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Enzymatic conversion of CO(2) to bicarbonate in functionalized mesoporous silica.


ABSTRACT: We report here a concept converting carbon dioxide to biocarbonate in a biomimetic nanoconfiguration. Carbonic anhydrase (CA), the fastest enzyme that can covert carbon dioxide to bicarbonate, can be spontaneously entrapped in carboxylic acid group-functionalized mesoporous silica (HOOC-FMS) with super-high loading density (up to 0.5 mg of protein/mg of FMS) in sharp contrast to normal porous silica. The binding of CA to HOOC-FMS resulted in a partial conformational change comparing to the enzyme free in solution, but it can be overcome with increased protein loading density. The higher the protein loading density, the less conformational change, hence the higher enzymatic activity and the higher enzyme immobilization efficiency (up to >60%). The released enzyme still displayed the native conformational structure and the same high enzymatic activity as that prior to the enzyme entrapment, indicating that the conformational change resulted from the electrostatic interaction of CA with HOOC-FMS was not permanent. This work may provide a new approach converting carbon dioxide to biocarbonate that can be integrated with the other part of biosynthesis process for the assimilation of carbon dioxide.

SUBMITTER: Yu Y 

PROVIDER: S-EPMC3266371 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature

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Enzymatic conversion of CO(2) to bicarbonate in functionalized mesoporous silica.

Yu Yuehua Y   Chen Baowei B   Qi Wen W   Li Xiaolin X   Shin Yongsoon Y   Lei Chenghong C   Liu Jun J  

Microporous and mesoporous materials : the official journal of the International Zeolite Association 20120501


We report here a concept converting carbon dioxide to biocarbonate in a biomimetic nanoconfiguration. Carbonic anhydrase (CA), the fastest enzyme that can covert carbon dioxide to bicarbonate, can be spontaneously entrapped in carboxylic acid group-functionalized mesoporous silica (HOOC-FMS) with super-high loading density (up to 0.5 mg of protein/mg of FMS) in sharp contrast to normal porous silica. The binding of CA to HOOC-FMS resulted in a partial conformational change comparing to the enzym  ...[more]

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