Hamamelitannin's Antioxidant Effect and Its Inhibition Capability on ?-Glycosidase, Carbonic Anhydrase, Acetylcholinesterase, and Butyrylcholinesterase Enzymes
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Tarih
2024
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Mdpi
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
Hamamelitannin (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.
Açıklama
Anahtar Kelimeler
hamamelitannin, polyphenolic compound, antioxidant activity, acetylcholinesterase, carbonic anhydrase, butyrylcholinesterase, alpha-glycosidase
Kaynak
Processes
WoS Q Değeri
N/A
Scopus Q Değeri
Q2
Cilt
12
Sayı
11
