TY - JOUR
T1 - Design of a synthetic enzyme cascade for the
T2 - In vitro fixation of a C1carbon source to a functional C4sugar
AU - Güner, Samed
AU - Wegat, Vanessa
AU - Pick, André
AU - Sieber, Volker
N1 - Publisher Copyright:
© The Royal Society of Chemistry.
PY - 2021/9/7
Y1 - 2021/9/7
N2 - Realizing a sustainable future requires intensifying the waste stream conversion, such as converting the greenhouse gas carbon dioxide into value-added products. In this paper, we focus on utilizing formaldehyde as a C1 carbon source for enzymatic C-C bond formation. Formaldehyde can be sustainably derived from other C1 feedstocks, and in this work, we designed a synthetic enzyme cascade for producing the functional C4 sugar erythrulose. This involved tailoring the enzyme formolase, which was optimized for fusing formaldehyde, from a three-carbon producer (dihydroxyacetone) to sets of variants with enhanced two-carbon (glycolaldehyde) or four-carbon (erythrulose) activity. To achieve this, a high-throughput combinatorial screening was developed, and every single variant was evaluated in terms of glycolaldehyde, dihydroxyacetone and erythrulose activity. By applying the two most promising variants in an enzyme cascade, we were able to show for the first time production of ERY starting from a C1 carbon source. In addition, we demonstrated that one of our tailored formolase variants was able to convert 25.0 g L-1 glycolaldehyde to 24.6 g L-1 erythrulose (98% theoretical yield) in a fully atom-economic biocatalytic process. This represents the highest achieved in vitro concentration of erythrulose to date.
AB - Realizing a sustainable future requires intensifying the waste stream conversion, such as converting the greenhouse gas carbon dioxide into value-added products. In this paper, we focus on utilizing formaldehyde as a C1 carbon source for enzymatic C-C bond formation. Formaldehyde can be sustainably derived from other C1 feedstocks, and in this work, we designed a synthetic enzyme cascade for producing the functional C4 sugar erythrulose. This involved tailoring the enzyme formolase, which was optimized for fusing formaldehyde, from a three-carbon producer (dihydroxyacetone) to sets of variants with enhanced two-carbon (glycolaldehyde) or four-carbon (erythrulose) activity. To achieve this, a high-throughput combinatorial screening was developed, and every single variant was evaluated in terms of glycolaldehyde, dihydroxyacetone and erythrulose activity. By applying the two most promising variants in an enzyme cascade, we were able to show for the first time production of ERY starting from a C1 carbon source. In addition, we demonstrated that one of our tailored formolase variants was able to convert 25.0 g L-1 glycolaldehyde to 24.6 g L-1 erythrulose (98% theoretical yield) in a fully atom-economic biocatalytic process. This represents the highest achieved in vitro concentration of erythrulose to date.
UR - https://www.scopus.com/pages/publications/85114348886
U2 - 10.1039/d1gc02226a
DO - 10.1039/d1gc02226a
M3 - Article
AN - SCOPUS:85114348886
SN - 1463-9262
VL - 23
SP - 6583
EP - 6590
JO - Green Chemistry
JF - Green Chemistry
IS - 17
ER -