Hamamelitannin's Antioxidant Effect and Its Inhibition Capability on ?-Glycosidase, Carbonic Anhydrase, Acetylcholinesterase, and Butyrylcholinesterase Enzymes

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dc.contributor.authorDurmaz, Lokman
dc.contributor.authorKaragecili, Hasan
dc.contributor.authorErturk, Adem
dc.contributor.authorOzden, Eda Mehtap
dc.contributor.authorTaslimi, Parham
dc.contributor.authorAlwasel, Saleh
dc.contributor.authorGulcin, Ilhami
dc.date.accessioned2024-12-24T19:33:44Z
dc.date.available2024-12-24T19:33:44Z
dc.date.issued2024
dc.departmentSiirt Üniversitesi
dc.description.abstractHamamelitannin (2 ',5-di-O-galloyl-hamamelose) bears two-gallate moieties in its structure, and is a natural phenolic product in the leaves and the bark of Hamamelis virginiana. The antioxidant capacity of hamamelitannin was evaluated by a range of methods, with the following findings: the ability to reduce potassium ferric cyanide; the scavenging of N,N-dimethyl-p-phenylenediamine dihydrochloride radical (DMPD center dot+); the scavenging of 2,2 '-azinobis-(3-ethylbenzothiazoline-6-sulphonate) radical (ABTS center dot+); the scavenging of 1,1-diphenyl-2-picrylhydrazyl radical (DPPH center dot); and the ability to reduce cupric ions (Cu2+). Additionally, reference antioxidants of alpha-Tocopherol, butylated hydroxyanisole (BHA), Trolox, and butylated hydroxytoluene (BHT) were used for comparison. For DPPH radical scavenging, hamamelitannin had an IC50 value of 19.31 mu g/mL, while the IC50 values for BHA, BHT, Trolox, and alpha-Tocopherol were 10.10, 25.95, 7.05, and 11.31 mu g/mL, respectively. The study found that hamamelitannin functioned similarly to BHA, alpha-tocopherol, and Trolox in terms of DPPH center dot scavenging, but better than BHT. Additionally, as a polyphenolic secondary metabolite, the hamamelitannin inhibition capability of several metabolic enzymes was demonstrated, including acetylcholinesterase (AChE), butyrylcholinesterase (BChE), carbonic anhydrase I (CA I), carbonic anhydrase II (CA II) and alpha-glycosidase. The Ki values of hamamelitannin exhibited 7.40, 1.99, 10.18, 18.26, and 25.79 nM toward AChE, BChE, hCA I, hCA II, and alpha-glycosidase, respectively.
dc.description.sponsorshipTUBA; King SaudUniversity, Saudi Arabia [RSP-2024/59]
dc.description.sponsorshiplhami Gulcin is a member Turkish Academy of Sciences (TUBA). He would liketo extend his sincere appreciation to the TUBA for their financial support. Saleh Alwasel would liketo extend his sincere appreciation to the Researchers Supporting Project (RSP-2024/59), King SaudUniversity, Saudi Arabia.
dc.identifier.doi10.3390/pr12112341
dc.identifier.issn2227-9717
dc.identifier.issue11
dc.identifier.scopus2-s2.0-85210299542
dc.identifier.scopusqualityQ2
dc.identifier.urihttps://doi.org/10.3390/pr12112341
dc.identifier.urihttps://hdl.handle.net/20.500.12604/8263
dc.identifier.volume12
dc.identifier.wosWOS:001365898900001
dc.identifier.wosqualityN/A
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherMdpi
dc.relation.ispartofProcesses
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/openAccess
dc.snmzKA_20241222
dc.subjecthamamelitannin
dc.subjectpolyphenolic compound
dc.subjectantioxidant activity
dc.subjectacetylcholinesterase
dc.subjectcarbonic anhydrase
dc.subjectbutyrylcholinesterase
dc.subjectalpha-glycosidase
dc.titleHamamelitannin's Antioxidant Effect and Its Inhibition Capability on ?-Glycosidase, Carbonic Anhydrase, Acetylcholinesterase, and Butyrylcholinesterase Enzymes
dc.typeArticle

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