Zinc is an essential micronutrient that strongly influences human health and nutrition through its involvement in several biological processes. Zinc functions as structural and functional component of many transcription factors and enzymes that regulate cell growth, gene expression, and immune response, and its deficiency can lead to retarded growth and impaired immune functions. The physiological functions of zinc are dependent on its bioavailability in tissues, which in turn depends on intestinal absorption of dietary zinc. The presence of dietary fibre and phytates impedes intestinal zinc absorption, as they can form insoluble complexes with zinc, decreasing its bioavailability. Peptides derived from food proteins can enhance zinc absorption and bioavailability. Peptides that contain amino acid residues such as cysteine, histidine, serine, aspartate and glutamate can chelate divalent metals, including zinc, forming soluble metal coordinate complexes. The structure-function relationship of zinc-chelating peptides and the stability of the peptide-metal complexes to gastrointestinal digestion are critical to their relevance in human nutrition and health promotion.

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Enzymatic hydrolysis of whey proteins increased the reducing capacity and decreased reactive sulfhydryl (SH) content of the peptides. Hydrolysis yielded Maillard reaction products and the carbonyl compounds depleted SH by nucleophilic reaction.

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Rye secalin-derived cysteine-containing tripeptides and analogues inhibited ADAM17 activity via active site zinc coordination, hydrogen bonds and hydrophobic interactions.