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Journal article

Upgrading of biomass monosaccharides by immobilized glucose dehydrogenase and xylose dehydrogenase

From

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
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.

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