Journal
ENERGY & FUELS
Volume 34, Issue 8, Pages 10050-10058Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.energyfuels.0c01033
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Funding
- Ministry of Science and Technology of Taiwan [MOST-108-2221-E-005-026]
- Ministry of Education, Taiwan, R.O.C. under the Higher Education Sprout Project
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The real-world application of an enzyme-based biofuel cell (EBFC) requires the desirable immobilization of enzymes on the electrode surface, offering the feasibility of addressing its short lifetime and low-power density. Nevertheless, an efficient immobilization of enzymes strongly relies on the preferred scaffolding between the enzyme and the electrode. Accordingly, the development of a promising route to attain a tunable scaffold structure is urgently required. Herein, we present a facile and ecofriendly route for efficiently controlling the scaffold structure by investigating the interplay of tripolyphosphate (TPP), chitosan (CS), and Na. A series of glucose oxidase (GOx)-based anodic electrodes, GOx[CS/TPP]CC, GOx[CS/Na]CC, and GOx[CS/TPP/Na]CC, are synthesized using CS/TPP, CS/Na, and CS/TPP/Na as the scaffolding on carbon cloth (CC) followed by the immobilization of GOx for a comparative study of the microstructure, enzyme loading, and electrochemical property. It is revealed that the self-pumping EBFC, driven by capillary force, utilizing GOx[CS/TPP/Na]CC can deliver a higher peak power density (1.077 mW cm(-2)) than that utilizing GOx[CS/TPP]CC (0.776 mW cm(-2)) and GOx[CS/Na]CC (0.682 mW cm(-2)). The selfpumping EBFC utilizing GOx[CS/TPP/Na]CC can retain 89.2% of its beginning performance even after 240 h of testing, as compared with that utilizing GOx[CS/Na]CC (61.1%). This enhancement can be attributed to the formation of a desirable scaffold structure via the cross-linked CS/TPP matrices combined with Na polymers for the hybrid enzyme immobilization, simultaneously offering the capability of improving the enzyme-loading efficiency, facilitating the interaction between the surface electrode and the enzyme, and preventing the release of the enzyme during the cell operation.
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