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Updated: Jun 27, 2026
Measurement of Tissue Non-Heme Iron Content using a Bathophenanthroline-Based Colorimetric Assay
Published on: January 31, 2022
Binding modes and in vitro digestion profiles of an iron-binding peptide (EEEWDRE) derived from fermented scallop
Xu Yan1, Ying Yue1, Bingrui Guo1
1SKL of Marine Food Processing & Safety Control, National Engineering Research Center of Seafood, Collaborative Innovation Center of Provincial and Ministerial Co-construction for Deep Processing, Collaborative Innovation Center of Seafood Deep Processing, School of Food Science and Technology, Dalian Polytechnic University, Dalian, Liaoning 116034, China.
Abstract:
Studies on the preparation of bioactive peptides by fermentation are rare, let alone the structural characterization of peptides. This study investigated the binding modes and digestion profiles of a novel heptapeptide (EEEWDRE) identified from fermented scallop skirts, which owned a excellent ferrous chelating rate of 92.44 ± 0.43 %. Specifically, the molecular docking, ITC and spectroscopy results of the heptapeptide‑iron complex (EEEWDRE-Fe) indicated that ferrous ions were chelated with EEEWDRE through "monodentate" and "bidentate" modes, each molecule of heptapeptide could bind three molecules of ferrous ions, and the carboxyl oxygen atom was the main binding site. Furthermore, EEEWDRE-Fe maintained a high ferrous chelating rate throughout the digestion process, consistently exceeding 80 %. The proportion of the "EEEW" sequence in EEEWDRE and EEEWDRE-Fe was 88.77 % and 90.21 %, respectively. "EEEW" was crucial in the formation of the EEEWDRE-Fe. Our findings provided novel insights into the unique properties of fermentation-derived peptides, highlighting their potential as iron supplements.
