Effect of some redox mediators on FAD fluorescence of glucose oxidase from Penicillium adametzii LF F-2044.1

• Glucose oxidase (GOx) was purified from Penicillium adametzii LF F-2044.
• Interaction of several different redox mediators with GOx was determined and evaluated.
• GOx from P. adametzii was characterized by evaluation of FAD and FADH2 fluorescence spectra.

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.