Abstract
Effective bio-electrocatalysts require stable immobilization of sufficient amounts of the bioactive component. In this study, a novel and efficient method for specific binding of laccase enzyme onto magnetite nanoparticles (NPs) is presented. The interaction between the chemically modified magnetite NPs and the enzyme was evidenced by both infrared (FT-IR) and X-ray photoelectron spectroscopy (XPS). Subsequently, the enzyme-coated magnetite NPs were successfully incorporated into polypyrrole (PPy) matrix during galvanostatic electropolymerization. The encapsulation of laccase covered NPs was proved by EQCN, TEM, and FT-IR spectroscopy; whereas the electrochemical behaviour of the formed bionanocomposite was characterized by cyclic voltammetry. In oxygen saturated solution a cathodic charge surplus was observed, related to the electrochemical reduction of oxygen. This surplus was two times higher in the case of the laccase containing layer compared to its only magnetite containing counterpart. Kinetic aspects of the oxygen reduction reaction (ORR) on the laccase containing films were investigated by hydrodynamic voltammetry, and the four-electron route was found to be exclusive, which is promising from the fuel cell perspective. Such synergistic combination of inorganic NPs and enzymes may open new avenues in the application of these bio-nanocomposite materials.
Original language | English |
---|---|
Pages (from-to) | 282-288 |
Number of pages | 7 |
Journal | Electrochimica Acta |
Volume | 122 |
DOIs | |
Publication status | Published - márc. 10 2014 |
Fingerprint
ASJC Scopus subject areas
- Electrochemistry
- Chemical Engineering(all)
Cite this
Fixation of laccase enzyme into polypyrrole, assisted by chemical interaction with modified magnetite nanoparticles : A facile route to synthesize stable electroactive bionanocomposite catalysts. / Endrodi, B.; Kormányos, A.; Janáky, C.; Berkesi, O.; Visy, C.
In: Electrochimica Acta, Vol. 122, 10.03.2014, p. 282-288.Research output: Article
}
TY - JOUR
T1 - Fixation of laccase enzyme into polypyrrole, assisted by chemical interaction with modified magnetite nanoparticles
T2 - A facile route to synthesize stable electroactive bionanocomposite catalysts
AU - Endrodi, B.
AU - Kormányos, A.
AU - Janáky, C.
AU - Berkesi, O.
AU - Visy, C.
PY - 2014/3/10
Y1 - 2014/3/10
N2 - Effective bio-electrocatalysts require stable immobilization of sufficient amounts of the bioactive component. In this study, a novel and efficient method for specific binding of laccase enzyme onto magnetite nanoparticles (NPs) is presented. The interaction between the chemically modified magnetite NPs and the enzyme was evidenced by both infrared (FT-IR) and X-ray photoelectron spectroscopy (XPS). Subsequently, the enzyme-coated magnetite NPs were successfully incorporated into polypyrrole (PPy) matrix during galvanostatic electropolymerization. The encapsulation of laccase covered NPs was proved by EQCN, TEM, and FT-IR spectroscopy; whereas the electrochemical behaviour of the formed bionanocomposite was characterized by cyclic voltammetry. In oxygen saturated solution a cathodic charge surplus was observed, related to the electrochemical reduction of oxygen. This surplus was two times higher in the case of the laccase containing layer compared to its only magnetite containing counterpart. Kinetic aspects of the oxygen reduction reaction (ORR) on the laccase containing films were investigated by hydrodynamic voltammetry, and the four-electron route was found to be exclusive, which is promising from the fuel cell perspective. Such synergistic combination of inorganic NPs and enzymes may open new avenues in the application of these bio-nanocomposite materials.
AB - Effective bio-electrocatalysts require stable immobilization of sufficient amounts of the bioactive component. In this study, a novel and efficient method for specific binding of laccase enzyme onto magnetite nanoparticles (NPs) is presented. The interaction between the chemically modified magnetite NPs and the enzyme was evidenced by both infrared (FT-IR) and X-ray photoelectron spectroscopy (XPS). Subsequently, the enzyme-coated magnetite NPs were successfully incorporated into polypyrrole (PPy) matrix during galvanostatic electropolymerization. The encapsulation of laccase covered NPs was proved by EQCN, TEM, and FT-IR spectroscopy; whereas the electrochemical behaviour of the formed bionanocomposite was characterized by cyclic voltammetry. In oxygen saturated solution a cathodic charge surplus was observed, related to the electrochemical reduction of oxygen. This surplus was two times higher in the case of the laccase containing layer compared to its only magnetite containing counterpart. Kinetic aspects of the oxygen reduction reaction (ORR) on the laccase containing films were investigated by hydrodynamic voltammetry, and the four-electron route was found to be exclusive, which is promising from the fuel cell perspective. Such synergistic combination of inorganic NPs and enzymes may open new avenues in the application of these bio-nanocomposite materials.
KW - Laccase
KW - Magnetite
KW - Nanocomposite
KW - Oxygen reduction reaction
KW - Polypyrrole
UR - http://www.scopus.com/inward/record.url?scp=84897607666&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84897607666&partnerID=8YFLogxK
U2 - 10.1016/j.electacta.2013.08.175
DO - 10.1016/j.electacta.2013.08.175
M3 - Article
AN - SCOPUS:84897607666
VL - 122
SP - 282
EP - 288
JO - Electrochimica Acta
JF - Electrochimica Acta
SN - 0013-4686
ER -