Electrochemical Characterization of the Laccase-Catalyzed Oxidation of 2,6-Dimethoxyphenol: an Insight into the Direct Electron Transfer by Enzyme and Enzyme-Mediator System.

Autor: Mattos GJ; Centro de Ciências Exatas, Departamento de Química, Universidade Estadual de Londrina, Rodovia Celso Garcia Cid, PR 445, Km 380, Cx.P. 10.011, CEP: 86057-970, Londrina, PR, Brazil. gabriel.junquetti@uel.br., Schirmann JG; Centro de Ciências Exatas, Departamento de Química, Universidade Estadual de Londrina, Rodovia Celso Garcia Cid, PR 445, Km 380, Cx.P. 10.011, CEP: 86057-970, Londrina, PR, Brazil., Salamanca-Neto CAR; Centro de Ciências Exatas, Departamento de Química, Universidade Estadual de Londrina, Rodovia Celso Garcia Cid, PR 445, Km 380, Cx.P. 10.011, CEP: 86057-970, Londrina, PR, Brazil., Dekker RFH; Beta-Glucan Produtos Farmoquímicos EIRELI, Universidade Tecnológica Federal Do Paraná, Lote 24A, Bloco Zircônia, Câmpus Londrina, Avenida João Miguel Caram 731, CEP, Londrina, Paraná, 86036-700, Brazil., Barbosa-Dekker AM; Beta-Glucan Produtos Farmoquímicos EIRELI, Universidade Tecnológica Federal Do Paraná, Lote 24A, Bloco Zircônia, Câmpus Londrina, Avenida João Miguel Caram 731, CEP, Londrina, Paraná, 86036-700, Brazil., Sartori ER; Centro de Ciências Exatas, Departamento de Química, Universidade Estadual de Londrina, Rodovia Celso Garcia Cid, PR 445, Km 380, Cx.P. 10.011, CEP: 86057-970, Londrina, PR, Brazil. elensartori@uel.br.
Jazyk: angličtina
Zdroj: Applied biochemistry and biotechnology [Appl Biochem Biotechnol] 2022 Oct; Vol. 194 (10), pp. 4348-4361. Date of Electronic Publication: 2022 Feb 11.
DOI: 10.1007/s12010-022-03838-3
Abstrakt: The oxidation process of 2,6-dimethoxyphenol (2,6-DMP) by laccase from Botryosphaeria rhodina MAMB-05 and the corresponding enzyme-mediator systems was studied using cyclic voltammetry (CV). The enzyme was classified as a high oxidation potential laccase (> 0.70) V vs. NHE) based on its Redox potential at different pHs. The cyclic voltammograms for 2,6-DMP (- 58.7 mV pH -1 ) showed that its oxidation potential decreased more significantly compared to the enzyme (- 50.2 mV pH -1 ) by varying the pH. The 2,2'-azino-bis[3-ethyl-benzothiazoline-6-sulfonic acid] diammonium salt (ABTS) and 2,2,6,6-tetramethylpiperidine 1-oxyl radical (TEMPO) mediators were effectively oxidized by laccase from B. rhodina MAMB-05. The influence of laccase on the comproportionation of ABTS and the ionic step of the oxidation of TEMPO was also studied using CV. A higher potential difference was observed between laccase and the substrate, and correlated with higher enzyme activity. For the laccase-mediator systems, there was no clear correlation of potential difference between laccase and mediators with enzyme activity towards 2,6-DMP. This observation suggests that there are other limiting parameters for enzyme activity despite Redox potential difference, especially during ionic steps of the mechanism.
(© 2022. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.)
Databáze: MEDLINE
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