Successful bi-enzyme stabilization for the biomimetic cascade transformation of carbon dioxide
- Authors
- Hwang, Ee Taek; Seo, Bo-Kuk; Gu, Man Bock; Zeng, An-Ping
- Issue Date
- 2016
- Publisher
- ROYAL SOC CHEMISTRY
- Citation
- CATALYSIS SCIENCE & TECHNOLOGY, v.6, no.19, pp.7267 - 7272
- Indexed
- SCIE
SCOPUS
- Journal Title
- CATALYSIS SCIENCE & TECHNOLOGY
- Volume
- 6
- Number
- 19
- Start Page
- 7267
- End Page
- 7272
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/90190
- DOI
- 10.1039/c6cy00783j
- ISSN
- 2044-4753
- Abstract
- 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.
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