Effect of some redox mediators on FAD fluorescence of glucose oxidase from Penicillium adametzii LF F-2044.1 |
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| Affiliation: | 1. Institute of Microbiology, Belarus National Academy of Sciences, Kuprevich str., 2, 220141 Minsk, Belarus;2. NanoTechnas – Center of Nanotechnology and Material Science, Department of Analytical and Environmental Chemistry, Faculty of Chemistry, Vilnius University, Naugarduko 24, 03225 Vilnius, Lithuania;3. Department of Physical Chemistry, Faculty of Chemistry, Vilnius University, Naugarduko 24, 03225 Vilnius, Lithuania;4. Laboratory of BioNanoTechnology, Department of Material Science and Electrical Engineering, Semiconductor Physics Institute, State Research Institute Center for Physical and Technological Sciences, A. Gostauto 11, LT-01108 Vilnius, Lithuania;1. Key Laboratory of Functional Inorganic Material Chemistry, Ministry of Education, School of Chemistry and Materials Science, Heilongjiang University, Harbin 150080, PR China;2. College of Environmental and Chemical Engineering, Heilongjiang University of Science and Technology, Harbin 150022, PR China;3. School of Mathematical Science, Heilongjiang University, Harbin 150080, PR China;1. Mater Research Institute, University of Queensland, Woolloongabba, Australia;2. Southern Medical University and Guangdong Genetic Testing Engineering Research Center, Guangzhou, China;3. Weatherall Institute of Molecular Medicine, Oxford, United Kingdom;4. Department of Pharmacy, University of Patras, Patras, Greece;5. Department of Biology, University of Vermont, Burlington, VT;6. Mount Sinai School of Medicine, New York, NY;7. Department of Cell Biology, Erasmus University Medical Center Rotterdam, Rotterdam, The Netherlands;1. Department of Physics, Jadavpur University, Kolkata 700032, India;2. Department of Physics, Sammilani Mahavidyalaya, E.M. Bypass, Baghajatin Station, Kolkata 700094, India;3. School of Laser Science and Engineering, Jadavpur University, Jadavpur, Kolkata 700032, India |
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| Abstract: | Glucose oxidase (GOx) of Penicillium adametzii LF F-2044.1 recovered by ultrafiltration, was characterized by spectrophotometric and spectrofluorometric methods. It was shown that spectra of GOx from P. adametzii are typical for flavoproteins. Optimal buffer composition was chosen. It was determined that the GOx is the most efficiently interacting with substrate (glucose) in phosphate buffer at pH 7.0 with kkat/KM = 15,217 ± 550 M−1 s−1. P. adametzii GOx fluorescence in the presence of different redox mediators (9,10-phenanthroline-5,6-dione, 9,10-phenanthrenequinone, 1,4-benzoquinone, methylene blue, ferrocene, ferrocenecarboxylic acid, α-methylferrocenemethanol, ferrocenecarboxaldehyde) was evaluated. Maximal differences in fluorescence emission intensity were observed in the presence of ferrocene and 9,10-phenanthrenequinone. |
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| Keywords: | Glucose oxidase Redox mediators Spectrofluorometric analysis 9,10-Phenanthrenequinone |
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