A proteomic analysis of ferulic acid metabolism in Amycolatopsis sp. ATCC 39116

  • Florian Meyer
  • Julius Netzer
  • Christina Meinert
  • Birgit Voigt
  • Katharina Riedel
  • Alexander Steinbüchel
Genomics, transcriptomics, proteomics
  • 36 Downloads

Abstract

The pseudonocardiate Amycolatopsis sp. ATCC 39116 is used for the biotechnical production of natural vanillin from ferulic acid. Our laboratory has performed genetic modifications of this strain previously, but there are still many gaps in our knowledge regarding its vanillin tolerance and the general metabolism. We performed cultivations with this bacterium and compared the proteomes of stationary phase cells before ferulic acid feeding with those during ferulic acid feeding. Thereby, we identified 143 differently expressed proteins. Deletion mutants were constructed and characterized to analyze the function of nine corresponding genes. Using these mutants, we identified an active ferulic acid β-oxidation pathway and the enzymes which constitute this pathway. A combined deletion mutant in which the β-oxidation as well as non-β-oxidation pathways of ferulic acid degradation were deleted was unable to grow on ferulic acid as the sole source of carbon and energy. This mutant differs from the single deletion mutants and was unable to grow on ferulic acid. Furthermore, we showed that the non-β-oxidation pathway is involved in caffeic acid degradation; however, its deletion is complemented even in the double deletion mutant. This shows that both pathways can complement each other. The β-oxidation deletion mutant produced significantly reduced amounts of vanillic acid (0.12 instead of 0.35 g/l). Therefore, the resulting mutant could be used as an improved production strain. The quinone oxidoreductase deletion mutant (ΔytfG) degraded ferulic acid slower at first but produced comparable amounts of vanillin and significantly less vanillyl alcohol when compared to the parent strain.

Keywords

Actinomycetes Amycolatopsis Proteome Vanillin Ferulic acid 

Notes

Acknowledgements

We thank Isabelle Plugge for excellent technical assistance. We also thank Robin Vivod and Kim Cohrs for helpful discussions and proofreading.

Funding

This paper was financially supported by King Abdulaziz University under Grant no. 2-10-1432/HiCi. The project was also partially funded by SYMRISE AG, Holzminden, Germany. SYMRISE AG had no role in study design, data collection and interpretation, or the decision to submit the work for publication.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Ethical approval

This article does not contain any studies with human participants or animals performed by any of the authors.

Supplementary material

253_2018_9061_MOESM1_ESM.pdf (513 kb)
ESM 1 (PDF 513 kb)

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Authors and Affiliations

  1. 1.Institut für Molekulare Mikrobiologie und BiotechnologieWestfälische Wilhelms-Universität MünsterMünsterGermany
  2. 2.Institut für MikrobiologieErnst-Moritz-Arndt UniversitätGreifswaldGermany
  3. 3.Environmental Sciences DepartmentKing Abdulaziz UniversityJeddahSaudi Arabia

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