Universidade Federal do Ceará
PPGEQ – Programa de Pós-graduação em Engenharia Química

The cashew apple bagasse (CAB), an agroindustrial wastes, was used as a support for the immobilizing of lipase kind B de Candida antarctica (CALB). After treatment with alkaline hydrogen peroxide (AHP), CAB-AHP was functionalized with glycidol (GLY), epichlorohydrin (EPI), glycidol – ethylenediamine- glutaraldehyde (GEG) 5% and 10% and then, characterized through analysis of the Scanning Electron microscopy (MEV) and Red Infra Fourier Transform (FTIR). The biocatalysts produced at pH 10 (25 mM, 25 °C, 0.5% Triton® X-100) and at pH 7 (5 mM, 100 mM, 25 °C, 0.5% Triton® X- 100), were characterized with respect to thermal stability, stability in the presence of organic solvents, pH relationship and hydrolytic activity. The derivatives were applied in the enzymatic kinetic resolution of rac-acetate indanila (30 °C, 24h, 250 rpm). The biocatalyst produced at pH 10.0, CAB-GLI and CAB-EPI showed high swelling and low catalytic activity (0.22 ± 0.19 U/g and 0.21 ± 0.22 U/g) respectively. The CABGEG 5%, in the presence and in the absence of 0.5% Triton® X-100, showed high catalytic activities (21.8 ± 0.52 U/g 38.8 ± 0.37 U/g) and high immobilization yields (95.1% and 97.1%), respectively. The longest times of half-life t1/2 were obtained under assay conditions at 60 °C and pH 5.0, 32.9 minutes for the immobilized prepared in the absence of Triton® X-100 and 29.8 minutes with addition of detergent. The stability in the presence of tetrahydrofuran solvent (THF) was best achieved when the derivative was prepared with addition of 0.5% Triton® X-100, showing t1/2 of 60 minutes. For the derivatives produced at pH 7.0, CAB- GEG 10% (5 mM) in the presence of detergent showed enzymatic activity of 29.62 ± 0 74 U/g. This derivative showed the best immobilization parameters in assays at pH 7.0. The most stable derivative at 60 °C showed t1/2 of 100.7 minutes (CAB- GEG 10%, 5 mM at pH 5.0). For the stabilities to organic solvents in the presence of tetrahydrofuran, the biocatalyst obtained in higher ionic strength conditions (100 mM) and in the presence of detergent was the most stable, t1/2 129.7 minutes. The derivatives were applied in the enzymatic kinetic resolution of rac-acetate indanol, showing high conversion values (50%). They can be applied in the production of intermediates used in drug formulations, such as Rasagiline Mesylate, indicated for the management of Parkinson’s disease.