The cofactor challenge in synthetic methylotrophy: Bioengineering and 
industrial applications

Krüsemann, Jan L; Rainaldi, Vittorio; Cotton, Charles AR; Claassens, Nico J; Lindner, Steffen N

doi:10.1016/j.copbio.2023.102953

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

The cofactor challenge in synthetic methylotrophy: Bioengineering and industrial applications

MPS-Authors

Krüsemann, Jan L
Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

External Resource

https://doi.org/10.1016/j.copbio.2023.102953
(Publisher version)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Krüsemann, J. L., Rainaldi, V., Cotton, C. A., Claassens, N. J., & Lindner, S. N. (2023). The cofactor challenge in synthetic methylotrophy: Bioengineering and industrial applications. Current Opinion in Biotechnology, 82: 102953. doi:10.1016/j.copbio.2023.102953.

Cite as: https://hdl.handle.net/21.11116/0000-000D-4BEF-3

Abstract

Methanol is a promising feedstock for industrial bioproduction: it can be produced renewably and has high solubility and limited microbial toxicity. One of the key challenges for its bio-industrial application is the first enzymatic oxidation step to formaldehyde. This reaction is catalysed by methanol dehydrogenases (MDH) that can use NAD+, O2 or pyrroloquinoline quinone (PQQ) as an electron acceptor. While NAD-dependent MDH are simple to express and have the highest energetic efficiency, they exhibit mediocre kinetics and poor thermodynamics at ambient temperatures. O2-dependent methanol oxidases require high oxygen concentrations, do not conserve energy and thus produce excessive heat as well as toxic H2O2. PQQ-dependent MDH provide a good compromise between energy efficiency and good kinetics that support fast growth rates without any drawbacks for process engineering. Therefore, we argue that this enzyme class represents a promising solution for industry and outline engineering strategies for the implementation of these complex systems in heterologous hosts.