Oxidation of 2,5-diformfylfuran to 2,5-furandicarboxylic acid catalyzed by Candida antarctica Lipase B immobilized in a cyclodextrin-templated mesoporous silica. The critical role of pore characteristics on the catalytic performance

Porous silica has been extensively used as suitable carrier for the immobilization of various enzymes. Randomly Methylated β-Cyclodextrin (RaMeβCD) surface active properties and very high solubility in water could therefore be template fabrication particles with tunable pore size. Silica were prepared by sol-gel process alkaline medium without use RaMeβCD. Lipase Bfrom Candida antarctica (CALB) was either incorporated within pores RaMeβCD-derived support or covalently attached on CD-free its catalytic performance assayed oxidation 2,5-diformylfuran (DFF) to 2,5-furandicarboxylic acid (FDCA). Enzymatic reactors characterized N2-adsorption analysis, small angle XRD, TG/DSC experiments, ATR-FTIR spectroscopy, HR-TEM LSCM, while reaction products determined based 1H NMR spectroscopy combined HPLC. Results showed that RaMeβCD structure directing agent led mesoporous composed uniform 8 nm-sized 11 mesopores compatible dimensions CALB (3.0 nm × 4.0 5.0 nm). Incorporation caused almost a two-fold increase specific activity after 7 h at 40 °C when compared lipase immobilized (33.2 μmol g−1 min−1vs. 14.4 min−1). Moreover, biocatalyst demonstrated enhanced operational stability during recycling retaining more than 90% initial five 24 h-reaction cycles. These findings open up new avenues future research cyclodextrins development enzyme-based nanoreactors.