Kalın, Ramazan
Loading...
Profile URL
Name Variants
Ramazan Kalin
Kalin Ramazan
Kalin R
Kalın R
Kalın Ramazan
Kalin Ramazan
Kalin R
Kalın R
Kalın Ramazan
Job Title
Doç. Dr.
Email Address
ramazan.kalin@erzurum.edu.tr
Main Affiliation
2.3. Temel Bilimler Bölümü
Status
ORCID ID
Scopus Author ID
Turkish CoHE Profile ID
Google Scholar ID
WoS Researcher ID
Sustainable Development Goals
SDG data is not available
Scopus data could not be loaded because of an error. Please refresh the page or try again later.
WoS data could not be loaded because of an error. Please refresh the page or try again later.
Scholarly Output
17
Articles
17
Views / Downloads
0/0
Supervised MSc Theses
0
Supervised PhD Theses
0
WoS Citation Count
0
Scopus Citation Count
0
WoS h-index
0
Scopus h-index
0
Patents
0
Projects
0
WoS Citations per Publication
0.00
Scopus Citations per Publication
0.00
Open Access Source
6
Supervised Theses
0
Scholarly output chart could not be loaded because of an error. Please refresh the page or try again later.
| Journal | Count |
|---|---|
| Chemistryselect | 2 |
| Journal of Biochemical and Molecular Toxicology | 2 |
| International Journal of Food Properties | 2 |
| Current Computer-Aided Drug Design | 1 |
| Food Biophysics | 1 |
Current Page: 1 / 3
Scopus Quartile Distribution
Quartile distribution chart could not be loaded because of an error. Please refresh the page or try again later.
Competency Cloud
17 results
Scholarly Output Search Results
Now showing 1 - 10 of 17
Article Discovery of Potent Carbonic Anhydrase and Acetylcholinesterase Inhibitors: 2-Aminoindan Β-Lactam Derivatives(MDPI, 2016) Genc, Hayriye; Kalin, Ramazan; Koksal, Zeynep; Sadeghian, Nastaran; Kocyigit, Umit M.; Zengin, Mustafa; Ozdemir, Hasanbeta-Lactams are pharmacologically important compounds because of their various biological uses, including antibiotic and so on. beta-Lactams were synthesized from benzylidene-inden derivatives and acetoxyacetyl chloride. The inhibitory effect of these compounds was examined for human carbonic anhydrase I and II (hCA I, and II) and acetylcholinesterase (AChE). The results reveal that beta-lactams are inhibitors of hCA I, II and AChE. The Ki values of beta-lactams (2a-k) were 0.44-6.29 nM against hCA I, 0.93-8.34 nM against hCA II, and 0.25-1.13 nM against AChE. Our findings indicate that beta-lactams (2a-k) inhibit both carbonic anhydrases (CA) isoenzymes and AChE at low nanomolar concentrations.Article A Hierarchical Assembly of Flower-Like Hybrid Turkish Black Radish Peroxidase-Cu2+ Nanobiocatalyst and Its Effective Use in Dye Decolorization(Pergamon-Elsevier Science Ltd, 2017) Altinkaynak, Cevahir; Tavlasoglu, Sureyya; Kalin, Ramazan; Sadeghian, Nastaran; Ozdemir, Hasan; Ocsoy, Ismail; Ozdemir, NalanEffective dye decolorization in wastewater still shows a big challenge. Although the biological methods, especially using enzymes, offer alternative and effective process for dye degradation and overcome the limitations of chemical and physical methods such as the instability, lack of reusability and high cost of free enzymes strictly, which limit their use in many scientific and technical applications. Enzymes rapidly lose their activities in aqueous solutions and against environmental changes due to their very susceptibility and unfavorable conformations. Herein, we report preparation of the enzyme-inorganic hybrid nanostructures with flower-like shape consisting of Turkish black radish peroxidase and Cu2+ metal ions using an encouraging enzyme immobilization approach. The peroxidase-Cu2+ hybrid nanoflowers (NFs) exhibited enhanced stability and activity towards various pH values and provided excellent dye decolorization efficiency for Victoria blue (VB) dye with more than 90% within 1 h. The NFs were also repeatedly used in efficient and caused 77% VB decolorization efficiency even at tenth cycles. However, to the best of our knowledge, for the first time, we prepared peroxidase enzyme isolated from Turkish black radish incorporated NFs and used them for dye decolorization. We believe that the NFs can be promising materials for dye decolorization in real wastewater treatment. (C) 2017 Elsevier Ltd. All rights reserved.Article In Vitro Inhibition Profiles and Molecular Docking Analysis of Benzohydrazide Derivatives on Red Blood Cell Carbonic Anhydrases Isozymes(Bentham Science Publ Ltd, 2022) Korkmaz, Isil Nihan; Guller, Pinar; Kalin, Ramazan; Oztekin, Aykut; Ozdemir, HasanBackground: Carbonic anhydrases (CAs, EC 4.2.1.1) are metalloenzymes that contain zinc ions on the active side and convert carbon dioxide to bicarbonate in metabolism. Human CA-I and CA-II, which are the most abundant CA isozymes in erythrocytes, have been therapeutic targets in the treatment of glaucoma, hypertension, ulcer, osteoporosis, and, neurological disorders. Benzohydrazides are biologically active compounds, and their various pharmacological effects have been reported. Aim: In light of this, the objective of this study was to investigate the in vitro effects of benzohydrazide derivatives on the activities of hCA-I and hCA-II, determine the compounds as selective inhibitors for these isoenzymes, and estimate the inhibition mechanism through molecular docking studies. Methods: In this work, we synthesized the 10 different derivatives of benzohydrazide containing various functional group of different positions. Results: As a result, all benzohydrazide derivatives inhibited both isozymes in vitro and 2-amino 3-nitro benzohydrazide (10) was found to be the most efficient inhibitor of both hCA isozymes with the IC50 values of 0.030 and 0.047 mu M, respectively. In the molecular docking studies, 3-amino 2-methyl benzohydrazide (3) had the lowest estimated free binding energies against hCA isozymes as -6.43 and -6.13 kcal/mol. Conclusion: In this study, hCA-I & II isozymes were isolate from human erythrocytes. CA isozymes are one of these target enzymes. WBC hope that the benzohydrazide derivatives, can guide remedies targeting carbonic anhydrase.Article Assessment of 3-Amino Acid Methyl Ester Derivatives as Glutathione S-Transferase and Glutathione Reductase Inhibitor: Supported by Molecular Docking Studies(Wiley-V C H Verlag GmbH, 2024) Korkmaz, Isil Nihan; Guller, Pinar; Kalin, Ramazan; Ozdemir, HasanGSTs catalyze detoxification reactions of harmful xenobiotics via conjugation with glutathione (GSH) while glutathione reductase (GR) is the sole enzyme that acts in the recovery reaction of GSH from oxidized glutathione (GSSG). In this study, in vitro inhibitory impacts of 3-amino-benzoic acid methyl ester compounds on GR and GST were investigated. For this firstly, GR and GST were obtained from human blood with specific activity of 6.26 EU/mg protein and 8.57 EU/mg protein respectively. Then, inhibition studies were performed. It was found that methyl 3-amino-5-chlorobenzoate had the highest inhibitory effect on hGR with Ki value of 0.524 +/- 0.109 mu M) and methyl 3-amino-4-nitrobenzoate was the most effective inhibitor on hGST with Ki value of 37.05 +/- 4.487 mu M. Besides, molecular docking analysis was used to estimate the binding energies of molecules. Methyl 3-amino-4-nitrobenzoate and methyl 3-amino-4-chlorobenzoate were predicted to have the highest binding affinity into GR and GST receptors respectively.Article One-Step Isolation and Biochemical Characterization of a Novel Peroxidase Enzyme from Jerusalem Artichoke (Helianthus Tuberosus L.)(Wiley-V C H Verlag GmbH, 2023) Kalin, RamazanIn the present study, a novel peroxidase was purified and characterized from the jerusalem artichoke (Helianthus Tuberosus L.) using an efficient one-step purification method. The purification factor for the jerusalem artichoke peroxidase (POD) was 87.17-fold (with a yield of 13.28 %). Molecular mass and POD purity were controlled with the SDS-PAGE and seen a single band at approximately 47.8 kDa. The optimum parameters (pH, ionic strength, and temperature) for POD activity were investigated and determined as pH 6.5, 0.7 M in phosphate buffer, and 40 degrees C, respectively. The K-M and V-max values of the jerusalem artichoke POD were calculated to be 94.33 mM and 12.74 EU/mL.min for guaiacol, and 0.208 mM and 1.481 EU/mL.min for hydrogen peroxide, respectively. Furthermore, the 4-aminobenzohydrazide was shown to act as a competitive inhibitor of the jerusalem artichoke POD. Finally, molecular docking studies of the 4-aminobenzohydrazide were performed, and the estimated binding energy value was calculated to be -3.79 kcal/mol.Article Lactoperoxidase Inhibition of Some Natural Phenolic Compounds: Kinetics and Molecular Docking Studies(Wiley, 2020) Koksal, Zeynep; Kalin, Ramazan; Kalin, Pinar; Karaman, Muhammet; Gulcin, Ilhami; Ozdemir, HasanThe inhibition effects of some phenolic compounds from natural products such as taxifolin, resveratrol, olivetol, cynarine, and phloretin on bovine milk lactoperoxidase (LPO) enzyme were examined. For this aim, LPO was purified by the affinity chromatography technique with a yield of 77.68% in 421.32 times. The kinetic value, K-i, was calculated from the equations obtained from drawn graphs. In order to discover inhibition mechanism of phenolic compounds, induced fit docking process was performed on the LPO receptors. The binding affinity of the compounds was calculated and at the best-scored ligand-receptor complex, residues responsible for enzyme inhibition were detected. As a result, this molecule demonstrated the potential inhibitory effect on LPO. According to the results of kinetic study. It has shown a noncompetitive inhibition effect, Phloretin's K-i value was determined by 48.89 +/- 14.22 nM. Practical applications There are natural antimicrobial systems, such as the lactoperoxidase (E.C.1.11.1.7; LPO) system, which eliminates the harmful effects of microorganisms in milk. The chemical reactions in this system are catalyzed by the LPO. In the dairy industry, the LPO system is considered critical for the preservation of pasteurized milk, yogurt, raw milk, and cheese. The system is used for improvement the protection condition of milk at high temperatures.Article Inhibitory Effects of Selected Pesticides on Peroxidases Purified by Affinity Chromatography(Taylor & Francis Inc, 2018) Koksal, Zeynep; Kalin, Ramazan; Gulcin, Ilhami; Ozdemir, HasanThe objective of this study was to determine the in vitro inhibition effects of seven commonly used pesticides including 2,4-d-acid dimethylamine, fenoxaprop-p-ethyl, glyphosate isopropylamine, haloxyfop-p-methyl, cypermethrin, -cyhalothrin, and dichlorvos on the peroxidase purified from turnip (Brassica rapa L.) and black radish (Raphanus sativus L.) using 4-amino benzohydrazide affinity column chromatography. The purification factors for the turnip and black radish peroxidases were found to be 263.29-fold (with a yield of 12.89%) and 36.20-fold (with a yield of 6.90%), respectively. Among these compounds, -cyhalothrin showed the strongest inhibitory effect against turnip peroxidase (K-i: 1.23 x 10(-2)+/- 0.21 x 10(-2)mM) as noncompetitive inhibition. On the other hand, cypermethrin demonstrated the highest inhibition effect against black radish peroxidase (K-i: 2.14 x 10(-2)+/- 0.08 x 10(-2)mM) as competitive inhibition.Article Secondary Sulfonamides as Effective Lactoperoxidase Inhibitors(MDPI, 2017) Koksal, Zeynep; Kalin, Ramazan; Camadan, Yasemin; Usanmaz, Hande; Almaz, Zuleyha; Gulcin, Ilhami; Ozdemir, HasanSecondary sulfonamides (4a-8h) incorporating acetoxybenzamide, triacetoxybenzamide, hydroxybenzamide, and trihydroxybenzamide and possessing thiazole, pyrimidine, pyridine, isoxazole and thiadiazole groups were synthesized. Lactoperoxidase (LPO, E.C.1.11.1.7), as a natural antibacterial agent, is a peroxidase enzyme secreted from salivary, mammary, and other mucosal glands. In the present study, the in vitro inhibitory effects of some secondary sulfonamide derivatives (4a-8h) were examined against LPO. The obtained results reveal that secondary sulfonamide derivatives (4a-8h) are effective LPO inhibitors. The K-i values of secondary sulfonamide derivatives (4a-8h) were found in the range of 1.096 x 10(-3) to 1203.83 mu M against LPO. However, the most effective inhibition was found for N-(sulfathiazole)-3,4,5-triacetoxybenzamide (6a), with K-i values of 1.096 x 10(-3) +/- 0.471 x 10(-3) mu M as non-competitive inhibition.Article Impact of Some Avermectins on Lactoperoxidase in Bovine Milk(Taylor & Francis Inc, 2016) Koksal, Zeynep; Kalin, Ramazan; Gulcin, Ilhami; Ozdemir, Hasan; Atasever, AliMany macrocyclic lactones, including avermectins, are known to be used as a veterinary drug, agricultural pesticides, and insecticides. Lactoperoxidase (EC 1.11.1.7) is one of the peroxidases found in milk. Lactoperoxidase has a natural host defense system against micro-organisms and a natural antimicrobial system. In this study, some macrocyclic lactones, including emamectin-benzoate, doramectin, eprinomectin, abamectin, moxidectin-vetranal, and ivermectin were investigated for in vitro inhibitory effects on the bovine lactoperoxidase enzyme, which was purified using amberlite CG-50 H+ resin and sepharose 4B-L-tyrosine-sulphanamide affinity chromatography 344.6-fold, with a yield of 61.1% and a specific activity of 39.11 EU/mg protein. Emamectin-benzoate, doramectin, eprinomectin, abamectin, moxidectin-vetranal, and ivermectin are also known strong antiparasitary properties. In this study, we demonstrated that avermectins have strong lactoperoxidase inhibitory effects. Of these, the emamectin-benzoate was shown to have the most inhibiting effect against lactoperoxidase with Ki value of 6.82 +/- 2.60 mu M.Article In Vitro Effects of Standard Antioxidants on Lactoperoxidase Enzyme-A Molecular Docking Approach(Wiley, 2020) Kalin, Ramazan; Koksal, Zeynep; Kalin, Pinar; Karaman, Muhammet; Gulcin, Ilhami; Ozdemir, HasanLactoperoxidase (LPO), an antioxidant enzyme, is a natural antimicrobial system that eliminates the harmful effects of microorganisms in milk. It has a wide range of applications and is also preferred in cosmetic and clinical applications, as well as used in foods. The use of antioxidants is well recognized in the food and feed industries to improve the shelf life of products. This study aimed to determine the in vitro inhibition effects of Trolox, alpha-tocopherol, butylated hydroxyanisole, butylated hydroxytoluene, and propyl gallate, which are commonly used as antioxidants in food and pharmaceutical products. For this purpose, LPO was first purified in a single step using sepharose-4B-l-tyrosine-sulfanilamide affinity gel chromatography. Also, some inhibition parameters, including half-maximal inhibitory concentration (IC50), K-i values, and inhibition types, were calculated for each antioxidant molecule. The IC50 values of these molecules, which exhibited competitive inhibition, varied between 377.7 and 3397.8nM. Molecular docking studies were also performed for all compounds. According to the binding scores, alpha-tocopherol was shown to exhibit the most effective inhibitor property (IC50: 377.7nM and K-i: 635.8 +/- 16.8nM) among the standard antioxidants used in this study. Inhibiting the LPO activity by standard antioxidants results in the weakening of the immune system during lactation, which is important for metabolism.
