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Health Services Vocational School, Igdır University, Igdır, Turkey AbstractCaffeic acid phenethyl ester (CAPE) is an active component of honeybee propolis extracts. Carbonic anhydrases (CAs, EC 4.2.1.1) are widespread and intensively studied metalloenzymes present in higher vertebrates including humans as many diverse isoforms. Acetylcholinesterase (AChE) is responsible for acetyl choline (ACh) hydrolysis and plays a fundamental role in nerve impulse transmission by terminating the action of the ACh neurotransmitter at cholinergic synapses and neuromuscular junctions. Butyrylcholinesterase (BChE) is another enzyme abundantly present in the liver and released into blood in a soluble form. Lactoperoxidase (LPO) is an enzyme involved in fighting pathogenic microorganisms whereas glutathione S-transferases (GSTs) are dimeric proteins present both in prokaryotic and eukaryotic organisms and involved in cellular detoxification mechanisms. In the present study, the inhibition effect of CAPE on human carbonic anhydrase (hCA) isoforms I, II, IX, and XII, AChE, BChE, LPO, and GST was evaluated. CAPE inhibited these enzymes with K i s in the range between micromolar to picomolar. The best inhibitory effect was observed against AChE and BChE.

In this paper, synephrine and phenylephrine compounds showed excellent inhibitory effects against human carbonic anhydrase (hCA) isoforms I and II, α-amylase, α-glycosidase, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE). Synephrine and phenylephrine had K values of 199.02 ± 16.01 and 65.01 ± 5.00 μM against hCA I and 336.02 ± 74.01 and 92.04  ±  18.03 μM against hCA II, respectively. On the other hand, their K values were found to be 169.10  ±  80.03 and 88.03  ±  5.01 nM against AChE and 177.06  ±  6.01 and 78.03  ±  3.05 nM against BChE, respectively. α-Amylase and α-glycosidase enzymes were easily inhibited by these compounds. α-Glycosidase inhibitors, generally defined to as starch blockers, are anti-diabetic drugs that help to decrease post comestible blood glucose levels.

Ethanolic (EEC) and aqueous (WEC) extracts of cinnamon (Cinnamomum verum)were evaluated for their antioxidant profiles by eight distinguished bioanalytical antioxidant methods. Their inhibitory effects were tested against some enzymes including acetylcholinesterase, butyrylcholinesterase, α-glycosidase and αamylase, which linked to different diseases. Additionally, the antioxidant properties were determined and polyphenolic compositions of the both extracts were evaluated by LC-MS/MS analysis. According to the LC-MS/MS experiments, thirteen compounds were found in WEC and EEC. Also, p-hydroxybenzoic acid (321.1 mg/kg extract), p-coumaric acid (291.4 mg/kg extract), and pyrogallol (142.4 mg/kg extract) were found to be the most abundant ingredients in the WEC. On the other hand, pyrogallol (264.3 mg/kg extract), ferulic acid (224.7 mg/ kg extract) and p-coumaric acid (170.2 mg/kg extract) were found as the most plentiful chemicals in the EEC. For the estimation of the antioxidant capacities of the both extracts (WEC and EEC), DPPH· and ABTS •+ scavenging activities, as well as Fe 3+ -Fe 2+ , and Cu 2+ -Cu + reducing assays were studied. The IC 50 values of the WEC and EEC indicated that they were potent effective DPPH· (21. 25 and 15.71 μg/mL) and ABTS •+ (6.52 and 5.79 μg/mL) scavengers, as well as AChE (221.33 and 110.26 μg/mL), BChE (461.69 and 94.93 μg/mL), α-glycosidase (206.86 and 220.00 μg/mL) and α-amylase (189.86 and 200.86 μg/mL) inhibitors. As a conclusion, both EEC and WEC had rich phenolic contents and demonstrated effective anticholinergic, antidiabetic and antioxidant effects. ARTICLE HISTORY