Journal
COLLOIDS AND SURFACES B-BIOINTERFACES
Volume 200, Issue -, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.colsurfb.2021.111606
Keywords
Cyclodextrin; Mesoporous silica; Sober process; Enzyme; Biocatalysis; 2-diformyfuran; 2; 5-furandicarboxylic acid
Funding
- Chevreul Institute [FR 2638]
- Ministere de l'Enseignement Superieur, de la Recherche et de l'Innovation
- FEDER
- Region Hauts-de-France
- University of Artois
- Conseil Regional des Hauts-de-France
- European Regional Development Fund (ERDF)
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The study successfully prepared mesoporous silica with tunable pore size by using RaMe8CD as a template in the fabrication of silica particles, demonstrating effective immobilization of enzymes. Incorporation of CALB within the pores of RaMe8CD-derived silica led to almost two-fold increase in specific activity, as well as enhanced operational stability during recycling experiments. These findings pave the way for future research on the use of cyclodextrins in the development of enzyme-based nanoreactors.
Hypothesis: Porous silica has been extensively used as suitable carrier for the immobilization of various enzymes. Randomly Methylated 8-Cyclodextrin (RaMe8CD) has surface active properties and very high solubility in water and could therefore be used as template in the fabrication of silica particles with tunable pore size. Experiments: Silica particles were prepared by sol-gel process in alkaline medium with and without use of RaMe8CD. Lipase Bfrom Candida antarctica (CALB) was either incorporated within the pores of RaMe8CD-derived support or covalently attached on the surface of CD-free silica particles and its catalytic performance was assayed in the oxidation of 2,5-diformylfuran (DFF) to 2,5-furandicarboxylic acid (FDCA). Enzymatic reactors were characterized by N2-adsorption analysis, small angle XRD, TG/DSC experiments, ATR-FTIR spectroscopy, HRTEM and LSCM, while reaction products were determined based on 1H NMR spectroscopy combined with HPLC. Findings: Results showed that the use of RaMe8CD as structure directing agent led to mesoporous silica composed of uniform 8 nm-sized particles with 11 nm-sized mesopores compatible with the dimensions of CALB (3.0 nm ? 4.0 nm ? 5.0 nm). Incorporation of CALB within the pores of RaMe8CD-derived silica caused almost a two-fold increase in specific activity after 7 h at 40 ?C when compared to lipase immobilized on the surface of CD-free silica particles (33.2 ?mol g-1 min- 1vs. 14.4 ?mol g-1 min-1). Moreover, the RaMe8CD-derived biocatalyst demonstrated enhanced operational stability during the recycling experiments, retaining more than 90% of its initial activity after five 24 h-reaction cycles. These findings open up new avenues for future research on the use of cyclodextrins in the development of enzyme-based nanoreactors.
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