Sürdürülebilir Kalkınma Amaçları
Yazarlar
- Dertli, Enes(4)
- Şahin, Engin(4)
- Beydemir, Şükrü(3)
- Serencam, Hüseyin(2)
- İspirli, Hümeyra(2)
- Şengül, Bülent(2)
- Alim, Zuhal(1)
- Asadov, Elsevar(1)
- Boyraci, Gulsum Merve(1)
- Can, Zehra(1)
- Colquhoun, Ian J.(1)
- Degirmenci, Atiye(1)
- Kilinç, Namik(1)
- Kolayli, Sevgi(1)
- Sağdıç, Osman(1)
- Skory, Christopher(1)
- Söyüt, Hakan(1)
- Tozlu, Caner(1)
- Türkeş, Cüneyt(1)
- Yildiz, Oktay(1)
- Yüzer, Mustafa Onur(1)
Yayınlar
- MakaleYalnız künye2020Scopus SJRQ2Honeys from some different regions of Azerbaijan: bioactive characteristics based on phenolic profile and antioxidant activity
Degirmenci, Atiye; Can, Zehra; Boyraci, Gulsum Merve; Yildiz, Oktay; Asadov, Elsevar; Kolayli, Sevgi
Azerbaijan is an important region for the beekeeping and honey industry. Biochemical characteristics of eleven honey samples from different regions of Azerbaijan were analyzed through measuring electrical conductivity, optical activity, moisture content, proline and diastase number. Phenolic components are analyzed by reverse-phase high-performance liquid chromatography (RP-HPLC) with UV–Vis double beam detector. Sugars profiles of samples were carried out using HPLC with a refractive index detector (RID). Total phenolic content (TPC), ferric reducing antioxidant power (FRAP) and 2,2-diphenyl-1-picryhydrazyl (DPPH) free radical scavenging activity were measured with the aim of gathering information on the antioxidant power of samples. Biochemical and antioxidant characteristics are also supported with melissopalynological data. Conductivity ranged between 0.32 and 0.82 mS cm−1, moisture 14.52 and 20.78%, proline 314.34 and 1077.21 mg kg−1, diastase 13.05 and 22.19. Azerbaijan honeys exhibited levorotatory properties. Total phenolic content varied from 18.82 to 154.75 mg gallic acid equivalent per 100 g honey. The results confirm that physico-chemical and biologically active properties of Azerbaijan honeys are affected by the flora and geographical variations.
AtıfScopus17WoS16OpenAlex20
İncele - MakaleYalnız künye2020Scopus SJRQ3Production of mannose-containing oligosaccharides by glucansucrase E81 and determination of their functional characteristics
İspirli, Hümeyra; Dertli, Enes
Oligosaccharides are one of the functional ingredients to be used in food technology. In this study, by using an active glucansucrase GTFA-ΔN E81 in the acceptor reaction of mannose, mannose-containing oligosaccharides were produced and their functionality was tested. The formation of the oligosaccharides were visualised by TLC analysis and mannose-containing oligosaccharides up to DP 7 were determined by LC-MS analysis. The presence of the (1,6)Glc and (1,3)Glc units within the oligosaccharides were determined by NMR analysis. The in vitro immune-modulatory functions of the mannose-containing oligosaccharides were determined but no induction in IL-4, IL-10, IL-12 and TNF-α cytokine levels were detected. Importantly this oligosaccharide mixture showed prebiotic effect by triggering the growth of tested probiotics and not affecting the growth of pathogen strains. Our findings reveals the potential of the role of glucansucrases for the production of functional oligosaccharides.
AtıfScopus8WoS7OpenAlex8İncele - MakaleYalnız künye2020Scopus SJRQ3First green synthesis of (R)-2-methyl-1-phenylpropan-1-ol using whole-cell Lactobacillus paracasei BD101 biotransformation
Şahin, Engin
Green chemistry includes a novel process in the production of drugs precursors and biological active molecules using biocatalysts, so reducing the threats for human sanitary and ecological pollutions. Asymmetric bioreduction of prochiral ketones by biocatalysts is one of the best prevalent used methods in synthetic organic chemistry due to the production of enantiopure chiral carbinols. This study emphasizes the application biocatalyst L paracasei BD101 for enantioselective bioreduction of 2-methyl-1-phenylpropan-1-one ketone, which contain branched alkyl chain, to (R)-2-methyl-1-phenylpropan-1-ol ((R)-2) in high yields and excellent enantiomeric excess (>99%). The scale-up production was performed, and 4.61 g of (R)-2 in enantiopure form was synthesized. L paracasei BD101 was proved to be a substantial biocatalyst in asymmetric bioreduction of a ketone which contains a branched alkyl chain. There is not any work in the literature similar to our study. Hence, it is important to work on filling this gap. This study is the first example for an enantiopure synthesis of (R)-2 by a biocatalyst. The new green method was developed for bioreduction of bulky ketones, which contains a branched alkyl chain, and it approves the synthesis of novel chiral carbinols in an easy, cheap, and environmentally friendly condition using L paracasei BD101.
AtıfScopus10WoS9OpenAlex10İncele - MakaleAçık Erişim2019Scopus SJRQ3Characterization of a glucansucrase from Lactobacillus reuteri E81 and production of malto-oligosaccharides
İspirli, Hümeyra; Yüzer, Mustafa Onur; Skory, Christopher; Colquhoun, Ian J.; Sağdıç, Osman; Dertli, Enes
Glucansucrases, which can be produced by different Lactic Acid Bacteria (LAB), catalyze the synthesis of α-glucans with different structures and properties using sucrose as substrate. In this study, a novel glucansucrase (GTFA) from Lactobacillus reuteri E81 was identified and heterologously expressed. Alignments of GTFA with other glucansucrases revealed its novelty and a putative 3D model structure was obtained. The biochemical properties of the truncated enzyme without the N-terminal variable region, GTFA-ΔN, was characterized. The Km and Vmax were found to be 7.5 mM and 1.49 IU/mg, respectively, and it showed optimum activities at pH 7 and at 50 °C. The GTFA-ΔN produced in vitro an α-glucan with (α1 → 3) and (α1 → 6) glycosidic linkages using sucrose as the substrate. Importantly, GTFA-ΔN synthesized DP = 9 oligosaccharides using sucrose and maltose as the donor and acceptor sugars, respectively, as detected by TLC, HPLC, LC-MS and NMR analysis.
AtıfScopus40WoS40OpenAlex40İncele - MakaleAçık Erişim2019Scopus SJRQ3Production of enantiomerically pure (S)-phenyl(pyridin-2-yl)methanol with Lactobacillus paracasei BD101
Şahin, Engin; Serencam, Hüseyin; Dertli, Enes
Asymmetric reduction studies of heteroaryl ketones, including phenyl(pyridin-2-yl)methanone in enantioselective form with biocatalysts are very few, and chiral heteroaryl alcohols have been synthesized generally in the small scale. In this study, seven bacterial strains have been used to produce the (S)-phenyl(pyridin-2-yl)methanol in high enantiomeric excess and yield. Among the tested strains, Lactobacillus paracasei BD101, was found to be the best biocatalyst for the reducing phenyl(pyridin-2-yl)methanone to the (S)-phenyl(pyridin-2-yl)methanol at gram scale. The asymmetric bioreduction conditions were systematically optimized using L. paracasei BD101, which demonstrated excellent enantioselectivity and high level of conversion for the bioreduction reaction. (S)-phenyl(pyridin-2-yl)methanol, which is an analgesic, was produced enantiomerically pure form in the first time on gram scale using a biocatalyst. In total, 5.857 g of (S)-phenyl(pyridin-2-yl)methanol in enantiomerically pure form (>99% enantiomeric excess) was obtained in 52 h with 93% yield using whole cells of L. paracasei BD101. Enantiomerically pure (S)-phenyl (pyridin-2-yl)methanol, which is an analgesic, was first produced in the gram scale using a biocatalyst with excellent ee (>99%) and yield (93%).
AtıfScopus9WoS7OpenAlex9İncele - MakaleYalnız künye2019Scopus SJRQ3Production of enantiomerically enriched chiral carbinols using Weissella paramesenteroides as a novel whole cell biocatalyst
Tozlu, Caner; Şahin, Engin; Serencam, Hüseyin; Dertli, Enes
In this study, four bacterial strains were tested for their ability to reduce acetophenones to its corresponding alcohol. Among these strains Weissella paramesenteroides N7 was found to be the most successful biocatalyst to reduce the ketones to the corresponding alcohols. The reaction conditions were systematically optimized for W. paramesenteroides N7 that resulted in high enantioselectivity and conversion rates for the bioreduction. The scale-up asymmetric reduction of 1-(4-methoxyphenyl) propan-1-one (1r) by W. paramesenteroides N7 gave (R)-1-(4-methoxyphenyl) propan-1-ol (2r) with 94% yield and >99% enantiomeric excess. This is the first report showing the synthesis of (R)-1-(4-methoxyphenyl) propan-1-ol (2r) in enantiopure form using a biocatalyst on a gram scale. The whole cell catalyzed the reductions of ketone substrates on the preparative scale, demonstrating that W. paramesenteroides N7 would be a valuable biocatalyst for the preparation of chiral aromatic alcohols of pharmaceutical interest as a promising and alternative green approach.
AtıfScopus12WoS10OpenAlex11İncele - 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.
AtıfScopus12WoS12OpenAlex13
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 - MakaleAçık Erişim2017Scopus SJRQ3Debaryomyces hansenii as a new biocatalyst in the asymmetric reduction of substituted acetophenones
Şahin, Engin
Chiral secondary alcohols are convenient mediator for the synthesis of biologically active compounds and natural products. In this study fifteen yeast strains belonging to three food originated yeast species Debaryomyces hansenii, Saccharomyces cerevisiae and Hanseniaspora guilliermondii were tested for their capability for the asymmetric reduction of acetophenone to 1-phenylethanol as biocatalyst microorganisms. Of these strains, Debaryomyces hansenii P1 strain showed an effective asymmetric reduction ability. Under optimized conditions, substituted acetophenones were converted to the corresponding optically active secondary alcohols in up to 99% enantiomeric excess and at high conversion rates. This is the first report on the enantioselective reduction of acetophenone by D. hansenii P1 from pastırma, a fermented Turkish meat product. The preparative scale asymmetric bio reduction of 3-methoxy acetophenone 1g by D. hansenii P1 gave (R)-1-(3-methoxyphenyl) ethanol 2g 82% yield, and >99% enantiomeric excess. Compound 2g can be used for the synthesis of (+)-NPS-R-568 [3-(2-chlorophenyl)-N-[(1R)-1-(3-methoxyphenly) ethyl] propan-1-amine] which have a great potential for the treatment of primary and secondary hyper-parathyroidism. In addition, D. hansenii P1 successfully reduced acetophenone derivatives. This study showed that this yeast can be used industrially to produce enantiomerically pure chiral secondary alcohols, which can be easily converted to different functional groups.
AtıfScopus25WoS24OpenAlex26İncele - 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 - DergiJournal of Enzyme Inhibition and Medicinal Chemistry
- DergiArchives of Physiology and Biochemistry