한빛사논문
Hye-Jin Jo‡,a, Jun-Hong Kim‡,b, Ye-Na Kim‡,a, Pil-Won Seo‡,b, Chae-Yun Kima, Ji-Won Kimb, Han-na Yua, Huijin Cheona, Eun Yeol Leec, Jeong-Sun Kim*,b and Jin-Byung Park*,a
aDepartment of Food Science and Engineering, Ewha Womans University, Seoul 03760, Republic of Korea
bDepartment of Chemistry, Chonnam National University, Gwangju 61186, Republic of Korea
cDepartment of Chemical Engineering (Integrated Engineering), Kyung Hee University, Gyeonggi-do 17104, Republic of Korea
*Corresponding authors
‡These authors contributed equally to this work.
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.
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