Enzyme-substrate interaction based approach for screening electroactive microorganisms for Microbial Fuel Cell applications

Alcohol dehydrogenase (ADH) of A. aceti is one of the potential enzyme for biological fuel cell applications. The modeled structure of ADH of A. aceti and its validation has been reported. The docking investigations have been made to assess the catalytic activity of the modeled ADH. The experimental...

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Bibliographic Details
Published in:Indian journal of chemical technology 2017-01, Vol.24 (1), p.93-96
Main Authors: Krishnaraj, R Navanietha, Pal, Parimal
Format: Article
Language:English
Subjects:
Affinity
Binding
Biochemical fuel cells
Catalytic activity
Chemical technology
Docking
Microorganisms
Screening
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Summary:Alcohol dehydrogenase (ADH) of A. aceti is one of the potential enzyme for biological fuel cell applications. The modeled structure of ADH of A. aceti and its validation has been reported. The docking investigations have been made to assess the catalytic activity of the modeled ADH. The experimental results show that the modeled ADH of A. aceti has lowest binding affinity to its substrate when compared with the ADH structures of few other microorganisms. It indicates that the ADH of A. aceti has higher catalytic activity and better electrogenic activity. This study documents a computational procedure for screening electroactive microorganisms for biological fuel cell applications.
ISSN:0971-457X
0975-0991