Abstract
[Display omitted]
•CALB immobilized on (CAB) activated then 1h with a 90% immobilization yield.•High thermal stability of CAB-AHP derivatives at temperatures below 100°C.•The loading capacity of the new biocatalyst is around 10–11mg/g of support.•The biocatalyst was 10,000 times more stable than the soluble enzyme.•Biocatalyst is efficient in hydrolysis of rac-indanyl acetate, for 5 cycles.
Lipase B from Candida antarctica lipase expressed in Aspergillus niger has been covalently immobilized on cashew apple bagasse, and it stability and performance in the chemoenzymatic synthesis of (R)-Indanol has been evaluated. The cashew apple bagasse (CAB) has been treated with alkaline hydrogen peroxide and activated with glycidol (GLY) to obtain glyoxyl groups, in addition to ethylenediamine and further activation with glutaraldehyde (GEG).The maximum loading of the support was 10mg protein/g support, and its thermal and solvent stability was much higher than that of the soluble enzyme. The CAB-GEG preparation (with 95% yield of immobilization and 124% activity recovery) was used in the hydrolysis of ethyl rac-indanyl acetate using an enzyme/substrate ratio of 2: 1 and a pH value of 7.0 at 30°C for 24h. The conversion attained was 50% of conversion and e.e. of 99%. The reusability studies showed maintenance of conversion and e.e. during five cycles. The results suggest that the new CAB support may be an excellent alternative for lipase immobilization and stabilization.