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A novel nonapeptide DTDSEEEIR identified from Antarctic krill (Euphausia superba) iron-binding peptides was used in this study to analyze its iron-binding sites and structural changes after iron coordination. The enzymatic resistance and transport of DTDSEEEIR–iron during gastrointestinal digestion and absorption as well as the relationship between the DTDSEEEIR stability and the enhancement of iron absorption were further explored. Results revealed that iron ions spontaneously bound to the carboxyl, hydroxyl, and amino groups of the DTDSEEEIR peptide, which induced the folding of DTDSEEEIR to form a more orderly structure. The DTDSEEEIR peptide remained stable to a certain extent (79.60 ± 0.19%) after gastrointestinal digestion and the coordination of iron improved the digestive stability of the DTDSEEEIR peptide (93.89 ± 1.37%). Moreover, the stability of DTDSEEEIR across intestinal epithelium had a positive effect on iron absorption, which implied that DTDSEEEIR might carry iron ions through intestinal epithelial cells.

The effects of dynamic ultra-high pressure homogenization (UHPH) on the structure and functional properties of whey protein were investigated in this study. Whey protein solution of 10 mg/mL (1% w/w) was prepared and processed by a laboratory scale high pressure homogenizer with different pressures (25, 50, 100, 150, 200, and 250 MPa) at an initial temperature of 25 °C. Then, the solution samples were evaluated in terms of secondary structure, sulfhydryl and disulfide bond contents, surface hydrophobicity, average particle size, solubility, foaming capacity, emulsifying activity, and thermal properties. It was found that the secondary structure of whey protein changed with the dynamic UHPH treatment. The interchange reaction between the disulfide bond and the sulfhydryl group was promoted and the surface hydrophobicity significantly increased. The functional properties of the whey protein accordingly changed. Specifically, after dynamic UHPH treatment, the average particle size of the whey protein and emulsion decreased while the solubility, the foaming capability and the emulsification stability increased significantly. The results also revealed that with the dynamic UHPH at 150 MPa, the best improvement was observed in the whey protein functional properties. The whey protein solubility increased from 63.15 to 71.61% and the emulsification stability improved from 195 to 467 min.

A novel heptapeptide QEELISK derived from Antarctic krill was used to assemble a calcium delivery system, of which the calcium binding mechanism of QEELISK, in vitro digestion kinetics, and calcium absorption behaviors were explored. QEELISK with continuous Glu possessed higher calcium binding capacity than that of QELEISK and QAALISK. Ca2+ bound to the carboxyl oxygen of Glu at position 3 of the QEELISK peptide at a stoichiometric ratio of 1:1 through charge–charge interaction; the formed QEELISK–Ca showed superior stability. Moreover, QEELISK–Ca underwent disaggregation and self-assembly during in vitro digestion reflected by visualization of calcium ions and circular dichroism spectra. QELEISK was partially stable during gastrointestinal digestion, and calcium chelation improved the digestive stability of QELEISK. In addition, a significant enhancement of calcium absorption with QELEISK–Ca occurred in the duodenum and ileum when compared to CaCl2 absorption, which indicated that QEELISK might carry calcium ions through the gastrointestinal tract.

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