therefore, WPP-Gal A showed more significant structural and characteristic changes, higher antioxidant activity and better proliferative activity than WPP-Gal B.
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