Earticle

초록

영어

Strategies for environmental-friendly reduction of CO2 to organic compounds have gained worldwide attention due to the growing consensus that increasing emissions of CO2 are causing global warming. The efficient utilization of CO2 will not only help to alleviate greenhouse effect, but also to obtain useful chemicals as well. In this work, biocatalytic reduction of CO2 by formate dehydrogenase (FDH) was investigated. In order to improve the catalytic stability of FDH, the enzyme was immobilized through cross-linked enzyme aggregates (CLEAs). The optimal conditions for the preparation of CLEAs were determined by changing kinds and concentration of cross-linker. Bovine serum albumin (BSA) was also used as a proteic feeder to increase the immobilization yield. The recovered activities of CLEAs were highly dependent on the concentration of glutaraldehyde, while the recovered activity was not severely influenced by the content of dextran polyaldehyde as a mild cross-linker. The recovered activity of CLEAs was about 18% under optimized conditions. The residual activity of FDH CLEAs cross-linked with dextran polyaldehyde (Dex-CLEAs) was over 95% after 10 times reuse. Thermal stability of Dex-CLEAs was 3.4 times enhanced compared with free enzyme. CLEAs of FDH could reduce CO2 to formate with very low reduction of activity after repeated use.

키워드

저자

• Min Hoo KIM [ Department of Microbial Engineering, Konkuk University, Seoul 143-701. ]
• Sang Hyun LEE [ Department of Microbial Engineering, Konkuk University, Seoul 143-701. ]

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간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576