Journal article
Upgrading of biomass monosaccharides by immobilized glucose dehydrogenase and xylose dehydrogenase
Department of Chemical and Biochemical Engineering, Technical University of Denmark1
PROSYS - Process and Systems Engineering Centre, Department of Chemical and Biochemical Engineering, Technical University of Denmark2
Poznań University of Technology3
Department of Biotechnology and Biomedicine, Technical University of Denmark4
Section for Protein Chemistry and Enzyme Technology, Department of Biotechnology and Biomedicine, Technical University of Denmark5
Enzyme Technology, Section for Protein Chemistry and Enzyme Technology, Department of Biotechnology and Biomedicine, Technical University of Denmark6
Direct upgrading and separation of the monosaccharides from biomass liquors is an overlooked area. In this work we demonstrate enzymatic production of gluconic acid and xylonic acid from glucose and xylose present in pretreated birchwood liquor by glucose dehydrogenase (GDH, EC 1.1.1.118) and xylose dehydrogenase (XDH, EC 1.1.1.175), respectively.
The biocatalytic conversions were compared using two different kinds of silica support materials (silica nanoparticles (nanoSiO2) and porous silica particles with hexagonal pores (SBA silica) for enzyme immobilization. Upon immobilization, both enzymes showed significant improvement in their thermal stability and robustness at alkaline pH and exhibited over 50% activity even at pH 10 and 60°C on both immobilization matrices.
When compared to free enzymes at 45°C, GDH immobilized on nanoSiO2 and SBA silica displayed a 4.5 and 7.25 fold increase in half‐life, respectively, whilst XDH immobilized on nanoSiO2 and SBA showed a 4.7 and 9.5 fold improvement in half‐life, respectively. Additionally, after five reaction cycles both nanoSiO2GDH and nanoSiO2XDH retained more than 40% activity and GDH and XDH immobilized on SBA silica maintained around 50% of their initial activity resulting in about 1.5‐1.6 fold increase in biocatalytic productivity compared to the free enzymes.
Language: | English |
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Year: | 2018 |
Pages: | 5164-5173 |
ISSN: | 18673899 and 18673880 |
Types: | Journal article |
DOI: | 10.1002/cctc.201801335 |
ORCIDs: | 0000-0003-0268-2116 , Pinelo, Manuel and Meyer, Anne S. |