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PTFE-Carbon Nanotubes and Lipase B from Candida antarctica—Long-Lasting Marriage for Ultra-Fast and Fully Selective Synthesis of Levulinate Esters

ABSTRACT: An effective method for levulinic acid esters synthesis by the enzymatic Fischer esterification of levulinic acid using a lipase B from Candida antarctica (CALB) immobilized on the advanced material consisting of multi-wall carbon nanotubes (MWCNTs) and a hydrophobic polymer—polytetrafluoroethylene (Teflon, PTFE)—as a heterogeneous biocatalyst, was developed. An active phase of the biocatalyst was obtained by immobilization via interfacial activation on the surface of the hybrid material MWCNTs/PTFE (immobilization yield: 6%, activity of CALB: 5000 U∙L∙kg−1, enzyme loading: 22.5 wt.%). The catalytic activity of the obtained biocatalyst and the effects of the selected reaction parameters, including the agitation speed, the amount of PTFE in the CALB/MWCNT-PTFE biocatalyst, the amount of CALB/MWCNT-PTFE, the type of organic solvent, n-butanol excess, were tested in the esterification of levulinic acid by n-butanol. The results showed that the use of a two-fold excess of levulinic acid to n-butanol, 22.5 wt.% of CALB on MWCNT-PTFE (0.10 wt.%) and cyclohexane as a solvent at 20 °C allowed one to obtain n-butyl levulinate with a high yield (99%) and selectivity (>99%) after 45 min. The catalyst retained its activity and stability after three cycles, and then started to lose activity until dropping to a 69% yield of ester in the sixth reaction run. The presented method has opened the new possibilities for environmentally friendly synthesis of levulinate esters.

PROVIDER: S-EPMC8003637 | BioStudies |

REPOSITORIES: biostudies

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