Bioactive Peptide Isolation and Characterization in Dairy Systems
Summary
Milk proteins, notably caseins and whey fractions, harbour latent bioactive sequences that can be liberated through controlled hydrolysis, fermentation or physical fractionation. Once released, these peptides exhibit a spectrum of health-promoting properties, including antihypertensive, antimicrobial, antioxidant and immunomodulatory activities. Isolation strategies encompass enzymatic hydrolysis using proteases or microbial cultures, followed by membrane techniques such as ultrafiltration and microfiltration to enrich target fractions. Chromatographic methods, including ion exchange and size-exclusion, permit fine-tuning of peptide purity, while emerging approaches such as supercritical fluid extraction offer solvent-free fractionation. Characterization relies on high-performance liquid chromatography, mass spectrometry and sequencing to define molecular weight, amino acid composition and post-translational modifications. Functional assays—ranging from angiotensin-converting enzyme inhibition to cell-based immunoassays—correlate structure with bioactivity. Advances in process design now enable valorisation of cheese and whey by-products, aligning with circular-economy goals and yielding ingredients for functional foods, nutraceuticals and tailored infant formulations. Collectively, the field is moving towards integrated biorefinery models that combine sustainable processing with robust analytical platforms to deliver high-value dairy-derived peptides.
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Bioactive Peptide Isolation and Characterization in Dairy Systems publication trend
The graph below shows the total number of articles in bioactive peptide isolation and characterization in dairy systems across all publications each year (not limited to Nature Index journals).
Technical terms
Caseinomacropeptide (CMP): A sialylated glycopeptide released from κ-casein during cheesemaking, valued for bioactivity and low phenylalanine content.
Ultrafiltration: A pressure-driven membrane process that separates molecules by size, commonly used to concentrate and fractionate peptides.
Ion exchange chromatography: A method exploiting charge interactions to separate peptides based on their net ionic charge under specific pH conditions.
Mass spectrometry: An analytical technique that determines peptide mass-to-charge ratios, enabling sequence identification and post-translational modification analysis.
Enzymatic hydrolysis: The use of proteolytic enzymes to cleave parent proteins into smaller bioactive peptide fragments under controlled conditions.
References
- The effect of whey source on heat-induced aggregation of casein and whey protein mixtures of relevance to infant nutritional product formulation. Journal of Dairy Science (2023).
- Effects of pH, stirring rate, reaction time and sequential ultrafiltration of whey protein solution on recovery and purification of glycomacropeptides. Journal of Dairy Research (2022).
- Use of batch anion exchange technique for separation of κ-casein glycomacropeptide from bovine whey fraction. Journal of Dairy Research (2022).
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