Lysis of Proteins Derived from Fresh Beef and Pastirma Generates Miscellaneous Peptides having Angiotensin Converting Enzyme Inhibitory Activity

dc.contributor.authorNesr, Abdulatef M Ahhmed
dc.contributor.authorÖzcan, Ceydan
dc.contributor.authorYetim, Hasan
dc.contributor.authorYetim, Hasan
dc.date.accessioned2025-08-22T11:20:23Z
dc.date.available2025-08-22T11:20:23Z
dc.date.issued2024en_US
dc.departmentMühendislik ve Doğa Bilimleri Fakültesien_US
dc.description.abstractHypertension 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, respec tively. 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 froen_US
dc.identifier.citationAbdulatef 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.en_US
dc.identifier.doi10.31080/ASNH.2024.08.1392
dc.identifier.endpage42en_US
dc.identifier.issn2582-1423
dc.identifier.issue7en_US
dc.identifier.orcid0000-0002-5388-5856en_US
dc.identifier.startpage33en_US
dc.identifier.urihttps://doi.org/DOI: 10.31080/asnh.2024.08.1392
dc.identifier.urihttps://hdl.handle.net/20.500.12436/7950
dc.identifier.volume8en_US
dc.institutionauthorYetim, Hasan
dc.language.isoen
dc.publisherActa Scientific Inc.en_US
dc.relation.ispartofActa Scientific Nutritional Healthen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectAntihypertensive Activityen_US
dc.subjectBioactive Peptidesen_US
dc.subjectPastirmaen_US
dc.subjectProtein Molecular Weighten_US
dc.subjectBeef Proteinsen_US
dc.subjectACE Inhibitory Activityen_US
dc.titleLysis of Proteins Derived from Fresh Beef and Pastirma Generates Miscellaneous Peptides having Angiotensin Converting Enzyme Inhibitory Activityen_US
dc.typeArticle
dspace.entity.typePublication
relation.isAuthorOfPublication3a17fe61-3246-4bb0-aa49-7f8be806f490
relation.isAuthorOfPublication.latestForDiscovery3a17fe61-3246-4bb0-aa49-7f8be806f490

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