Abdulatef M Ahhmed Nesr¹*, Ceyda Ozcan², Hasan Yetim³, Mustafa Cam⁴, Shiro Takeda⁵, Ryoichi Sakata⁵ and Mustafa T Yilmaz⁶

¹Department of Nutritional Therapy, Graduate School of Medical Sciences, Libyan Academy for Graduate Studies, Janzour-Tripoli, Libya
²Graduate Institute of Natural and Applied Science, Erciyes University, Kayseri, Turkey
³Food Engineering Department, Faculty of Engineering and Natural Science, Istanbul S. Zaim University, Istanbul, Turkey
⁴Department of Food Engineering, Faculty of Engineering, Erciyes University, Kayseri, Turkey
⁵Department of Animal Science and Biotechnology, School of Veterinary Medicine, Azabu University, Sagamihara, Japan
⁶Industrial Engineering Department, Engineering Faculty, King Abdulaziz University, Jeddah, Saudi Arabia

*Corresponding Author: Abdulatef M Ahhmed Nesr, Department of Nutritional Therapy, Graduate School of Medical Sciences, Libyan Academy for Graduate Studies, Janzour-Tripoli, Libya.

Received: May 20, 2024; Published: June 16, 2024

Abstract

Hypertension is known to be a major disease that causes advanced and continuous high levels of blood pressure in the human circulation system. The initiative mechanism of action of hypertension starts with an angiotensin converting enzyme (ACE) that exists in two forms (endothelial and soluble in blood). Normally, the disease is treated by chemically prepared medication which may cause health complications. Despite that, the current article attempted to find alternatives to the chemically prepared medications including bioactive compounds (antihypertensive peptides) derived from food products. The aim of this research was to determine the antihypertensive activity of hybrid peptides from muscle proteins of fresh beef and pastirma (dry-cured muscles). The beef and pastirma were digested with pepsin and trypsin to generate miscellaneous but not specific bioactive peptides. The samples were subjected to in vitro analyses to evaluate their ACE inhibitory activity using a substrate (HHL) representing angiotensin. Effects of processing and dry-curing treatment, which normally causes a lysis action on the chemical structure of proteins in beef and pastirma were also investigated. As a result, the processing of beef into pastirma degrades the major proteins such as MHC (200kDa) and many enzymes including: β-galactosidase, Phosphorylase B, Lactate Dehyrogenase, Trypsinogene into small peptides. Hydrolysates in fresh beef and pastirma with protein concentration of 5.65 and 6.09mg/ml showed inhibition rates against ACE activity of 83 and 79%, respectively. The biological values (IC50) of antihypertensive activity were 0.68 and 0.78 mg/ml for fresh meat and pastirma, respectively. Proteins in fresh beef have remarkable ACE inhibitory activities, which makes it a potent model for sourcing bioactive peptides to treat hypertensive abnormalities. We suggest that miscellaneous peptides from fresh meat will provide nutraceutical compounds after digestion by intestinal proteases. Hybrid bioactive peptides may differ in potency and duration of action against ACE activity. However, data indicated that it is not necessary to process meat into pastirma to enhance its biological activities. These findings demonstrated the protective effect of bioactive peptides derived from beef demonstrate that they are of significant importance for therapeutic interventions of hypertension-related complications.

Keywords: Antihypertensive Activity; Bioactive Peptides; Pastirma; Protein Molecular Weight; Beef Proteins; ACE Inhibitory Activity

References

1. Hippauf F., et al. “Towards a continuous adsorption process for the enrichment of ACE-inhibiting peptides from food protein hydrolysates”. Carbon 107 (2016): 116-123.
2. WHO, Hypertension, key facts, risk factors and symptoms, the information (2023).
3. WHO, Noncommunicable disease: Risk factors, the information retrieved from the website in (2015).
4. Skeggs LJ., et al. “The preparation and function of the hypertension-converting enzyme”. Experimental journal. 3 (1956): 295-299.
5. Öztürk HI., et al. “Harvesting bioactive peptides from sustainable protein sources: Unveiling technological and functional properties through in silico analyses”. Food and Humanity 2 (2024): 100294.
6. Katayama K., et al. “Porcine skeletal muscle troponin is a good source of peptides with Angiotensin-I converting enzyme inhibitory activity and antihypertensive effects in spontaneously hypertensive rats”. Journal of Agricultural and Food Chemistry 56 (2008): 355-360.
7. Dhaval A., et al. “Potential Applications of Food Derived Bioactive Peptides in Management of Health.” International Journal of Peptide Research and Therapeutics22 (2016): 377-398.
8. Antony P., et al. “Bioactive Peptides as Potential Nutraceuticals for Diabetes Therapy: A Comprehensive Review”. International Journal of Molecular Science16 (2021): 9059.
9. Hu Y., et al. “Bioactive peptides in dry-cured ham: A comprehensive review of preparation methods, metabolic stability, safety, health benefits, and regulatory frameworks”. Food Research International 186 (2024):
10. Ahhmed MA. “Traditional cured meat-making process degrades the proteins of M. latissimus dorsi of bovine”. International Food Research Journal 21 (2014a): 139-148.
11. Ahhmed M, et al. “Meat therapy for hypertension: hybrid hydrolysate as ace inhibitory compounds”. In Proceeding of the 19^th International Conference of FFC-Functional and Medical Foods, Bioactive Compounds and Biomarkers, (Pp. 108-111). November 17-18^th, 2015, Kobe University, Kobe, Japan
12. Aksu IM., et al. “Some microbiological, chemical, and physical characteristics of pastirma marketed in Erzurum”. Turkish Journal of Veterinary Animal Sciences 25 (2001): 319-326.
13. Kaban G. “Changes in the composition of volatile compounds and in microbiological and physicochemical l parameters during pastirma processing”. Meat Science 82 (2009): 17-23.
14. Muguruma M., et al. “A combination of soybean and skimmed milk reduces osteoporosis in rats”. Journal of Functional Foods4 (2012): 810-818.
15. Ahhmed MA., et al. “Proteins degradation value in cured meat product made from Cutaneous-omo brachialis muscle of bovine”. European Food Research and Technology Journal 238 (2014b): 387-396.
16. Ahhmed MA., et al. “Changes in physicochemical properties of proteins in Kayserian Pastirma made from the M. semimembranosus muscle of cows during traditional processing”. Food Science and Human Wellness1 (2013): 46-55.
17. Nesr AA., et al. “Nutritional, Physicochemical and Organoleptic Properties of Cookies Enriched with Green Lentil Dietary Flour Proposed for Children”. EC Nutrition5 (2024): 01-17.
18. Ahhmed MA., et al. “Solubility, Stability and Blood Pressure Lowering-Properties of Fresh and Cured Beef Proteins”. Acta Scientific Nutritional Health7 (2019): 16-27.
19. Cushman DW., et al. “Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung”. Biochemistry and Pharmacological 20 (1971): 16371648.
20. Muguruma M., et al. “Identification of pro-drug type ACE inhibitory peptide sourced from porcine myosin B: Evaluation of its antihypertensive effects in vivo”. Food Chemistry 114 (2009): 516-522.
21. Lan X., et al. “Rapid purification and characterization of angiotensin converting enzyme inhibitory peptides from lizardfish protein hydrolysates with magnetic affinity separation”. Food Chemistry 182 (2015): 136-142.
22. Ahhmed MA., et al. “Utilization of fermented soybeans paste as flavoring lamination for Turkish dry-cured meat”. Meat Science127 (2017): 35-44.
23. Kawahara S., et al. “Inconsistency in the improvements of gel strength in chicken and pork sausages induced by microbial transglutaminase”. Asian-Australian Journal of Animal Sciences 20 (2007): 1285-1291.
24. Ahhmed MA., et al. “Effect of microbial transglutaminase on the natural actomyosin cross-linking in chicken and beef”. Meat Science 82 (2009a): 170-178.
25. Ahhmed MA., et al. “Impact of transglutaminase on the textural, physicochemical, and structural properties of chicken skeletal, smooth, and cardiac muscles”. Meat Science 83 (2009b): 759-767.
26. Erwanto Y., et al. “Effect of existence of exogenous protein on physicochemical properties of heat- and transglutaminase-induced bovine collagen-peptide gel”. Journal of Food Science 70 (2005): E505- E509.
27. Takeda S., et al. “Reducing Effects of Whey Protein Hydrolysate on Coloration of Cured Sausages”. Foods 1 (2024): 13.
28. Ogata M., et al. “Effects of Inherent Lactic Acid Bacteria on Inhibition of Angiotensin I-Converting Enzyme and Antioxidant Activities in Dry-Cured Meat Products”.  Foods14 (2022): 2123.
29. Ahhmed MA., et al. “A review of meat protein hydrolysates and hypertension”. Meat Science, 86 (2010): 110-118.
30. Mora L., et al. “ACEI-Inhibitory Peptides Naturally Generated in Meat and Meat Products and Their Health Relevance.” Nutrients 10 (2018): 1259.
31. Nakade K., et al. “Identification of an antihypertensive peptide derived from chicken bone extract”. Animal Science Journal 79 (2008): 710-715.
32. Takeda S., et al. “Isolation, Evaluation, and Identification of Angiotensin I-Converting Enzyme Inhibitory Peptides from Game Meat”. Foods 9 (2020): 1168.
33. Kulczynski B., et al. “Characteristics of Selected Antioxidative and Bioactive Compounds in Meat and Animal Origin Products”. Antioxidants 8 (2018): 335.
34. Chourasia R., et al. “Bioactive peptides in fermented foods and their application: a critical review”. Systems Microbiology and Biomanufacturing1 (2023): 10.
35. Ahhmed MA. “Roles of Genetics and Age in Diet Patterns”. EC Nutrition2 (2024): 01-03.
36. Li-Chan EC. “Bioactive peptides and protein hydrolysates: research trends and challenges for application as nutraceuticals and functional food ingredients”. Current Opinion in Food Science 1 (2015): 28-37.
37. Wang L., et al. “Therapeutic peptides: Current applications and future directions”. Signal Transduction and Targeted Therapy 1 (2022): 48.
38. Chai KF., et al. “Bioactive peptides from food fermentation: A comprehensive review of their sources, bioactivities, applications, and future development”. Comprehensive Reviews in Food Science and Food Safety6 (2020): 3825-3885.
39. Sardari RR., et al. “HPAEC-PAD analysis for determination of the amino acid profiles in protein fractions from oat flour combined with correction of amino acid loss during hydrolysis”. Journal of Cereal Science, 109 (2023): 103589.
40. Koh J., et al. “Top-down glycopeptidomics reveals intact glycomacropeptide is digested to a wide array of peptides in human jejunum”. Journal of Nutrition2 (2022): 429-438.
41. Li G., et al. “Angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects”. Nutritional Research 24 (2004): 469-486.
42. Takeda , et al. “Investigation of lactic acid bacterial strains for meat fermentation and the product’s antioxidant and angiotensin-I-converting-enzyme inhibitory activities”. Animal Science Journal 88 (2017): 507-516.
43. Takeda S., et al. “Isolation, Evaluation, and Identification of Angiotensin I-Converting Enzyme Inhibitory Peptides from Game Meat”. Foods9 (2020): 1168.
44. Abril B., et al. “Role of Enzymatic Reactions in Meat Processing and Use of Emerging Technologies for Process Intensification”. Foods12 (2023):1940.
45. Takeda S. et al. “Reducing Effects of Whey Protein Hydrolysate on Coloration of Cured Sausage”s. Foods 13 (2024): 13.
46. Awad , et al. “Thymus capitatus and Micromeria fruticusa foster the physicochemical and bioactive properties in beef products”. Fleischwirtschaft International 10 (2021): 90-97.

Citation

Citation: Abdulatef M Ahhmed Nesr., et al. “Lysis of Proteins Derived from Fresh Beef and Pastirma Generates Miscellaneous Peptides having Angiotensin Converting Enzyme Inhibitory Activity". Acta Scientific Nutritional Health 8.7 (2024): 33-42.

Copyright

Copyright: © 2024 Abdulatef M Ahhmed Nesr., et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.