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Review
. 2024 May;44(3):533-550.
doi: 10.5851/kosfa.2024.e31. Epub 2024 May 1.

Analytical Methods and Effects of Bioactive Peptides Derived from Animal Products: A Mini-Review

Affiliations
Review

Analytical Methods and Effects of Bioactive Peptides Derived from Animal Products: A Mini-Review

Jae Won Jeong et al. Food Sci Anim Resour. 2024 May.

Abstract

Peptides with bioactive effects are being researched for various purposes. However, there is a lack of overall research on pork-derived peptides. In this study, we reviewed the process of obtaining bioactive peptides, available analytical methods, and the study of bioactive peptides derived from pork. Pepsin and trypsin, two representative protein digestive enzymes in the body, are hydrolyzed by other cofactors to produce peptides. Bicinchoninic acid assay, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, chromatography, and in vitro digestion simulation systems are utilized to analyze bioactive peptides for protein digestibility and molecular weight distribution. Pork-derived peptides mainly exhibit antioxidant and antihypertensive activities. The antioxidant activity of bioactive peptides increases the accessibility of amino acid residues by disrupting the three-dimensional structure of proteins, affecting free radical scavenging, reactive oxygen species inactivation, and metal ion chelating. In addition, the antihypertensive activity decreases angiotensin II production by inhibiting angiotensin converting enzyme and suppresses blood pressure by blocking the AT1 receptor. Pork-derived bioactive peptides, primarily obtained using papain and pepsin, exhibit significant antioxidant and antihypertensive activities, with most having low molecular weights below 1 kDa. This study may aid in the future development of bioactive peptides and serve as a valuable reference for pork-derived peptides.

Keywords: angiotensin converting enzyme inhibitory peptide; antioxidative peptide; bioactive peptide; pork.

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Conflict of interest statement

The authors declare no potential conflicts of interest.

Figures

Fig. 1.
Fig. 1.. The renin-angiotensin system.
ACE, angiotensin converting enzyme.
Fig. 2.
Fig. 2.. The analytical process for assessing the digestibility and bioactivities of myofibrillar proteins and peptide extracts from Jeju black pigs and three-way crossbred pigs (Landrace×Yorkshire×Duroc, LYD).
ICR, Institute of Cancer Research; BCA, bicinchoninic acid; HPLC, high-performance liquid chromatography; SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis; GPC, gel permeation chromatography; ACE, angiotensin converting enzyme; SOD, superoxide dismutase; CAT, catalase; POD, peroxidase.

References

    1. Acharya K. Simplified methods for microtiter based analysis of in vitro antioxidant activity. Asian J Pharm. 2017;11:S327–S335.
    1. Adibi SA, Mercer DW. Protein digestion in human intestine as reflected in luminal, mucosal, and plasma amino acid concentrations after meals. J Clin Invest. 1973;52:1586–1594. doi: 10.1172/JCI107335. - DOI - PMC - PubMed
    1. Aluko RE. Antihypertensive peptides from food proteins. Annu Rev Food Sci Technol. 2015;6:235–262. doi: 10.1146/annurev-food-022814-015520. - DOI - PubMed
    1. AOAC . Association of Official Analytical Chemists; Arlington, VA, USA: 2000. Official methods of analysis.
    1. Arihara K. Functional properties of bioactive peptides derived from meat proteins. In: Nollet NML, Toldrá F, editors. Advanced technologies for meat processing. CRC Press; Boca Raton, FL, USA: 2006. pp. 245–274. (ed) - DOI