Two Novel β-Casein Iron-Chelating Peptides: Isolation, Identification, Prediction of Iron Binding Modes, and
Kaite Chen1, Feng Ma1, Linhui Lao1
1Guangdong Provincial Key Laboratory of Nutraceuticals and Functional Foods, College of Food Science, South China Agricultural University, Guangzhou, Guangdong Province, China.
Abstract:
In this study, β-casein was used to prepare iron-chelating peptides through the enzymatic hydrolysis. β-casein hydrolysates were purified and identified, and combined with molecular docking to screen high-activity iron-chelating peptides. Additionally, their iron binding modes and enhancement of intestinal iron absorption activities were investigated. The results indicated that 232 peptides were identified from high-activity M4 fractions, and two novel peptides, SpEESITRINKKIE (1706.77617 Da) and SpSpSpEESITRINKKIE (1800.87390 Da), exhibited the strongest iron chelation potential. These peptides bound to Fe2+ through metal-acceptor and charge--charge interactions, achieving Fe2+ chelation rates of 87.18 ± 0.89% and 91.15 ± 0.31%, respectively. In Caco-2 cell monolayers, the iron transport quantities of SpEESITRINKKIE and SpSpSpEESITRINKKIE within 30 min significantly (p < 0.05) increased by 79 ± 1% and 129 ± 2%, respectively, compared to the control group. These peptides demonstrated excellent enhancement of intestinal iron absorption activities. This study provides a theoretical basis for developing dietary iron supplements utilizing β-casein iron-chelating peptides.
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