Integrated in silico and in vitro characterization of a novel anti-elastase peptide from Moringa oleifera

The lack of stable, plant-derived elastase inhibitors for inclusion in health-promoting formulations necessitates the discovery of bioactive agents from sustainable sources. This study investigated the production, stability, and peptide profile of elastase-inhibitory hydrolysates from Moringa oleifera seed proteins. Through a comparative enzymatic approach, Alcalase was identified as the most effective protease for generating bioactive hydrolysates. Response surface methodology was employed to optimize the bioprocess, identifying substrate and enzyme concentrations as the primary determinants of elastase-inhibitory activity. De novo sequencing identified the decapeptide NVRPNGSHFR, and subsequent in silico characterization and molecular docking suggested an inhibitory mechanism potentially driven by interaction with the elastase catalytic site, where the decapeptide is predicted to be stabilized by specific hydrogen-bonding networks. Validation using the synthetic decapeptide showed elastase-inhibitory activity with an IC50 of 2.55 mM. Furthermore, a cell-based model indicated dose-dependent anti-inflammatory activity of the optimized hydrolysate, which also exhibited high stability across pH 2–12 and temperatures up to 100 °C. These findings suggest NVRPNGSHFR as a promising lead bioactive agent and establish a robust protocol for the measurement and extraction of high-value functional food ingredients from climate-resilient crops.

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