Search for antihypertensive peptides in hydrolysates of pork by-products using peptidomic approaches
https://doi.org/10.20914/2310-1202-2025-1-93-99
Abstract
Recently, food products with a functional focus that promote health have been in increased demand. Promising raw materials for such products may be meat by-products, for example, pork stomachs, rich in sources of biologically available protein. The aim of this study was to search and identify peptides for angiotensin-converting enzyme (ACE) inhibitory activity using in silico peptidomic approaches. The object of study was a protein identified in the UniProt database as P01284. By combining bioinformatics tools, the workflow required for screening ACE inhibitory peptides can be greatly simplified and the costs of searching for active peptides can be significantly reduced, increasing overall efficiency. It has been established that monopeptides L (Leu), F (Phe) and M (Met) are active fragments of known peptides that have the function of lowering blood pressure, which were previously found in proteins of fish, vegetable, and dairy products. VF (Val-Phe) is contained in 103 sequences, of which 29 contain the exact Val-Phe peptide. The exact VF (Val-Phe) peptide isolated from pork sarcoplasmic proteins was chosen as the prototype. Future research should include studies of anti-ACE activity in vivo and the search for new peptides, which will lead to the availability of more beneficial fortified products on the market. The integrated approach allowed to speed up and reduce the cost of identifying promising antihypertensive peptides. The presented methodology can be effectively applied to further search for bioactive compounds in animal raw materials. The obtained results confirm the potential of using pork by-products for the production of functional food ingredients. In the future, in vivo studies are planned to confirm the biological activity of the identified peptides and expand the range of nutraceuticals with proven action.
About the Authors
E. S. Razumovskaya
KGBU "Administration of Veterinary Medicine of the Altai Territory for the city of Barnaul"
Russian Federation
Russian Federation
Cand. Sci. (Vet.), leading veterinarian, st. Shevchenko, 158 Barnaul, 656043, Russia
I. S. Milentyeva
Kemerovo State University
Dr Sci. (Engin.), Associate Professor, Laboratory of Biotesting of Natural Nutraceuticals, Krasnaya St., 6, Kemerovo, 650000, Russia
References
1. World Health Organization (WHO). Hypertension. Available at: http://www.who.int/news-room/fact-sheets/detail/hypertension (accessed: 26.12.2024).
2. Mirzaei M., Mirdamadi S., Safavi M. Structural analysis of ACE-inhibitory peptide (VL9) derived from Kluyveromyces marxianus protein hydrolysate. J. Mol. Struct. 2020. vol. 1213. pp. 128199. doi: 10.1016/j.molstruc.2020.128199.
3. Gomes C. et al. Current genetic engineering strategies for the production of antihypertensive ACEI peptides. Biotechnology and Bioengineering. 2020. vol. 117. no. 8. pp. 2610–2628.
4. Aluko R.E. Food protein‐derived renin‐inhibitory peptides: in vitro and in vivo properties. J. Food Biochem. 2019. vol. 43. no. 1. e12648.
5. Xu Z. et al. Identification of post-digestion ACE inhibitory peptides from soybean protein isolate: production conditions and in silico molecular docking. Food Chem. 2021. vol. 345. pp. 128855. doi: j.foodchem.2020.128855.
6. Hajat C., Stein E. The global burden of multiple chronic conditions: A narrative review. Prev. Med. Rep. 2018. vol. 12. pp. 284–293. doi: 10.1016/j.pmedr.2018.10.008.
7. Abdelhedi O., Nasri M. Advances in marine antihypertensive peptides: production, structure-activity and bioavailability. Trends Food Sci. Technol. 2019. vol. 88. pp. 543–557. doi: 10.1016/j.tifs.2019.04.002.
8. Filiptsova G.G. The role of peptide hormones in regulation of plant growth, development and adaptation to environmental factors. Experimental Biology and Biotechnology. 2024. no. 2. pp. 4–23. (in Russian).
9. Daskaya-Dikmen C. et al. Angiotensin-I-Converting Enzyme (ACE) Inhibitory Peptides from Plants. Nutrients. 2017. vol. 9. no. 4. 316 p. doi: 10.3390/nu9040316.
10. Rezvankhah A. et al. Generation of bioactive peptides from lentil protein. J. Food Meas. Charact. 2021. vol. 15. pp. 5021–5035.
11. Ajeigbe O.F. et al. Food-drug interactions and anti-hypertensive mechanisms of food bioactive compounds // J. Food Biochem. 2021. vol. 45. no. 3. pp. e13317.
12. Bravo F.I. et al. Production of antihypertensive peptides from chicken by-products // Nutrients. 2023. vol. 15. no. 2. 457 p.
13. Lee S.Y., Hur S.J. ACE inhibitory peptides from beef proteins and their effect in hypertensive rat model // Biomed Pharmacother. 2019. vol. 116. pp. 109046.
14. Abachi S. et al. ACE-inhibitory peptides from fish // Mar. Drugs. 2019. vol. 17. no. 11. 613 p. doi: 0.3390/md17110613.
15. Lu Y, Wang Y, Huang D, Bian Z, Lu P, Fan D, Wang X. Inhibitory mechanism of ACE inhibitory peptides from black tea. J. Zhejiang Univ. Sci. B. 2021. vol. 22. no. 7. pp. 575–589. doi: 10.1631/jzus. B2000520.
16. Zhang P, Chang C, Liu HJ, Li B, Yan QJ, Jiang ZQ, et al. Identification of novel angiotensin I-converting enzyme (ACE) inhibitory peptides from wheat gluten hydrolysate by the protease of Pseudomonas aeruginosa. J Funct Foods. 2020. vol. 65. pp. 103751. 10.1016/j.jff.2019.103751
17. López-Fernández-Sobrino R, Torres-Fuentes C, Bravo FI, Muguerza B. Winery by-products as a valuable source for natural antihypertensive agents. Crit Rev Food Sci Nutr. 2023. vol. 63. no. 25. pp. 7708–7721. doi: 10.1080/10408398.2022.2049202.
18. Tikhonov S.L., Kolberg N.A., Tikhonova N.V., Lazarev V.A. The influence of peptides of animal origin on the total cellularity of the bone marrow and the myelogram of immunodeficient mice .Baltic Marine Forum: materials of the X International Baltic Marine Forum. 2022. vol. 4. pp. 165–173.
19. Voroshilin R.A., Prosekov A. Yu., Makhambetov E.M. Bioactive peptides from secondary raw materials of animal origin. Agrarian science in the conditions of modernization and digital development of the Russian agro-industrial complex: Collection of articles based on the materials of the International Scientific and Practical Conference. 2022. pp. 93–96.
20. Khodoreva O.G., Marchenko K.A., Gordynets S.A. Pork by-products: amino acid composition and protein balance. Food Industry: Science and Technology. 2022. no. 15(3). pp. 79–85.
21. Siegrist M, Hartmann C. Why alternative proteins will not disrupt the meat industry. Meat Sci. 2023. vol. 203. pp. 1–6.
22. Arihara K, Yokoyama I, Ohata M. Bioactivities generated from meat proteins by enzymatic hydrolysis and the Maillard reaction. Meat Sci. 2021. vol. 180. pp. 108561.
23. Zheng SL, Luo QB, Suo SK, Zhao YQ, Chi CF, Wang B. Preparation, Identification, Molecular Docking Study and Protective Function on HUVECs of Novel ACE Inhibitory Peptides from Protein Hydrolysate of Skipjack Tuna Muscle. Mar Drugs. Mar. Drugs. 2022. vol. 20. no. 3. pp. 176. doi: 10.3390/md20030176.
24. Liu WY, Zhang JT, Miyakawa T, Li GM, Gu RZ, Tanokura M. Antioxidant properties and inhibition of angiotensin-converting enzyme by highly active peptides from wheat gluten. Sci Rep. 2021. vol. 11. no. 1. pp.5206. doi: 10.1038/s41598–021–84820–7.
25. Pipaliya R, Basaiawmoit B, Sakure AA, Maurya R, Bishnoi M, Kondepudi KK, Singh BP, Paul S, Liu Z, Sarkar P, Patel A, Hati S. Peptidomics-based identification of antihypertensive and antidiabetic peptides from sheep milk fermented using Limosilactobacillus fermentum KGL4 MTCC 25515 with anti-inflammatory activity: in silico, in vitro, and molecular docking studies. Front. Chem. 2024. vol. 12. pp. 1389846. doi: 10.3389/fchem.2024.1389846.
26. Mahta Mirzaei, Saeed Mirdamadi, Maliheh Safavi Structural analysis of ACE-inhibitory peptide (VL-9) derived from Kluyveromyces marxianus protein hydrolysate // Journal of Molecular Structure. 2020. vol. 1213. pp. 128199. doi:10.1016/j.molstruc.2020.128199.
27.
Review
For citations:
Razumovskaya E.S., Milentyeva I.S. Search for antihypertensive peptides in hydrolysates of pork by-products using peptidomic approaches. Proceedings of the Voronezh State University of Engineering Technologies. 2025;87(1):93-99. (In Russ.) https://doi.org/10.20914/2310-1202-2025-1-93-99
Views:
38
Email this article 
Post a Comment 
