Glyoxylate carboligase-based whole-cell biotransformation of formaldehyde into ethylene glycol via glycolaldehyde

Hye Jin Jo, Jun Hong Kim, Ye Na Kim, Pil Won Seo, Chae Yun Kim, Ji Won Kim, Han Na Yu, Huijin Cheon, Eun Yeol Lee, Jeong Sun Kim, Jin Byung Park

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

A novel biocatalytic system for the synthesis of industrially relevant C2 chemicals (e.g., ethylene glycol (3)) from formaldehyde (1) was established. The biocatalytic system consisted of a newly discovered thermostable glyoxylate carboligase from Escherichia coli K-12 (EcGCL) and a lactaldehyde reductase (FucO) of E. coli K-12. EcGCL's affinity for formaldehyde was first improved by engineering the substrate access tunnel. One of the variants (i.e., EcGCLR484MN283QL478M) showed a high substrate affinity and catalytic efficiency of 18 mM and 5.2 M−1 s−1, respectively, for the condensation of two molecules of formaldehyde into one molecule of glycolaldehyde. The recombinant E. coli cells expressing both EcGCLR484MN283QL478M and FucO produced ethylene glycol (3) up to 6.6 mM from formaldehyde (1) with a bioconversion of 66% via glycolaldehyde (2), without leaving the reactants (1 and 2) in the reaction medium. This study demonstrated the biocatalytic synthesis of ethylene glycol from C1 compounds in an environment-friendly way.

Original languageEnglish
Pages (from-to)218-226
Number of pages9
JournalGreen Chemistry
Volume24
Issue number1
DOIs
StatePublished - 7 Jan 2022

Bibliographical note

Funding Information:
The X-ray diffraction experiments were performed with Beamline 11C at the Pohang Accelerator in Korea. This work was supported by C1 Gas Refinery Research Center (NRF grant number: 2018M3D3A1A01055735) of the National Research Foundation (NRF) of Korea funded by Ministry of Science and ICT. D. metallilatus genomic DNA was obtained from the Radiation Bio-Resources Bank (RBB) at KAERI Advance Radiation Technology Institute, Republic of Korea. We also thank Prof. Sunghoon Park (Pusan National University) for the kind donation of dhaT.

Publisher Copyright:
This journal is © The Royal Society of Chemistry

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