Immobilization of Pyrroloquinoline Quinone-Dependent Alcohol Dehydrogenase with a Polyion Complex and Redox Polymer for a Bioanode

A bioanode for ethanol oxidation was prepared by immobilizing the recombinant pyrroloquinoline quinone (PQQ)-dependent alcohol dehydrogenase from Pseudomonas putida KT 2440 (PpADH) with polyion complex (PIC) and redox polymer. The PIC based on poly-l-lysine (PLL) and poly-l-glutamic acid (PGA) was s...

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Main Authors: Yuki Sakurada, Kouta Takeda, Hiroyuki Ohno, Nobuhumi Nakamura
Format: Article
Language:English
Published: MDPI AG 2017-10-01
Series:Catalysts
Subjects:
Online Access:https://www.mdpi.com/2073-4344/7/10/296
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spelling doaj-c4359b233ff442529f15c115980933932020-11-24T23:08:34ZengMDPI AGCatalysts2073-43442017-10-0171029610.3390/catal7100296catal7100296Immobilization of Pyrroloquinoline Quinone-Dependent Alcohol Dehydrogenase with a Polyion Complex and Redox Polymer for a BioanodeYuki Sakurada0Kouta Takeda1Hiroyuki Ohno2Nobuhumi Nakamura3Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-24-16 Nakacho, Koganei, Tokyo 184-8588, JapanDepartment of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-24-16 Nakacho, Koganei, Tokyo 184-8588, JapanDepartment of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-24-16 Nakacho, Koganei, Tokyo 184-8588, JapanDepartment of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-24-16 Nakacho, Koganei, Tokyo 184-8588, JapanA bioanode for ethanol oxidation was prepared by immobilizing the recombinant pyrroloquinoline quinone (PQQ)-dependent alcohol dehydrogenase from Pseudomonas putida KT 2440 (PpADH) with polyion complex (PIC) and redox polymer. The PIC based on poly-l-lysine (PLL) and poly-l-glutamic acid (PGA) was suitable for immobilizing PpADH on the electrode. PpADH was immobilized using only one redox polymer, aminoferrocene, which was attached to the PGA backbone (PGA-AmFc) on the electrode. The anodic current density at 0.6 V (vs. Ag/AgCl) was 22.6 μA·cm−2. However, when the number of the cycles was increased, the catalytic current drastically decreased. PpADH was immobilized using PGA-AmFc and PIC on the electrode. The anodic current density at 0.5 V (vs. Ag/AgCl) was 47.3 μA·cm−2, and the performance maintained 74% of the initial value after five cycles. This result indicated that the combination of PIC and PGA-AmFc was suitable for the immobilization of PpADH on the electrode. In addition, the long-term stability and catalytic current density were improved by using the large surface area afforded by the gold nanoparticles.https://www.mdpi.com/2073-4344/7/10/296biofuel cellsquinoproteinspyrroloquinoline quinonealcohol dehydrogenasepolyion complexredox mediatorgold nanoparticles
collection DOAJ
language English
format Article
sources DOAJ
author Yuki Sakurada
Kouta Takeda
Hiroyuki Ohno
Nobuhumi Nakamura
spellingShingle Yuki Sakurada
Kouta Takeda
Hiroyuki Ohno
Nobuhumi Nakamura
Immobilization of Pyrroloquinoline Quinone-Dependent Alcohol Dehydrogenase with a Polyion Complex and Redox Polymer for a Bioanode
Catalysts
biofuel cells
quinoproteins
pyrroloquinoline quinone
alcohol dehydrogenase
polyion complex
redox mediator
gold nanoparticles
author_facet Yuki Sakurada
Kouta Takeda
Hiroyuki Ohno
Nobuhumi Nakamura
author_sort Yuki Sakurada
title Immobilization of Pyrroloquinoline Quinone-Dependent Alcohol Dehydrogenase with a Polyion Complex and Redox Polymer for a Bioanode
title_short Immobilization of Pyrroloquinoline Quinone-Dependent Alcohol Dehydrogenase with a Polyion Complex and Redox Polymer for a Bioanode
title_full Immobilization of Pyrroloquinoline Quinone-Dependent Alcohol Dehydrogenase with a Polyion Complex and Redox Polymer for a Bioanode
title_fullStr Immobilization of Pyrroloquinoline Quinone-Dependent Alcohol Dehydrogenase with a Polyion Complex and Redox Polymer for a Bioanode
title_full_unstemmed Immobilization of Pyrroloquinoline Quinone-Dependent Alcohol Dehydrogenase with a Polyion Complex and Redox Polymer for a Bioanode
title_sort immobilization of pyrroloquinoline quinone-dependent alcohol dehydrogenase with a polyion complex and redox polymer for a bioanode
publisher MDPI AG
series Catalysts
issn 2073-4344
publishDate 2017-10-01
description A bioanode for ethanol oxidation was prepared by immobilizing the recombinant pyrroloquinoline quinone (PQQ)-dependent alcohol dehydrogenase from Pseudomonas putida KT 2440 (PpADH) with polyion complex (PIC) and redox polymer. The PIC based on poly-l-lysine (PLL) and poly-l-glutamic acid (PGA) was suitable for immobilizing PpADH on the electrode. PpADH was immobilized using only one redox polymer, aminoferrocene, which was attached to the PGA backbone (PGA-AmFc) on the electrode. The anodic current density at 0.6 V (vs. Ag/AgCl) was 22.6 μA·cm−2. However, when the number of the cycles was increased, the catalytic current drastically decreased. PpADH was immobilized using PGA-AmFc and PIC on the electrode. The anodic current density at 0.5 V (vs. Ag/AgCl) was 47.3 μA·cm−2, and the performance maintained 74% of the initial value after five cycles. This result indicated that the combination of PIC and PGA-AmFc was suitable for the immobilization of PpADH on the electrode. In addition, the long-term stability and catalytic current density were improved by using the large surface area afforded by the gold nanoparticles.
topic biofuel cells
quinoproteins
pyrroloquinoline quinone
alcohol dehydrogenase
polyion complex
redox mediator
gold nanoparticles
url https://www.mdpi.com/2073-4344/7/10/296
work_keys_str_mv AT yukisakurada immobilizationofpyrroloquinolinequinonedependentalcoholdehydrogenasewithapolyioncomplexandredoxpolymerforabioanode
AT koutatakeda immobilizationofpyrroloquinolinequinonedependentalcoholdehydrogenasewithapolyioncomplexandredoxpolymerforabioanode
AT hiroyukiohno immobilizationofpyrroloquinolinequinonedependentalcoholdehydrogenasewithapolyioncomplexandredoxpolymerforabioanode
AT nobuhuminakamura immobilizationofpyrroloquinolinequinonedependentalcoholdehydrogenasewithapolyioncomplexandredoxpolymerforabioanode
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