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- MakaleYalnız künye2023Scopus SJRQ2Design, synthesis, antioxidant and anticholinesterase activities of novel isonicotinic hydrazide-hydrazone derivatives
Aslanhan, Özlem; Kalay, Erbay; Tokalı, Feyzi Sinan; Can, Zehra; Şahin, Engin
The design and synthesis of hydrazone derivatives are increasing in popularity day by day due to the significant biological activities of this scaffold. In the present study, twelve novel isonicotinic hydrazide-hydrazone analogues were synthesized by the condensation reaction of isonicotinic hydrazide with benzaldehyde possessing sulfonate moiety. The structures of the novel compounds have been characterized in detail using spectroscopic techniques. All compounds have shown inhibitory effects against the AChE enzyme at rates ranging from 21.00 to 59.48%. Among them, compound 5 has exhibited the best inhibitory effect of 59.48% against AChE at a concentration of 0.1 mM. Furthermore, to determine how effective the novel compounds are as antioxidants, FRAP and DPPH studies were also carried out. FRAP values in compounds 1–12 were found to range from 26.989–3415.556 µmol FeSO4.7H2O/mg. They also displayed moderate antioxidant potential in the range of SC50=0.03–87.32 mg/mL compared with the control Trolox (SC50 =0.004) in DPPH radical scavenging activities. It was seen that the AChE inhibition percentages of the compounds were in the range of 23.04–58.10% at 0.1 mM concentration. This is the first research on the synthesis, antioxidant and enzyme inhibition properties of these compounds.
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İncele - MakaleAçık Erişim2020Scopus SJRQ2Removal Kinetics of Olive-Mill Wastewater in a Batch-Operated Aerobic Bioreactor
Kul, Sinan; Nuhoglu, Alper
This study involves the removal of the olive-mill wastewater (OMW), which is a significant pollutant, in a batch reactor under aerobic conditions by mixed cultures. It also includes comparison of different substrate inhibition models, calculation of kinetic parameters, and testing the merit of the chosen mathematical model with respect to OMW concentration and changes with time. Average initial microorganism concentration (X0) in the batch reactor was 100 +/- 15 mg L-1. During the study the treatment of OMW with initial chemical oxygen demand (S0) concentration between 10 and 1,000 mg COD L-1 was investigated. Maximum specific growth rate (mu max) was reached with 130 mg COD L-1 initial concentration and 3 h experimental duration produced 57.17% chemical oxygen demand (COD) removal efficiency. Other experiments with increasing initial concentration increased COD removal duration, with 927 mg COD L-1 initial concentration regressing to 8.88% removal efficiency after 3 h. The biokinetic equations of Aiba, Haldane, Tseng, and Yano and Koga were chosen to relate S0 concentration to specific growth rate (mu) and the biokinetic parameters in these equations were calculated. The most appropriate biokinetic equation was the Haldane model in terms of R2 value and the Haldane equation parameters 0.43 h-1, 45.34 mg L-1, and 207.97 mg L-1 were calculated for mu max, half-saturation constant (Ks) and inhibition constant (Ki), respectively. Also, a mathematical biokinetic model including the Haldane equation was used to test the OMW removal performance and it was seen that the chosen model was well able to reflect system behavior. After the calibration of mu max, the most-sensitive parameter of the Haldane model, to 0.22 h-1, the model gave a better fit for all tested conditions.
AtıfWoS2OpenAlex7İncele - MakaleYalnız künye2018Scopus SJRQ2The interactions of cephalosporins on polyol pathway enzymes from sheep kidney
Şengül, Bülent; Beydemir, Şükrü
Context: Cephalosporins are derived from the fungus Acremonium. Due to their strong bactericidal ability, these drugs have to a wide usage in medicine. Objective: An investigation of the effects on sheep renal aldose reductase (AR) and sorbitol dehydrogenase (SDH) of cefoperazone, cefazolin, cefuroxime, ceftazidime and ceftriaxone as cephalosporin drugs was carried out in the present study. Methods: AR and SDH were purified from sheep kidney by ion exchange, gel filtration and affinity methods with approximately 219- and 484-fold, respectively. Some kinetic properties of the enzymes were determined such as optimal pH, optimal ionic strength, optimal temperature, stable pH, Km and Vmax. IC50 values of the drugs were found for each enzyme. Results: While the AR was inhibited by all drugs, SDH enzyme was inhibited by only CXM (IC50 8.10 mM). Interestingly, CZO activated SDH enzyme. This result was evaluated as important for the flow of the polyol reactions. Ki values and inhibition types were determined for AR. However, these values could not have determined for SDH, due to insufficient inhibition. Conclusions: From these results, it was concluded that cephalosporins may have an important effect on flow of the polyol metabolism.
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İncele - MakaleAçık Erişim2017Scopus SJRQ1Inhibition behaviours of some phenolic acids on rat kidney aldose reductase enzyme: an in vitro study
Alim, Zuhal; Kilinç, Namik; Şengül, Bülent; Beydemir, Şükrü
Aldose reductase (AR) inhibitors have vital importance in the treatment and prevention of diabetic complications. In this study, rat kidney AR was purified 19.34-fold with a yield of 3.49% and a specific activity of 0.88 U/mg using DE-52 Cellulose anion exchange chromatography, gel filtration chromatography and 2′5′ ADP Sepharose-4B affinity chromatography, respectively. After purification, the in vitro inhibition effects of some phenolic acids (tannic acid, chlorogenic acid, sinapic acid, protocatechuic acid, 4-hydroxybenzoic acid, p-coumaric acid, ferulic acid, vanillic acid, syringic acid, α-resorcylic acid, 3-hydroxybenzoic acid and gallic acid) were investigated on purified enzyme. We determined IC50, Ki values and inhibition types of these phenolic acids. As a result, tannic and chlorogenic acid had a strong inhibition effect. On the other hand, gallic acid had a weak inhibition effect. In this study, all phenolic acids except for chlorogenic acid and p-coumaric acid showed non-competitive inhibition effects on rat kidney AR.
AtıfScopus61WoS60OpenAlex64İncele - MakaleYalnız künye2017Scopus SJRQ2Mechanism of capsaicin inhibition of aldose reductase activity
Alim, Zuhal; Kilinc, Namık; Sengul, Bulent; Beydemir, Sukru
Aldose reductase (AR) inhibitors play a vital importance as a potential therapeutic and preventive medicine when it comes to hyperglycemia associated diabetic complications. Additionally, capsaicin is used as a food additive and a drug in a number of diverse clinical trials. The aim of this study is to determine the in vitro inhibition behavior of capsaicin on AR enzyme activity, which was obtained from different rat tissues (heart, kidney, liver, and brain). We showed that AR was inhibited by capsaicin in the micromolar range and noncompetitive manner in all of the tissues. Ki values of capsaicin were found to be 8.87, 264, 535, and 597, respectively, in heart AR, kidney AR, liver AR, and brain AR. In conclusion, capsaicin may be an effective molecule when used in low concentrations to prevent diabetic complications associated with the polyol pathway.
AtıfScopus21WoS19OpenAlex24İncele - MakaleYalnız künye2016Scopus SJRQ2In vitro inhibitory effects of palonosetron hydrochloride, bevacizumab and cyclophosphamide on purified paraoxonase-I (hPON1) from human serum
Türkeş, Cüneyt; Söyüt, Hakan; Beydemir, Şükrü
In this study, we investigated the effects of the drugs, palonosetron hydrochloride, bevacizumab and cyclophosphamide, on human serum paraoxonase-I (hPON1) enzyme activity in in vitro conditions. The enzyme was purified ~231-fold with 34.2% yield by using ammonium sulphate precipitation, DEAE-Sephadex A-50 ion-exchange chromatography and Sephadex G-200 gel-filtration chromatography from human serum. hPON1 exhibited a single protein band on the SDS polyacrylamide gel electrophoresis. The inhibition studies were performed on paraoxonase activity of palonosetron hydrochloride, bevacizumab and cyclophosphamide. Ki constants were found as 0.033 ± 0.001, 0.054 ± 0.003 mM and 3.419 ± 0.518 mM, respectively. Compared to the inhibition rates of the drugs, palonosetron hydrochloride has the maximum inhibition rate. However, inhibition mechanisms of the drugs were determined as noncompetitive by Lineweaver-Burk curves.
AtıfScopus49WoS49OpenAlex56İncele - MakaleYayıncıda açık erişim2015Scopus SJRQ1Human serum paraoxonase-1 (hPON1): In vitro inhibition effects of moxifloxacin hydrochloride, levofloxacin hemihidrate, cefepime hydrochloride, cefotaxime sodium and ceftizoxime sodium
Türkeş, Cüneyt; Söyüt, Hakan; Beydemir, Şükrü
In this study, we investigated the effects of antibacterial drugs (moxifloxacin hydrochloride, levofloxacin hemihidrate, cefepime hydrochloride, cefotaxime sodium and ceftizoxime sodium) on human serum paraoxonase-1 (hPON1) enzyme activity from human serum in vitro conditions. For this purpose, hPON1 enzyme was purified from human serum using simple chromatographic methods. The antibacterial drugs exhibited inhibitory effects on hPON1 at low concentrations. Ki constants were calculated to be 2.641 ± 0.040 mM, 5.525 ± 0.817 mM, 35.092 ± 1.093 mM, 252.762 ± 5.749 mM and 499.244 ± 10.149 mM, respectively. The inhibition mechanism of moxifloxacin hydrochloride was competitive, whereas levofloxacin hemihidrate, cefepime hydrochloride, cefotaxime sodium and ceftizoxime sodium were noncompetitive inhibitors.
AtıfScopus53WoS53OpenAlex57İncele - MakaleAçık Erişim2014Scopus SJRQ2Impact of antibacterial drugs on human serum paraoxonase-1 (hPON1) activity: An in vitro study
Söyüt, Hakan; Kaya, Elif Duygu; Beydemir, Şükrü
Objective: To investigate the in vitro effects of the antibacterial drugs, meropenem trihydrate, piperacillin sodium, and cefoperazone sodium, on the activity of human serum paraoxonase (hPON1). Methods: hPON1 was purified from human serum using simple chromatographic methods, including DEAE-Sephadex anion exchange and Sephadex G-200 gel filtration chromatography. Results: The three antibacterial drugs decreased in vitro hPON1 activity. Inhibition mechanisms meropenem trihydrate was noncompetitive while piperacillin sodium and cefoperazone sodium were competitive. Conclusions: Our results showed that antibacterial drugs significantly inhibit hPON1 activity, both in vitro, with rank order meropenem trihydrate piperacillin sodium cefoperazone sodium in vitro.
AtıfScopus5OpenAlex7İncele - MakaleAçık Erişim2013Scopus SJRQ2Carbonic anhydrase activity from the gilthead sea bream (Sparus aurata) liver: The toxicological effects of heavy metals
Kaya, Elif Duygu; Söyüt, Hakan; Beydemir, Sukru
Many studies have shown that metal ions may lead to oxidative stress in biological systems. Accordingly, DNA damage, protein modification, enzyme inhibition and activation, lipid peroxidation and many other effects may occur in living organisms. Many different formations of metal ions may enter human cells along with water, air, and various foods, and humans are negatively affected by these conditions, either directly or indirectly. These effects may cause irreversible damage to human metabolism. In this study, the toxicological effects of heavy metals on carbonic anhydrase enzyme activity from the gilthead sea bream liver were investigated. The carbonic anhydrase enzyme was purified via affinity chromatography and had a specific activity of 6775.5 EU mg(-1). The kinetics and characteristic properties, such as optimum pH, stable pH, optimum temperature, activation energy (E-a), activation enthalpy (Delta H), Q(10), K-m, and V-max, were determined for the purified enzyme SDS-polyacrylamide gel electrophoresis showed a single band and molecular weight of the subunit was approximately 25 kDa. Cd(II), Cu(II), Ni(II) and Ag(I) inhibited the enzyme activity in vitro. The type of inhibition and K-i values for these metals were calculated from Lineweaver-Burk plots as 17.74 mM, 36.20 mM, 12.85 mM and 0.025 mM for Cd(II), Cu(II), Ni(II) and Ag(I), respectively. All the metals were noncompetitive inhibitors. (C) 2013 The Authors. Published by Elsevier B.V. All rights reserved.
AtıfWoS27OpenAlex32İncele - MakaleAçık Erişim2012Scopus SJRQ2The impact of heavy metals on the activity of carbonic anhydrase from rainbow trout (Oncorhynchus mykiss) kidney
Söyüt, Hakan; Beydemir, Şükrü
Many environmental and health problems have become a consequence of contamination of soil and water by toxic heavy metals and organic pollutants in the present age of technology. Heavy metals play vital roles in enzyme activities and other metabolic events with their bioaccumulative and nonbiodegradable properties among aquatic pollutants. Metal toxicity causes irregular metallothioneins protein synthesis, renal damage, and disruption of bone structure in humans and wildlife. In this study, we investigated in vitro effects of some metals on chemical-targeted carbonic anhydrase (CA) enzyme from rainbow trout kidney. The enzyme was purified with a specific activity of 17,285 EU × mg-1 and 31.7% yield and approximately 1800-fold using simple affinity purification method. Molecular weights of the subunit and native enzyme were estimated as 28.7 kDa and 26.9 kDa via sodium dodecyl sulfate polyacrylamide gel electrophoresis and Sephadex-G 200 column, respectively. Other kinetic properties of the enzyme were determined. Apparent Km, Vmax and kcat values were 0.40 mM, 0.097 μmol min-1 and 15.2 s-1 for p-nitrophenylacetate substrate, respectively. Inhibitory effects of cobalt, zinc, copper, cadmium and silver on CA activity were determined using the esterase method under in vitro conditions. IC50 and Ki values were calculated for metals. Ki values for Co2+, Zn2+, Cu2+, Cd2+ and Ag+ were 0.035, 1.2, 34.8, 103 and 257 from Lineweaver-Burk graphs, respectively. Consequently, in vitro inhibition rank order was determined as Co2+ > Zn2+ > Cu 2+ > Cd2+ > Ag+. The potential inhibitor for CA was found as Co2+ from these results.
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