Please use this identifier to cite or link to this item: http://hdl.handle.net/10603/424969
Title: Development of Small Scale Alcohol Biofuel Cells using Enzymes as Catalyst
Researcher: Das, Priyanki
Guide(s): Goswami, Pranab
Keywords: Energy and Fuels
Engineering and Technology
Material Science
University: Indian Institute of Technology Guwahati
Completed Date: 2021
Abstract: The major objective of the present study is to develop small-scale alcohol fuel-based enzymatic biofuel cells (EFCs) for power generation and alcohol biosensing applications using alcohol oxidase (AOx) as anodic catalyst. One of the key approaches we propose to develop the small-scale EFCs is to exclude external pumping system from fabricating the devices. To make the idea effective, we introduce natural cellulosic materials (cotton or papers) in the device fabrications to deliver the fuel to the bioanode through passive diffusion activity. An additional important objective of the present work is to develop a biocompatible conductive ink with high aqueous stability for fabrication of the bioelectrodes, as these are vital properties of an ink to harvest stable bioelectrocatalytic function of the redox enzymes on the electrode surfaces. We studied some biopolymers and eventually identified silk-sericin and polyethylene glycol (PEG) as suitable materials for developing a graphite-based conductive ink in a ratio of 0.03:2.0:1.0 for sericin:PEG:graphite. Interestingly, sericin facilitates transformation of amorphous graphite powder to a crystalline form in PEG environment that improved the conductivity of the ink (11.2 mS.cm-1) by 5.6-folds from the ink devoid of sericin. The viscosity and shear rate values of the ink were calculated as 0.11 Pa.s and 100s-1, respectively, thermos-stability up to 100 0C, and heat of formation (and#916;Hf) -4.204 KJ/g. In addition, the ink coated over newlinepaper surface retains high aqueous stability and the reason being recognized as the enhancement of and#946; sheets content of sericin by 2.8% upon mixing it with PEG. Then we moved towards the selection of a cathodic enzyme and used laccase for the same.
Pagination: Not Available
URI: http://hdl.handle.net/10603/424969
Appears in Departments:SCHOOL OF ENERGY SCIENCE AND ENGINEERING

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