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The Potential of Some Plant-Derived Compounds in Inhibition of α-Amylase, Important for Diabetic Patients      
Yazarlar
Ahmed Menshaz
Prof. Dr. Ergin Murat ALTUNER Prof. Dr. Ergin Murat ALTUNER
Kastamonu Üniversitesi, Türkiye
Özet
α-Amylase is an enzyme, which hydrolyses starch into glucose. After consuming starch rich foods, as a result of the α-amylase activity, the glucose concentration in the blood increases drastically and cause hyperglycaemia. Thus, α-amylase inhibitors take account to decrease the α-amylase activity, which is important especially in diabetic patients to control the glucose concentration in the blood. Several compounds have been isolated and defined in microorganisms, plants, and animals, which can be used as a-amylase inhibitors. The aim of this study was to determine the α-amylase inhibitory activity of some plant derived secondary metabolites, namely phloridzin, naringenin, quercetin, umbelliferone, and cinnamic acid, and the results were compared against a positive control, acarbose. As a result, it was observed that quercetin and umbelliferone were effective α-amylase inhibitors, which present similar activity as acarbose. This result is extremely important for proposing some compounds, which could have a potential in diabetes management. On the other hand, phloridzin and cinnamic acid seem to act as good activators for a-amylase. Naringenin was also observed to act as an activator for a-amylase, but it is not as good as phloridzin and cinnamic acid. Further study should be conducted to determine the mechanism of inhibition and activation.
Anahtar Kelimeler
Cinnamic acid | Naringenin | Phloridzin | Quercetin | Umbelliferone | α-amylase inhibition
Makale Türü Özgün Makale
Makale Alt Türü SSCI, AHCI, SCI, SCI-Exp dergilerinde yayımlanan tam makale
Dergi Adı FRESENIUS ENVIRONMENTAL BULLETIN
Dergi ISSN 1018-4619
Dergi Tarandığı Indeksler SCI-Expanded
Makale Dili İngilizce
Basım Tarihi 01-2020
Cilt No 29
Sayı 9
Sayfalar 8642 / 8646
BM Sürdürülebilir Kalkınma Amaçları
Atıf Sayıları
WoS 1
Google Scholar 3

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