Tuning dimeric formate dehydrogenases reduction/oxidation activities by immobilization
| Autor: | S. Seyhan Tükel, Deniz Yildirim, Roberto Fernandez-Lafuente, Ali Toprak, Dilek Alagöz |
|---|---|
| Přispěvatelé: | Çukurova Üniversitesi |
| Rok vydání: | 2019 |
| Předmět: |
Calcium alginate
integumentary system Immobilized enzyme Formic acid Bioengineering Enzyme properties tuning Formate dehydrogenase Applied Microbiology and Biotechnology Biochemistry Redox Multimeric enzymes Formate oxidation Immobilization chemistry.chemical_compound chemistry CO2 reduction Biocatalysis Formate Nuclear chemistry |
| Zdroj: | Process Biochemistry. 85:97-105 |
| ISSN: | 1359-5113 |
| Popis: | 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. © 2019 Elsevier Ltd CTQ2017-86170-R Ministerio de Economía y Competitividad The authors thank to Dr. Baris Binay (Gebze Technical University) for the kind gift of the enzyme. We also gratefully recognize the support from the MINECO from Spanish Government, (project number CTQ2017-86170-R). The help and suggestions from Dr. Angel Berenguer (Departamento de Química Inorgánica, Universidad de Alicante) are gratefully recognized. |
| Databáze: | OpenAIRE |
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