Person: KAHRAMAN, MEMET VEZİR
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KAHRAMAN
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MEMET VEZİR
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Publication Metadata only Preparation and drug release properties of lignin-starch biodegradable films(WILEY-V C H VERLAG GMBH, 2012) OGAN, AYŞE; Calgeris, Ilker; Cakmakci, Emrah; Ogan, Ayse; Kahraman, M. Vezir; Kayaman-Apohan, NilhanStarch is one of the most commonly available natural polymers which are obtained from agro-sources. It is renewable and abundant in nature. Unfortunately due to its poor mechanical properties and hygroscopic nature, there are some strong limitations to the development of starch-based products. Usually blends of starch are prepared and plasticized with glycerol to improve some of its properties. In this study, lignin was extracted from hazelnut shells and investigated as a potential additive for starch biofilms. The structural characterization of hazelnut lignin was performed by employing UV spectroscopy and Fourier transform infrared (FTIR) spectroscopy. Lignin was blended with corn starch in different ratios to obtain biofilms. Mechanical and thermal properties of the biofilms were enhanced as the lignin amount was increased in the formulations. Water absorption tests were performed at pH 2.0, 4.0, and 6.0. The percent swelling values of the starch/lignin films increased as pH increased. Also, the biofilm exhibiting the best properties was chosen for the drug release studies. Biofilms showed a fast ciprofloxacin (CPF) release within an hour and then the drug release rate decreased. A pH dependent drug release mechanism was also observed according to KoshnerPeppas model. The drug release increased with a decrease in pH.Publication Metadata only Soybean oil based resin: A new tool for improved immobilization of alpha-amylase(WILEY, 2006) OGAN, AYŞE; Kahraman, MV; Kayaman-Apohan, N; Ogan, A; Gungor, AAcrylated epoxidized soybean resin has been utilized to immobilize the alpha-amylase via UV-curing technique. Among the numerous methods that exist for enzyme immobilization, entrapment and covalent binding are the focus of this study. The properties of immobilized enzyme were investigated and compared with those of the free enzyme. Upon immobilization by the two methods, the catalytic properties of the enzyme were not considerably changed as compared with that of nonimmobilized form; enzyme. The free enzyme lost its activity completely in 20 days, where as storage and repeated usage capability experiments demonstrated higher stability for the immobilized form. Immobilized enzyme prepared by attachment method possesses relatively higher activity compared with the activity of those obtained by entrapment method. (c) 2006 Wiley Periodicals, Inc.Publication Metadata only Preparation and characterization of sol-gel hybrid coating films for covalent immobilization of lipase enzyme(ELSEVIER, 2016) OGAN, AYŞE; Yuce-Dursun, Basak; Cigil, Asli Beyler; Dongez, Dilek; Kahraman, M. Vezir; Ogan, Ayse; Demir, SerapIn this study UV-curable hybrid epoxy-silica polymer films were prepared via sol-gel method. Lipase (EC 3.1.1.3) from Candida rugosa was covalently immobilized onto hybrid epoxy-silica polymer films and immobilization capacity of polymer films was found 7.22 mg g(-1). The morphology of the polymeric support was characterized by scanning electron microscopy (SEM) and Fourier Transform Infrared Spectroscopy (FTIR). Immobilized and free enzymes were used in two different reaction systems: hydrolysis of p-nitrophenyl palmitate in aqueous medium and synthesis of p-nitrophenyl linoleate (from p-nitrophenol and linoleic acid) in n-hexane medium. The effect of temperature on hydrolytic and synthetic activities was investigated and observed maximum activities at 50 degrees C and 45 degrees C for immobilized enzyme, orderly. Km values for free enzyme were determined 0.71 and 1.12 mM by hydrolytic and synthetic activity assays, respectively, while these values were observed as 0.91 mM and 1.19 mM for immobilized enzyme. At the end of 30 repeated cycles, 56% and 59% of initial activities remained for hydrolytic and synthetic assays, respectively. Native enzyme lost its activity completely within 20 days, whereas the immobilized enzyme retained for hydrolytic and synthetic activities was approximately 82% and 72%, respectively, under the same storage time. (C) 2016 Elsevier B.V. All rights reserved.Publication Open Access Covalent immobilization of acetylcholinesterase on a novel polyacrylic acid-based nanofiber membrane(WILEY, 2018-04) OGAN, AYŞE; Cakiroglu, Bekir; Cigil, Asli Beyler; Ogan, Ayse; Kahraman, M. Vezir; Demir, SerapIn this study, polyacrylic acid-based nanofiber (NF) membrane was prepared via electrospinning method. Acetylcholinesterase (AChE) from Electrophorus electricus was covalently immobilized onto polyacrylic acid-based NF membrane by demonstrating efficient enzyme immobilization, and immobilization capacity of polymer membranes was found to be 0.4 mg/g. The novel NF membrane was synthesized via thermally activated surface reconstruction, and activation with carbonyldiimidazole upon electrospinning. The morphology of the polyacrylic acid-based membrane was investigated by scanning electron microscopy, Fourier Transform Infrared Spectroscopy, and thermogravimetric analysis. The effect of temperature and pH on enzyme activity was investigated and maxima activities for free and immobilized enzyme were observed at 30 and 35 degrees C, and pH 7.4 and 8.0, respectively. The effect of 1 mM Mn2+, Ni2+, Cu2+, Zn2+, Mg2+, Ca2+ ions on the stability of the immobilized AChE was also investigated. According to the Michaelis-Menten plot, AChE possessed a lower affinity to acetylthiocholine iodide after immobilization, and the Michaelis-Menten constant of immobilized and free AChE were found to be 0.5008 and 0.4733 mM, respectively. The immobilized AChE demonstrated satisfactory reusability, and even after 10 consecutive activity assay runs, AChE maintained ca. 87% of its initial activity. Free enzyme lost its activity completely within 60 days, while the immobilized enzyme retained approximately 70% of the initial activity under the same storage time. The favorable reusability of immobilized AChE enables the support to be employable to develop the AChE-based biosensors.Publication Metadata only Preparation, characterization, and drug release properties of poly(2-hydroxyethyl methacrylate) hydrogels having beta-cyclodextrin functionality(JOHN WILEY & SONS INC, 2008) OGAN, AYŞE; Demir, Serap; Kahraman, M. Vezir; Bora, Nil; Apohan, Nilhan Kayaman; Ogan, AyseA new beta-cyclodextrin urethane-methacrylate monomer was synthesized from the reaction of toluene-2,4-diisocyanate, 2-hydroxyethyl methacrylate (HEMA), and beta-cyclodextrin (beta-CD). Based on inclusion character of beta-CD, a series of hydrogels were prepared by irradiating the mixtures of beta-cyclodextrin urethane-methacrylate monomer (beta-CD-UM), poly(ethylene glycol) diacrylate (PEG-DA), HEMA, and the photoinitator. Gel percentages and equilibrium swelling ratios (%) of hydrogels were investigated. It was observed that the equilibrium-swelling ratio increased with increasing beta-CD-UM content in the hydrogel composition. SEM images demonstrated that beta-CD-UM based hydrogel have porous fractured surface. In this study four different drug molecules, salicylic acid, sulfathiazole, rifampicin, and methyl orange as model drug, which are capable of forming inclusion complexes with beta-CD were chosen. For sulfathiazole and rifampicin, the drug loadings are very low (0.04 and 0.008 mmol/g dry gel), whereas methyl orange and salicylic acid drug uptakes are found as 0.15 and 0.18 mmol/g dry gel, respectively. The incorporation of beta-CD-UM comonomer into the gel slightly reduces the methyl orange and salicylic acid releases. However, a significant enhancement was achieved in the case of sulfathiazole delivery. It can be concluded that the inclusion complex formation capability of beta-CD moiety increases the drug release by improving the aqueous solubility of hydrophobic drugs. On the other hand, in the case of hydrophilic drugs, the drug release retards by forming strong drug-beta-CD complex and reducing the drug diffusivity. (C) 2008 Wiley Periodicals, Inc.Publication Metadata only Optimizing the immobilization conditions of beta-galactosidase on UV-cured epoxy-based polymeric film using response surface methodology(WILEY, 2021) OGAN, AYŞE; KAHRAMAN, MEMET VEZİR; DANIŞ, ÖZKAN; DEMİR, SERAP; Beyler-Cigil, Asli; Danis, Ozkan; Sarsar, Onur; Kahraman, Memet Vezir; Ogan, Ayse; Demir, SerapUV-cured epoxy-based polymeric film was prepared from glycidyl methacrylate, trimethylolpropane triacrylate, and poly(ethylene glycol) methylether acrylate. 2-hydroxy-2- methylpropiophenone was used as photo initiator. Covalent binding through epoxy groups was employed to immobilize beta-galactosidase from Escherichia coli onto this film, and immobilization conditions were optimized by the response surface methodology. ATR-Fourier transform infrared (FTIR) and scanning electron microscopy (SEM) analysis was carried out to characterize the epoxy-based polymeric film. Immobilization yield of beta-galactosidase on the material was calculated as 3.57 mg/g and the highest enzyme activity for the immobilized enzyme recorded at pH 6.5 degrees C and 60 degrees C. The immobilized enzyme preserved 51% of its activity at the end of 12 runs. Free and immobilized enzyme hydrolyzed 163.8 and 172.3 mu M lactose from 1% lactose, respectively. Kinetic parameters of both free and immobilized beta-galactosidase were also investigated, and K-m values were determined to be 0.647 and 0.7263 mM, respectively. Practical applications In our study we prepared a UV-cured epoxy-based polymeric film and optimized the immobilization conditions of beta-galactosidase from Escherichia coli onto this polymeric film by using response surface methodology (RSM). For this purpose, three-level and three-factor Box-Behnken design, which is an independent, rotatable or nearly rotatable, quadratic design, was applied. Optimal levels of three variables, namely, the amount of enzyme, immobilization time, and pH were determined using Box-Behnken experimental design. Lactose hydrolysis studies were performed from milk and lactose samples using free and immobilized enzyme. In addition, kinetic parameters, storage stability, and re-usability of immobilized beta-galactosidase were examined.Publication Metadata only Preparation and antimicrobial properties of LL-37 peptide immobilized lignin/caprolactone polymer film(WILEY, 2020) OGAN, AYŞE; Ogan, Ayse; Yuce-Dursun, Basak; Abdullah, Deka; Beyler-Cigil, Asli; Kahraman, Memet Vezir; Caglayan, Pinar; Birbir, Meral; Mutlu, Ozal; Gulsoy, NagihanThe use of biopolymers has gained priority in tissue engineering and biotechnology, both as dressing material and for enhancing treatment efficiency. There is a demand for new biopolymers designed with protease inhibitors and antimicrobials. LL-37 is an important antimicrobial peptide in human skin and exhibits a broad spectrum of antimicrobial activity against bacteria, fungi, and viral pathogens. Using lignin which is an abundant carbohydrate polymer in nature and a polyacrylic acid, we prepared a lignin/caprolactone biodegradable film by plastifying caprolactone and polyacyrlic acid. Lignin/caprolactone biodegradable film was activated with CDI and then immobilized LL-37 peptide. The structure was elucidated in terms of its functional groups by attenuated total reflectance-fourier transform infrared spectroscopy (ATR-FTIR), and the morphology of the lignin/caprolactone biodegradable film was characterized by scanning electron microscopy (SEM) before and after the immobilization process. The amount of LL-37 immobilized was determined by ELISA method. It was found that 97% of LL-37 peptide was successfully immobilized onto the lignin/caprolactone biodegradable film. Antimicrobial activity was determined in the lignin/caprolactone biodegradable film samples by quantitative antimicrobial activity method. According to the results, LL-37 immobilized lignin/caprolactone biodegradable film samples were effective on test organisms; Gram-positive Staphylococcus aureus and Gram-negative Escherichia coli. In bio-compatibility assays, the ability to support tissue cell integration was detected by using 3 T3 mouse fibroblasts. Samples were examined under transverse microscope, non-immobilized sample showed a huge cellular death, whereas LL-37 immobilized lignin/caprolactone biodegradable film had identical cellular growth with the control group. This dual functional lignin/caprolactone biodegradable film with enhanced antibacterial properties and increased tissue cell compatibility may be used to design new materials for various types of biological applications.