A thermophilic-like ene-reductase originating from an acidophilic iron oxidizer

Anika Scholtissek*, Sophie R. Ullrich, Martin Mühling, Michael Schlömann, Caroline E. Paul, Dirk Tischler

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

13 Citations (Scopus)


Ene-reductases originating from extremophiles are gaining importance in the field of biocatalysis due to higher-stability properties. The genome of the acidophilic iron-oxidizing bacterium “Ferrovum” sp. JA12 was found to harbor a thermophilic-like ene-reductase (FOYE-1). The foye-1 gene was ligated into a pET16bp expression vector system, and the enzyme was produced in Escherichia coli BL21 (DE3; pLysS) cells in yields of 10 mg L−1. FOYE-1 showed remarkable activity and rates on N-phenylmaleimide and N-phenyl-2-methylmaleimide (up to 89 U mg−1, >97 % conversion, 95 % (R)-selective) with both nicotinamide cofactors, NADPH and NADH. The catalytic efficiency with NADPH was 27 times higher compared to NADH. At the temperature maximum (50 °C) and pH optimum (6.5), activity was almost doubled to 160 U mg−1. These findings accomplish FOYE-1 for a valuable biocatalyst in the synthesis of succinimides. The appearance of a thermophilic-like ene-reductase in an acidic habitat is discussed with respect to its phylogenetic placement and to the genomic neighborhood of the encoding gene, awarding FOYE-1 a putative involvement in a quorum-sensing process.

Original languageEnglish
Pages (from-to)609-619
Number of pages11
JournalApplied Microbiology and Biotechnology
Issue number2
Publication statusPublished - 1 Jan 2017


  • Biocatalysis
  • Extremophil
  • Ferrovum
  • Flavoprotein
  • Old yellow enzyme


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