Zobrazeno 1 - 10
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pro vyhledávání: '"D. Zouraris"'
Autor:
A. Zerva, C. Pentari, A. Termentzi, A. H. P. America, D. Zouraris, S. K. Bhattacharya, A. Karantonis, G. I. Zervakis, E. Topakas
Publikováno v:
Biotechnology for Biofuels, Vol 14, Iss 1, Pp 1-16 (2021)
Abstract Background Laccases and laccase-like multicopper oxidases (LMCOs) oxidize a vast array of phenolic compounds and amines, releasing water as a byproduct. Their low substrate specificity is responsible for their tremendous biotechnological int
Externí odkaz:
https://doaj.org/article/60280550a87e432d8cee98b18019b013
Autor:
Christina Pentari, A. H. P. America, Anastasia Zerva, Aikaterini Termentzi, Antonis Karantonis, S. K. Bhattacharya, Evangelos Topakas, D. Zouraris, Georgios I. Zervakis
Publikováno v:
Biotechnology for Biofuels, Vol 14, Iss 1, Pp 1-16 (2021)
Biotechnology for Biofuels
Biotechnology for Biofuels, 14(1)
Biotechnology for Biofuels 14 (2021) 1
Biotechnology for Biofuels
Biotechnology for Biofuels, 14(1)
Biotechnology for Biofuels 14 (2021) 1
Background Laccases and laccase-like multicopper oxidases (LMCOs) oxidize a vast array of phenolic compounds and amines, releasing water as a byproduct. Their low substrate specificity is responsible for their tremendous biotechnological interest, si
Publikováno v:
Applied Sciences
Volume 11
Issue 11
Applied Sciences, Vol 11, Iss 4715, p 4715 (2021)
Volume 11
Issue 11
Applied Sciences, Vol 11, Iss 4715, p 4715 (2021)
Lytic polysaccharide monooxygenases (LPMOs) consist of a class of enzymes that boost the release of oxidised products from plant biomass, in an approach that is more eco-friendly than the traditional ones, employing harsh chemicals. Since LPMOs are r
Publikováno v:
Bioelectrochemistry. 124:149-155
MtLPMO9 and FoLPMO9 are two lytic polysaccharide monooxygenases (LPMOs), from the filamentous fungi Thermothelomyces thermophila and Fusarium oxysporum, respectively. In the present study an attempt has been made to achieve direct electron transfer b
Autor:
A. Zerva, C. Pentari, A. Termentzi, A. H. P. America, D. Zouraris, S. K. Bhattacharya, A. Karantonis, G. I. Zervakis, Topakas, E.
Additional file 1. Figure S1. 3rd Harmonic of (a) PcLac1 and (b) PcLac2. Experimental conditions: deaerated tartrate buffer pH 4.0 100 mM, T 43oC, v 50 mV/s, A 180 mV and f 6 (black), 9 (red), 12 (green) and 16 (blue) Hz. Figure S2. Possible products
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b1f5f447f52c0c381c98c3e39541ed7
Autor:
Evangelos Topakas, Pavlos K. Pandis, Chr. Argirusis, Antonis Karantonis, Anthi Karnaouri, D. Zouraris
Publikováno v:
Journal of Electroanalytical Chemistry. 897:115540
In this work, a lytic polysaccharide monooxygenase (LPMO) belonging to the AA9 family from the filamentous fungus Thermothelomyces thermophilus, MtLPMO9H, is immobilized on cobalt functionalized multi-walled carbon nanotubes modified glassy carbon el
Publikováno v:
Bioelectrochemistry. 118:19-24
The enzyme MtPerII is a new peroxidase which has been isolated only recently from fungus Myceliophthora thermophila and has significant thermostability and stability at high H2O2 concentrations. In the present work, an electrochemical kinetic study,
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Autor:
D. Zouraris, Antonis Karantonis
Publikováno v:
Journal of Electroanalytical Chemistry. 876:114729
In the present work, the derivation of the standard rate constant k0, the transfer coefficient a and the standard (or formal) potential E0 of immobilized electroactive species, with the use of large amplitude Fourier transform alternating current cyc
Publikováno v:
Bioelectrochemistry. 134:107538
In the present work, a kinetic analysis is made concerning the reaction of an electroactive immobilized enzyme with a free substrate, based on a Michaelis-Menten scheme. The proposed kinetic equations are investigated numerically for conditions descr