Journal
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
Volume 133, Issue -, Pages 246-258Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molcatb.2016.08.009
Keywords
Modified SBA-15; Candida antarctica lipase B; Enzyme immobilization; Chemical modification
Funding
- CAPES (Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior)
- CNPq (Conselho Nacional de Desenvolvimento Cientifico e Tecnologico)
- FUNCAP (Fundacao Cearense de Apoio ao Desenvolvimento Cientifico e Tecnologico)
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A recombinant Candida antarctica lipase B expressed in Pichia pastoris (LIPB) was immobilized on pore expanded SBA-15 previously modified 3-amino-propyltriethoxysilane (APTES) and activated with two bifunctional reagents, glutaraldehyde (GA) or divinylsulfone (DVS), producing the biocatalysts: SBA-15-APTES-GA-LIPB and SBA-15-APTES-DVS-LIPB, respectively. After LIPB immobilization, both preparations were then modified with glutaraldehyde, producing the biocatalysts: SBA-15-APTES-GA-LIPB-GA, SBA-15-APTES-DVS-LIPB-DVS. Alternatively, LIPB was immobilized on SBA-15-APTES-DVS at pH 10.2 and the biocatalyst was named SBA-15-APTES-DVS-LIPB-pH10. The different biocatalysts were assayed to check the effect of the immobilization strategies on the stability and in the substrate specificity during the kinetic resolution of (R,S)-Phenylethyl acetate. The thermal stability of some new preparations were higher than LIPB adsorbed on SBA-15 (SBA-15-LIPB) and LIPB immobilized on Glyoxyl-agarose. High conversions in the enzymatic kinetic resolution were obtained (43-50%) for all biocatalysts studied. Regarding activity and stability, the SBA-15-APTES-DVS-LIPB-pH10 was the most successful strategy, since, in first cycle, the maximum conversion was obtained (50%), and the biocatalyst remained active and enantioselective even after five successive cycles. (C) 2016 Elsevier B.V. All rights reserved.
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