Blood Pressure-Lowering Peptides Identified from Lupin Protein Using Ultrasound and Computer Modeling

Lupin protein isolate was pre-treated with ultrasound and then hydrolyzed using two different enzymes (alcalase and flavourzyme). The resulting hydrolysates were fractionated by molecular weight (1, 5, and 10 kDa) using membrane ultrafiltration. ACE-inhibitory activity was measured in vitro. Molecular docking simulations were used to predict which specific peptide sequences in the hydrolysates were most likely responsible for ACE inhibition.

High blood pressure affects over a billion people worldwide, and there is growing interest in food-derived bioactive peptides as natural alternatives or supplements to pharmaceutical ACE inhibitors. Identifying specific peptide sequences from lupin protein could lead to functional foods or nutraceuticals for blood pressure management, adding value to an underutilized plant protein source.

Food-derived bioactive peptides are an expanding area of research linking nutrition and health. This study adds lupin to the growing list of plant proteins that yield ACE-inhibitory peptides, alongside well-studied sources like milk, soy, and fish. The use of ultrasound pre-treatment represents an emerging approach to enhancing bioactive peptide release from plant proteins.

This study was entirely in vitro and computational — no animal or human testing was performed. Molecular docking predicts binding potential but does not confirm biological activity. The identified peptides have not been synthesized and tested individually. Whether these peptides survive digestion and reach the bloodstream in active form is unknown. The IC50 values are relatively high compared to pharmaceutical ACE inhibitors.