Non-covalent and covalent immobilization of Candida antarctica lipase B on chemically modified multiwalled carbon nanotubes for a green acylation process in supercritical CO2

Abstract

• Efficient immobilization of Candida antarctica B lipase on modified MWCNTs. • Enzyme loading reaching as high as 21 wt.% for non-covalent immobilization. • Active O-acylation of geraniol into geranyl acetate by CAL-B in supercritical CO 2 . • Reaction regioselectivity unchanged through immobilization. • Development of a fully green enzymatic process. Candida antarctica B lipase (CAL-B) was immobilized on purified and functionalized multiwalled carbon nanotubes (MWCNTs). Both immobilization routes, physical adsorption and covalent bonding, were investigated. MWCNT functionalization by a non-aggressive oxidation by potassium permanganate led to an interesting balance between the hydrophilic and the hydrophobic areas of the MWCNT surface; the former being responsible of the good dispersion of MWCNTs in water and the latter having a favorable affinity with CAL-B. The enzyme loadings reached were significant: around 16 wt. % and 21 wt.% for non-covalent and covalent immobilization, respectively. The enzymatic activity was studied with the reaction of O-acylation of geraniol into geranyl acetate by CAL-B in supercritical CO 2 . Even if a decay in synthesis of geranyl acetate was observed over cycling for both CAL-B@MWCNT catalysts, it was demonstrated that the regioselectivity of CAL-B was unchanged through immobilization on the MWCNT surface for both routes. Interestingly, it was shown that a fully green enzymatic process can be achieved with these prepared CAL-B@MWCNT biocatalyst. Such approach could be transferred to other support/enzyme systems for developing new eco-friendly synthesis processes.