Fusion of pyruvate decarboxylase and alcohol dehydrogenase increases ethanol production in escherichia coli

Aleksandra J. Lewicka, Jan J. Lyczakowski, Gavin Blackhurst, Christiana Pashkuleva, Kyle Rothschild-Mancinelli, Dainius Tautvaišas, Harry Thornton, Hugo Villanueva, Weike Xiao, Justinas Slikas, Louise Horsfall, Alistair Elfick, Christopher French*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

Ethanol is an important biofuel. Heterologous expression of Zymomonas mobilis pyruvate decarboxylase (Pdc) and alcohol dehydrogenase (AdhB) increases ethanol production in Escherichia coli. A fusion of PDC and ADH was generated and expressed in E. coli. The fusion enzyme was demonstrated to possess both activities. AdhB activity was significantly lower when fused to PDC than when the two enzymes were expressed separately. However, cells expressing the fusion protein generated ethanol more rapidly and to higher levels than cells coexpressing Pdc and AdhB, suggesting a specific rate enhancement due to the fusion of the two enzymes.

Original languageEnglish
Pages (from-to)976-978
Number of pages3
JournalACS Synthetic Biology
Volume3
Issue number12
DOIs
Publication statusPublished - 1 Jan 2014

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