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

Ee Taek Hwang; Bo Kuk Seo; Man Bock Gu; An Ping Zeng

doi:10.1039/c6cy00783j

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

Ee Taek Hwang, Bo Kuk Seo, Man Bock Gu, An Ping Zeng

Department of Biotechnology

Research output: Contribution to journal › Article › peer-review

16 Citations (Scopus)

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.

Original language	English
Pages (from-to)	7267-7272
Number of pages	6
Journal	Catalysis Science and Technology
Volume	6
Issue number	19
DOIs	https://doi.org/10.1039/c6cy00783j
Publication status	Published - 2016

ASJC Scopus subject areas

Catalysis

Access to Document

10.1039/c6cy00783j

Cite this

@article{08988a93017c4246a3b13a70bec2e968,

title = "Successful bi-enzyme stabilization for the biomimetic cascade transformation of carbon dioxide",

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.",

author = "Hwang, {Ee Taek} and Seo, {Bo Kuk} and Gu, {Man Bock} and Zeng, {An Ping}",

note = "Funding Information: This work was supported by the National Research Foundation of Korea Grant funded by the Korean Government (MEST) (NRF-C1ABA001-2010-0020501), 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 and Future Planning (2015M1A5A1037055), and in part by the German Federal Ministry for Research and Education through the project Komparti (FKZ 031A174). Publisher Copyright: {\textcopyright} 2016 The Royal Society of Chemistry.",

year = "2016",

doi = "10.1039/c6cy00783j",

language = "English",

volume = "6",

pages = "7267--7272",

journal = "Catalysis Science and Technology",

issn = "2044-4753",

publisher = "Royal Society of Chemistry",

number = "19",

}

TY - JOUR

T1 - Successful bi-enzyme stabilization for the biomimetic cascade transformation of carbon dioxide

AU - Hwang, Ee Taek

AU - Seo, Bo Kuk

AU - Gu, Man Bock

AU - Zeng, An Ping

N1 - Funding Information: This work was supported by the National Research Foundation of Korea Grant funded by the Korean Government (MEST) (NRF-C1ABA001-2010-0020501), 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 and Future Planning (2015M1A5A1037055), and in part by the German Federal Ministry for Research and Education through the project Komparti (FKZ 031A174). Publisher Copyright: © 2016 The Royal Society of Chemistry.

PY - 2016

Y1 - 2016

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84989282203&partnerID=8YFLogxK

U2 - 10.1039/c6cy00783j

DO - 10.1039/c6cy00783j

M3 - Article

AN - SCOPUS:84989282203

SN - 2044-4753

VL - 6

SP - 7267

EP - 7272

JO - Catalysis Science and Technology

JF - Catalysis Science and Technology

IS - 19

ER -

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

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this