A novel enzyme-immobilization method for a biofuel cell
- Authors
- Lee, Jin Young; Shin, Hyun Yong; Lee, Jong Ho; Song, Yoon Seok; Kang, Seong Woo; Park, Chulhwan; Kim, Jung Bae; Kim, Seung Wook
- Issue Date
- 8월-2009
- Publisher
- ELSEVIER
- Keywords
- beta-Nicotinamide adenine dinucleotide; Pyrroloquinoline quinone; Lactate dehydrogenase; Immobilization; Enzyme stability
- Citation
- JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, v.59, no.4, pp.274 - 278
- Indexed
- SCIE
SCOPUS
- Journal Title
- JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
- Volume
- 59
- Number
- 4
- Start Page
- 274
- End Page
- 278
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/119556
- DOI
- 10.1016/j.molcatb.2008.10.008
- ISSN
- 1381-1177
- Abstract
- Biofuel cells utilizing biocatalysts are attractive alternatives to metal catalyst-based cells because of environmentally friendly cells and their renewability and good operations at room temperatures, even though they provide a low level of electrical power. In this study, the effect of a novel enzyme immobilization method on anodic electrical properties was evaluated under ambient conditions for increasing the power of an enzyme-based biofuel cell. The anodic system employed in the cell contained a gold electrode, pyrroloquinoline quinone (PQQ) as the electron transfer mediator, lactate dehydrogenase (LDH), P-nicotinamide adenine dinucleotide (NAD(+)) as the cofactor, and lactate as the substrate. The anodic electrical properties increased as a result of the novel enzyme-immobilization method. Furthermore, lactate, NAD(+), or CaCl2, which can all influence enzyme activation, were used to prevent covalent bond formation near the active site of the LDH during enzyme-immobilization. Protection of the active site of the LDH using this novel enzyme-immobilization method increased its stability, which enabled to increase power production (142 mu W/cm(2)) in a basic enzymatic fuel cell (EFC). (C) 2008 Elsevier B.V. All rights reserved.
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