Modulation of lipase B from Candida antarctica properties via covalent immobilization on eco-friendly support for enzymatic kinetic resolution of rac-indanyl acetate

In this study, the modulation of enzymatic biocatalysts were developed by the use of lipase B fromCandida antarcticacovalently immobilized on an eco-friendly support, cashew apple bagasse, activated with 10% glycidol-ethylenediamine-glutaraldehyde (GEG) under different immobilization strategies (5 mM or 100 mM ionic strength and in absence or presence of 0.5% (v/v) Triton X-100). The biocatalysts were characterized for thermal and organic solvents stabilities and compared with the soluble enzyme. The biocatalysts were then applied to the hydrolysis of therac-indanyl acetate (2:1 ratio enzyme/substrate) at pH 7.0 and 30 degrees C for 24 h. For all the strategies evaluated, GEG promoted kinetic resolution ofrac-indanyl acetate with maximum conversion (50%) and led to (R)-indanol with excellent enantiomeric excess (97%), maintaining the maximum conversion for five consecutive cycles of hydrolysis. Therefore, the use of cashew apple bagasse has proved to be a promising eco-friendly support for enzyme immobilization, since it resulted in stable biocatalysts for enzymatic kinetic resolution. Graphic abstract