Abstract
Abstract Angiotensin converting enzyme (ACE) plays a key role in regulating blood pressure and ACE inhibitors are first-line drugs for treating hypertension. Food protein-derived peptides with ACE inhibitory activity are natural and safe alternatives for both prevention and treatment of hypertension. The second most abundant whey protein, α-lactalbumin (ALA) was hydrolysed with proteases from Bromelia antiacantha Bertol., a native plant. Two new peptides with potent ACE-inhibitory activity: TTFHTSGY (IC50 = 142 μM) and GYDTQAIVQ (IC50 = 1.0 mM) were purified by affinity chromatography and sequences were determined by mass spectrometry. In silico analysis indicated that neither of these peptides was toxic (ToxinPred). Inhibition kinetic analysis showed that TTFHTSGY was a fully functional ACE competitive inhibitor, whereas GYDTQAIVQ caused only partial ACE inhibition. Our results indicate that cysteine peptidases from B. antiacantha hydrolyse ALA to produce novel ACE inhibitory peptides that could be useful even as functional food ingredients.
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