Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
Permanent URI for this collectionhttps://hdl.handle.net/11147/7148
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Article Citation - WoS: 15Citation - Scopus: 17Improved Activity of Alpha-L From Geobacillus Vulcani Gs90 by Directed Evolution: Investigation on Thermal and Alkaline Stability(John Wiley and Sons Inc., 2019) Sürmeli, Yusuf; İlgü, Hüseyin; Şanlı Mohamed, Gülşahalpha-L-Arabinofuranosidase (Abf) is a potential enzyme because of its synergistic effect with other hemicellulases in agro-industrial field. In this study, directed evolution was applied to Abf from Geobacillus vulcani GS90 (GvAbf) using one round error-prone PCR and constructed a library of 73 enzyme variants of GvAbf. The activity screening of the enzyme variants was performed on soluble protein extracts using p-nitrophenyl alpha-L-arabinofuranoside as substrate. Two high activity displaying variants (GvAbf L307S and GvAbf Q90H/L307S) were selected, purified, partially characterized, and structurally analyzed. The specific activities of both variants were almost 2.5-fold more than that of GvAbf. Both GvAbf variants also exhibited higher thermal stability but lower alkaline stability in reference to GvAbf. The structural analysis of GvAbf model indicated that two mutation sites Q90H and L307S in both GvAbf variants are located in TIM barrel domain, responsible for catalytic action in many Glycoside Hydrolase Families including GH51. The structure of GvAbf model displayed that the position of L307S mutation is closer to the catalytic residues of GvAbf compared with Q90H mutation and also L307S mutation is conserved in both variants of GvAbf. Therefore, it was hypothesized that L307S amino acid substitution may play a critical role in catalytic activity of GvAbf. (C) 2018 International Union of Biochemistry and Molecular Biology, Inc.Article Citation - WoS: 38Citation - Scopus: 43Characterization and Performance Evaluation of Pt[sbnd]ru/C[sbnd]tio2 Anode Electrocatalyst for Dmfc Applications(Elsevier Ltd., 2017) Erçelik, Mustafa; Özden, Adnan; Şeker, Erol; Çolpan, C. ÖzgürIn this study, the effect of introduction of titania (TiO2) material into Pt[sbnd]Ru/C anode electrocatalyst on the performance of direct methanol fuel cells (DMFCs) was investigated. TiO2 materials were first synthesized applying a sol–gel method and then incorporated directly into commercial Pt[sbnd]Ru/C anode electrocatalyst with different TiO2 weight ratios (5, 15, and 25 wt.%) to improve the performance of the DMFC. For comparison, the anode electrocatalysts with the same TiO2 weight ratios were also prepared using commercial TiO2 materials. The performance tests of the DMFCs based on these composite anode electrocatalysts were conducted and their performances were also compared to that of a DMFC based on a traditional anode electrocatalyst (Pt[sbnd]Ru/C) under various operating conditions. In addition, 4 h short-term stability tests were conducted for all the manufactured DMFCs. The highest power densities were found as 705.12 W/m2 and 709.32 W/m2 at 80 °C and 1 M for the DMFCs based on Pt[sbnd]Ru/C[sbnd]TiO2 anode electrocatalysts containing 5 wt.% of commercial and in-house TiO2, respectively. The results of the short-term stability tests showed that introduction of 5 wt.% of commercial TiO2 into commercial Pt[sbnd]Ru/C anode electrocatalyst improved its stability characteristics significantly.Article Citation - WoS: 73Citation - Scopus: 78Functional Analysis of Free Methionine-R Reductase From Saccharomyces Cerevisiae(American Society for Biochemistry and Molecular Biology, 2009) Le, Dung Tien; Lee, Byung Cheon; Marino, Stefano M.; Zhang, Yan; Fomenko, Dmitri E.; Kaya, Alaattin; Hacıoğlu, Elise; Kwak, Geun-Hee; Koç, Ahmet; Kim, Hwa-Young; Gladyshev, Vadim N.Methionine sulfoxide reductases (Msrs) are oxidoreductases that catalyze thiol-dependent reduction of oxidized methionines. MsrA and MsrB are the best known Msrs that repair methionine S-sulfoxide (Met-S-SO) and methionine-R-sulfoxide (Met-R-SO) residues in proteins, respectively. In addition, an Escherichia coli enzyme specific for free Met-R-SO, designated fRMsr, was recently discovered. In this work, we carried out comparative genomic and experimental analyses to examine occurrence, evolution, and function of fRMsr. This protein is present in single copies and two mutually exclusive subtypes in about half of prokaryotes and unicellular eukaryotes but is missing in higher plants and animals. A Saccharomyces cerevisiae fRMsr homolog was found to reduce free Met-R-SO but not free Met-S-SO or dabsyl-Met-R-SO. fRMsr was responsible for growth of yeast cells on Met-R-SO, and the double fRMsr/MsrA mutant could not grow on a mixture of methionine sulfoxides. However, in the presence of methionine, even the triple fRMsr/MsrA/MsrB mutant was viable. In addition, fRMsr deletion strain showed an increased sensitivity to oxidative stress and a decreased life span, whereas overexpression of fRMsr conferred higher resistance to oxidants. Molecular modeling and cysteine residue targeting by thioredoxin pointed to Cys101 as catalytic and Cys125 as resolving residues in yeast fRMsr. These residues as well as a third Cys, resolving Cys91, clustered in the structure, and each was required for the catalytic activity of the enzyme. The data show that fRMsr is the main enzyme responsible for the reduction of free Met-R-SO in S. cerevisiae.Article Citation - WoS: 88Citation - Scopus: 108Biomimetic Co2 Sequestration: 1. Immobilization of Carbonic Anhydrase Within Polyurethane Foam(American Chemical Society, 2009) Özdemir, EkremBovine carbonic anhydrase (CA) was immobilized within polyurethane (PU) foam for biomimetic CO2 sequestration. The catalytic activities for the free and immobilized CA were estimated using paranitrophenyl acetate (p-NPA) as the substrate. Because the p-NPA has limited solubility in the aqueous phase, the activities were estimated in Tris buffer containing 10% acetonitrile. A Lineweaver-Burk relationship was employed to estimate the Michaelis-Menten kinetic parameters for the free and immobilized CA. The kcat, K m, and kcat/Km values for the free CA were found to be 2.02 s-1, 12.2 mM, and 166.4M-1 s-1, respectively. The Km value for the immobilized CA was estimated to be 9.6mMat the same conditions. The immobilized CA was stable and did not lose any activity over seven consecutive washings and activity tests. While the free CA lost its activity in 45 days stored at 4 °C in refrigerator, the immobilized CA maintained 100% of its activity over a 45 day period stored in Tris buffer at ambient conditions. It was concluded that the immobilized CA as a very stable biocatalyst could be employed in biomimetic CO2 sequestration.