Yeast-Fermented Wheat Produces Peptides That Lower Blood Pressure as Effectively as a Common Drug in Rats

Fermenting wheat with the yeast Candida phyllophila J14-4 increased angiotensin-converting enzyme (ACE) inhibition activity by 46.05%. Peptide components under 3 kDa in the fermented wheat showed strong ACE-inhibitory activity, with the most potent peptide reaching 93.23% inhibition. In spontaneously hypertensive rats, the antihypertensive effect of the fermented wheat was comparable to captopril, a standard prescription ACE inhibitor drug.

Researchers fermented wheat wort with Candida phyllophila J14-4 and measured ACE inhibition activity in vitro. The antihypertensive effect was tested in vivo using spontaneously hypertensive rats (SHR), with captopril as a positive control. Volatile compounds were characterized using GC-IMS, and peptide fractions were separated by molecular weight to identify the most active ACE-inhibitory components.

With hypertension affecting over 25% of adults globally, finding food-derived alternatives or complements to pharmaceutical ACE inhibitors is of great interest. This study shows that a simple fermentation process can generate bioactive peptides from wheat that rival a prescription drug's blood pressure-lowering effect in animal models — pointing toward functional foods as a hypertension management tool.

Food-derived bioactive peptides are an expanding area of research at the intersection of nutrition and pharmacology. ACE-inhibitory peptides have been found in milk, fish, soy, and now fermented wheat. This study adds a new fermentation approach that could lead to functional foods or nutraceuticals for blood pressure management, potentially reducing dependence on pharmaceutical ACE inhibitors.

This is an animal study in spontaneously hypertensive rats, which may not predict blood pressure effects in humans. The fermented wheat product is not standardized for clinical use. The specific peptide sequences responsible for ACE inhibition were not fully identified. Bioavailability of the peptides after oral consumption in humans is unknown.