Nanozeolites as support for laccase immobilization: Application to mediated glycerol oxidation

• Published in: Applied catalysis. A, General General, 2021-09, Vol.626, p.118361, Article 118361
• Main Authors: Miller, Alex Henrique, de Vasconcellos, Adriano, Fielding, Alistair John, Nery, José Geraldo
• Format: Article
• Language: English
• Subjects: Electron paramagnetic resonance; Enzymes; EPR; Glycerol; Immobilization; Laccase; Nanozeolites; Oxidation; Perturbation; Selectivity
• ISSN: 0926-860X; 1873-3875
• DOI: 10.1016/j.apcata.2021.118361

This study investigated the use of nanozeolites as support for laccases from P. ostreatus (LPO), Aspergillus sp (LAsp) and A. bisporus (LAB) immobilization applied to 2,2,6,6-tetramethylpiperidine-N-oxyl (TEMPO) mediated glycerol oxidation. Selected complexes led to up to 5% glycerol conversion, and interestingly, up to 100% selectivity to glyceraldehyde after 48 h. Free enzymes led to significantly higher yields (up to 82%) but lacked selectivity when tested under the same conditions. These findings suggest that laccases immobilized into nanozeolites are promising catalysts for the selective oxidation of glycerol. With the aim to understand the different behavior of free or immobilized enzymes, electron paramagnetic resonance (EPR) spectroscopy was applied. A significant shift of the T2 parallel copper hyperfine coupling constant was observed. This suggested a perturbation on the catalytic site after immobilization due to pH variation of the enzymatic microenvironments, thus influencing performance of laccase immobilized on nanozeolites. [Display omitted] •Nanozeolites were functionalized with amino silane groups and glutaraldehyde.•Higher activity of immobilized laccases over Cu2+ derivative zeolitic support.•High selectivity of glycerol conversion to glyceraldehyde using immobilized laccase.•High yield of glycerol conversion using free P. ostreatus laccase.•Immobilized laccases structural changes due to immobilization investigated by EPR.