Successful bi-enzyme stabilization for the biomimetic cascade transformation of carbon dioxide

In nature, carbon dioxide (CO2) conversion to valuable chemicals occurs via several metabolic pathways through multi-enzymatic reactions. Here, we aimed to mimic this by introducing enzyme immobilization in microbead compartments forming a stabilized multi-enzyme system. The system is assembled by encapsulation of phosphoenolpyruvate carboxylase (PEPCase) in branched polymeric microbeads followed by carbonic anhydrase (CA) immobilization on the silica-shell surface of the microbeads. The step-by-step construction of the CA/PEPCase microbeads is monitored based on the stability of each enzyme and cascade enzymatic oxaloacetate (OAA) production rate from a CO2 substrate. Each CA and PEPCase in the microbeads preserved their catalytic activity even after 20 times of reuse, with facile magnetic separability at room temperature. The CA/PEPCase system retained about 75% of the OAA production rate of free CA/PEPCase by forming a multi-enzyme/microbead complex structure. To the best of our knowledge, this report is the first demonstration of a stabilized cascade CA/PEPCase system that mimics the biomimetic CO2 conversion by a multi-enzymatic pathway found in biological systems.

DDC Class

570: Biowissenschaften, Biologie

600: Technik

More Funding Information

Supported by the National Research Foundation of Korea Grant funded by the Korean Government (MEST) (NRF- 1ABA001-2010-0020501), in part by the Basic Core Technology Development Program for the Oceans and the Polar Regions of the National Research Foundation (NRF) funded by the Ministry of Science, ICT & Future Planning
(2015M1A5A1037055), and in part by the German Federal Ministry for Research and Education through the project
Komparti (FKZ 031A174).

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Successful bi-enzyme stabilization for the biomimetic cascade transformation of carbon dioxide