Bioactive Peptides and Their Functional Properties in Food ...

Summary

Bioactive peptides are specific protein fragments released during enzymatic hydrolysis, fermentation or gastrointestinal digestion of food proteins. They exhibit a spectrum of health-promoting properties, including antihypertensive, antioxidant, antimicrobial and immunomodulatory activities, and contribute to technological functions such as emulsification, foaming and gelation. Sources range from dairy and meat to plant proteins in legumes, cereals and oilseeds. Advances in peptide profiling and structure–activity relationship analyses have clarified how sequence, length and amino-acid composition govern bioactivity and stability. The integration of sustainable protein sources and targeted release methods is driving innovation in functional foods and nutraceuticals, with implications for chronic disease prevention, clean-label formulations and food preservation.

Research from Nature Portfolio

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Research from all publishers

Recent work on plant-based yoghurts has shown that co-cultures of lactic acid bacteria applied to lupin–oat matrices produce low-molecular-weight peptides (<1 kDa) with potent angiotensin-converting enzyme (ACE) inhibitory activity. Nano-LC-MS/MS profiling revealed that mixed strains promoted diverse peptide release, with the greatest bioactivity in formulations containing Lactobacillus plantarum and Bifidobacterium sp.

A foundational investigation into the structure–activity relationships of antioxidant peptides derived from natural proteins has delineated key motifs—hydrophobic and aromatic residues—that enhance radical scavenging. Quantitative analyses have linked peptide length and conformation to efficacy, informing predictive models for novel antioxidant peptide design.

Studies of plant-derived ACE-inhibitory peptides have consolidated knowledge on production methods, including enzymatic hydrolysis and fermentation, and demonstrated how peptide chain length, sequence and gastrointestinal stability affect blood-pressure-lowering potential. Challenges such as bioavailability and in vivo validation have been identified, guiding future product development and clinical evaluation.

Bioactive Peptides and Their Functional Properties in Food Systems publication trend

The graph below shows the total number of articles in bioactive peptides and their functional properties in food systems across all publications each year (not limited to Nature Index journals).

Technical terms

Bioactive peptide: A short sequence of amino acids derived from food proteins that exerts a specific physiological effect beyond basic nutrition.

Enzymatic hydrolysis: The breakdown of proteins into peptides and amino acids through the action of proteases under controlled conditions.

Angiotensin-converting enzyme (ACE) inhibition: The capacity of certain peptides to reduce ACE activity, thereby modulating blood pressure via the renin-angiotensin system.

Structure–activity relationship: The correlation between a peptide’s molecular structure—sequence, length and conformation—and its observed biological activity.

Gastrointestinal bioavailability: The degree to which orally administered peptides survive digestion and are absorbed intact into the circulatory system.

References

1. The effect of probiotic strains on the proteolytic activity and peptide profiles of lupin oat-based yoghurt. Food Hydrocolloids (2024).
2. The Structure-Activity Relationship of the Antioxidant Peptides from Natural Proteins. Molecules (2016).
3. Towards the Improved Discovery and Design of Functional Peptides: Common Features of Diverse Classes Permit Generalized Prediction of Bioactivity. PLOS ONE (2012).
4. Bioactive Peptides. Foods (2017).
5. Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Plants. Nutrients (2017).

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