Properties of native and hydrophobic laccases immobilized in the liquid-crystalline cubic phase on electrodes
(2007) In Journal of Biological Inorganic Chemistry 12(3). p.335-344- Abstract
- Both native Trametes hirsuta laccase and the same laccase modified with palmytic chains to turn it more hydrophobic were prepared and studied with cyclic voltammetry and Raman spectroscopy. Native laccase immobilized in the monoolein cubic phase was characterized with resonance Raman spectroscopy, which demonstrated that the structure at the "blue" copper site of the protein remained intact. The diamond-type monoolein cubic phase prevents denaturation of enzymes on the electrode surface and provides contact of the enzyme with the electrode either directly or through the mediation by electroactive probes. Direct electron transfer for both laccases incorporated into a lyotropic liquid crystal was obtained under anaerobic conditions, whereas... (More)
- Both native Trametes hirsuta laccase and the same laccase modified with palmytic chains to turn it more hydrophobic were prepared and studied with cyclic voltammetry and Raman spectroscopy. Native laccase immobilized in the monoolein cubic phase was characterized with resonance Raman spectroscopy, which demonstrated that the structure at the "blue" copper site of the protein remained intact. The diamond-type monoolein cubic phase prevents denaturation of enzymes on the electrode surface and provides contact of the enzyme with the electrode either directly or through the mediation by electroactive probes. Direct electron transfer for both laccases incorporated into a lyotropic liquid crystal was obtained under anaerobic conditions, whereas bioelectrocatalytic activity was shown only for the native enzyme. The differences in electrochemical behavior of native and hydrophobic laccase as well as possible mechanisms of direct and mediated electron transfers are discussed. The Michaelis constant for 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonate) diammonium salt (ABTS(2-)), K-M(app), and the maximal current, I-max, for the native enzyme immobilized onto the electrode were estimated to be 0.24 mM, and 5.3 mu A, respectively. The maximal current density and the efficiency of the catalysis, I (max)/K-M(app), were found to be 73 mu A cm(-2) and 208.2 mu A cm(-2) mM(-1), respectively, and indicated a high efficiency of oxygen electroreduction by the enzyme in the presence of ABTS(2-) in the cubic-phase environment. Rate constants were calculated to be 7.5 x 10(4) and 3.6 x 10(4) M-1 s(-1) for native and hydrophobic laccase, respectively. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/667517
- author
- Nazaruk, Ewa ; Michota, Agnieszka ; Bukowska, Jolanta ; Shleev, Sergey LU ; Gorton, Lo LU and Bilewicz, Renata
- organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- diammonium salt, oxygen reduction, 2, 2'-azinobis(3-ethylbenzothiazoline-6-sulfonate), laccase, voltammetry
- in
- Journal of Biological Inorganic Chemistry
- volume
- 12
- issue
- 3
- pages
- 335 - 344
- publisher
- Springer
- external identifiers
-
- wos:000245457700006
- scopus:34147138970
- ISSN
- 1432-1327
- DOI
- 10.1007/s00775-006-0193-7
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Analytical Chemistry (S/LTH) (011001004)
- id
- 06255b2d-2e82-40fd-8101-afb8beba1503 (old id 667517)
- date added to LUP
- 2016-04-01 12:37:48
- date last changed
- 2022-02-11 17:33:36
@article{06255b2d-2e82-40fd-8101-afb8beba1503,
abstract = {{Both native Trametes hirsuta laccase and the same laccase modified with palmytic chains to turn it more hydrophobic were prepared and studied with cyclic voltammetry and Raman spectroscopy. Native laccase immobilized in the monoolein cubic phase was characterized with resonance Raman spectroscopy, which demonstrated that the structure at the "blue" copper site of the protein remained intact. The diamond-type monoolein cubic phase prevents denaturation of enzymes on the electrode surface and provides contact of the enzyme with the electrode either directly or through the mediation by electroactive probes. Direct electron transfer for both laccases incorporated into a lyotropic liquid crystal was obtained under anaerobic conditions, whereas bioelectrocatalytic activity was shown only for the native enzyme. The differences in electrochemical behavior of native and hydrophobic laccase as well as possible mechanisms of direct and mediated electron transfers are discussed. The Michaelis constant for 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonate) diammonium salt (ABTS(2-)), K-M(app), and the maximal current, I-max, for the native enzyme immobilized onto the electrode were estimated to be 0.24 mM, and 5.3 mu A, respectively. The maximal current density and the efficiency of the catalysis, I (max)/K-M(app), were found to be 73 mu A cm(-2) and 208.2 mu A cm(-2) mM(-1), respectively, and indicated a high efficiency of oxygen electroreduction by the enzyme in the presence of ABTS(2-) in the cubic-phase environment. Rate constants were calculated to be 7.5 x 10(4) and 3.6 x 10(4) M-1 s(-1) for native and hydrophobic laccase, respectively.}},
author = {{Nazaruk, Ewa and Michota, Agnieszka and Bukowska, Jolanta and Shleev, Sergey and Gorton, Lo and Bilewicz, Renata}},
issn = {{1432-1327}},
keywords = {{diammonium salt; oxygen reduction; 2; 2'-azinobis(3-ethylbenzothiazoline-6-sulfonate); laccase; voltammetry}},
language = {{eng}},
number = {{3}},
pages = {{335--344}},
publisher = {{Springer}},
series = {{Journal of Biological Inorganic Chemistry}},
title = {{Properties of native and hydrophobic laccases immobilized in the liquid-crystalline cubic phase on electrodes}},
url = {{http://dx.doi.org/10.1007/s00775-006-0193-7}},
doi = {{10.1007/s00775-006-0193-7}},
volume = {{12}},
year = {{2007}},
}