The Analysis of Enzyme Activity and Transcription Induced by Electrochemical Reducing Equivalent

The Analysis of Enzyme Activity and Transcription Induced by Electrochemical Reducing Equivalent
Issue Date
2012 한국화학공학회 추계학술대회
We previously reported reduced neutral red (NRred) by cathode enhanced butyrate production and decreased acetate production by C. tyrobutyricum in bioelectrochemical system (BES) (1). Electrochemically reducing equivalent increased NADH-consuming product but still it was not clear how extracellular electron donor modified its metabolic pathway. We investigated activity change of enzyme related with butyrate (3-hydroxybutyl-CoA dehydrogenase, butyrate kinase), acetate (phosphotransacetylase, acetate kinase) production with or without electricity. NADH-dependent 3-hydroxybutyl-CoA dehydrogenase increased 2.3 times but acetate kinase decreased up to 0.4 times in BES (cathode poised at -400 mV vs Ag/AgCl) than in control (no NR, no electricity). For the further study, we compared transcriptional differences between in these two conditions. The RNA was extracted after cell lysis and the level of transcription was analyzed by Illumina sequencing. The proteins having iron like 4Fe-4S ferredoxin, flavodoxin, iron-containing alcohol dehydrogenase were up-regulated. Also, FAD-related protein, stress-related, cell membrane modification-related, butyryl-CoA dehydrogenase, and NAD dependent oxidoreductase were highly regulated. Interestingly, the enzyme related with NAD+ biosynthesis was down-regulated like thiolase and ABC transporter. This study can help to investigate the study of electrofuel (2) and to understand how electrochemical reducing equivalent changes enzymes expression and its activity even though it was not fully analyzed yet.
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