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Hypertension is a worldwide health problem. It is the main cardiovascular risk factor and affects about 31% of the world's adult population. The drugs used to control hypertension may cause side effects; for this reason, there are many investigations focused on searching for alternatives to control or prevent this disease through diet. For example, many peptides have demonstrated antihypertensive effects. The insertion of bioactive peptides is a biotechnological implement used to improve the nutraceutical properties of proteins. This work reviews the current data on the insertion of antihypertensive peptides (AHPs) into food proteins, the systems used to produce the AHPs, the advantages and disadvantages between them, the parameters to produce them at major scales, and their potential applications in pharmacy and functional foods.

The insertion of peptides is a biotechnology tool widely used to improve the nutraceutical properties of proteins. Because the effect of these insertions in protein stability and function is difficult to predict, it should be determined experimentally. In this study, we created two variants of amarantin acidic subunit and analyzed them along with other four proteins reported previously. We measured their response against two destabilizing agents: temperature and urea. The six proteins presented the insertion of antihypertensive peptides (VYVYVYVY or RIPP) in the variable regions of the protein. We observed that their effect strongly depended on the site of the insertion. The insertion in the variable region I stabilized the protein both thermally and chemically, but it affected the inhibitory activity of the angiotensin-converting enzyme in vitro. In contrast, insertions in other three regions were severely destabilizing, producing molten globules. Our findings reveal that the insertion of bioactive peptides in variable regions of a protein can increase or decrease the protein's thermal and chemical stability and that these conformational changes may also alter its final activity.