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PublicationProcess Biochemistry
Year2019
Volume85
Pages97-105
International

Tuning dimeric formate dehydrogenases reduction/oxidation activities by immobilization

Authors:Roberto Fernandez-Lafuente
Groups of research:Optimization of biocatalysts and bioprocesses
Deniz Yildirima, Dilek Alagöz*b, Ali Toprakc, Seyhan Tükelc, Roberto Fernandez-Lafuente*d
a Cukurova University, Ceyhan Vocational School, Adana, Turkey
b Cukurova University, Imamoglu Vocational School, Adana, Turkey
 c Cukurova University, Sciences & Letters Faculty, Chemistry Department, 01330, Adana, Turkey
d Departamento de Biocatalisis. ICP-CSIC. C/Marie Crue 2. Campus UAM-CSIC. Contoblanco. 28049, Madrid, Spain
 Three differently immobilized preparations of an enzyme extract from Candida boidinii containing a NAD+-dependent formate dehydrogenase (CbFDH) were prepared by  encapsulation using calcium alginate (CbFDH-Alg) or polyvinyl alcohol (CbFDH-PVA) or by  adsorption on montmorillonite K 10 (CbFDH-Mont). All FDH preparations were  characterized in terms of both oxidation and reduction activities. For the formic oxidation  activity, all immobilized FDHs had 100% activity at pH 8.0 and 50 °C, as the soluble enzyme.  Among the immobilized biocatalyst, only CbFDH-PVA showed activity in the reduction of  hydrogen carbonate and had 100% activity at pH 6.0 and 40°C, as the soluble enzyme. The  half-life values of immobilized enzymes increased by at least 3.1-folds compared to the  soluble enzyme. Formic acid was produced from HCO3- as a source of carbon dioxide using soluble CbFDH and CbFDH-PVA and the formic acid yields were determined as 80 and 92%, respectively for soluble CbFDH and CbFDH-PVA after 240 min reaction. CbFDH-Alg,  CbFDH-PVA and CbFDH-Mont retained 40.1, 49.8 and 26.1% of their initial activities after  10 reuses in formate oxidation reaction. The remaining reduction activity of CbFDH-PVA  was 30% after 10 reuses. These results show the CbFDH immobilization following different  protocols strongly alter their oxidation/reduction activities.
 
Keywords:Immobilization, multimeric enzymes, Formate dehydrogenase, enzyme properties tuning, formate oxidation, CO2 reduction
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