In this study, pumpkin seeds peptide was purified, characterized, and evaluated for their zinc-chelating capability, as well as in vitro bioaccessibility and transportation. Raw pumpkin seeds protein hydrolysate (PSPH) was produced by papain hydrolysis. The peptide fractions with the highest zinc-chelating abilities were purified using immobilized metal affinity chromatography (IMAC) followed by gel filtration chromatography (GF). Eight peptides were identified, two of which with the lowest molecular weights were synthesized (RPKHPLK and RPKHPLSHDL) for determining potential bioaccessibility and bioavailability. Our results showed that the gastrointestinal stability of RPKHPLK-Zn and RPKHPLSHDL-Zn was higher than that of inorganic zinc salts in the simulated gastrointestinal tract model. Furthermore, the influence of the peptide zinc chelates on zinc transport was explored in vitro using Caco-2 cell monolayer model. It was also shown that both RPKHPLK-Zn and RPKHPLSHDL-Zn could increase zinc transport rate and may be used to facilitate effective zinc absorption. The result of this study may provide important implications for developing plant protein foods with higher nutritional value. PRACTICAL APPLICATION: As a potential alternative protein source, pumpkin seeds may find promising applications in plant-based foods and drinks to meet the growing market for nonanimal foods. In this study, pumpkin seed protein peptides were prepared and purified, and the zinc-chelating peptides were identified and evaluated for the abilities to promote the uptake of zinc. This type of mineral peptide chelates could be incorporated into plant-based foods to increase mineral contents, which is significantly higher in foods originated from animals. The result of our study may provide important information for food industry to increase the nutritional value of plant-based foods.
Keywords: chelating; in vitro digestion; pumpkin seeds peptide; zinc.
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