Research Article
Effects of Fe3+/Fe2+ on Glycation Reaction of
β-lactoglobulin
Issue:
Volume 15, Issue 3, June 2026
Pages:
93-103
Received:
19 April 2026
Accepted:
6 May 2026
Published:
8 May 2026
DOI:
10.11648/j.ijnfs.20261503.11
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Abstract: Iron ions (Fe2+ and Fe3+) are essential trace elements for the human body, and are often added to various foods, but their effects on protein glycation remain unclear. This study evaluated the differential influences of Fe2+ and Fe3+ on the glycation reaction of β-lactoglobulin (β-Lg)-D-ribose system in terms of glycation degree, protein conformation and the distribution of modification sites. Free amino group contents and HPLC HCD MS/MS analyses indicated that both Fe3+ and Fe2+ could catalyze the glycation process and increase the glycated sites. The system contain Fe2+ exhibited higher glycation degree and more glycation sites (8), and lesser glycation sites were identified in system contain Fe3+ (5) and system without ferric ions (2). Additional sites (L1, K14, K135) were facilitated glycation by Fe2+, and most glycation sites showed higher degree of substitution per peptide (DSP) values when with Fe2+. In comparison with Fe2+, Fe3+ caused more pronounced alterations on both secondary and tertiary protein structure, promoted the β-Lg unfolding, and changed the protein structure to a more unordered form. In conclusion, Fe2+ at a specified concentration was a better choice to promote glycation reaction while maintain the protein structure. This study provide a theoretical basis for protein glycation modification with iron ions at different valence states participated.
Abstract: Iron ions (Fe2+ and Fe3+) are essential trace elements for the human body, and are often added to various foods, but their effects on protein glycation remain unclear. This study evaluated the differential influences of Fe2+ and Fe3+ on the glycation reaction of β-lactoglobulin (β-Lg)-D-ribose system in terms of glycation degree, protein conformati...
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,
Qiannan Jiang
