Strategies of covalent immobilization of a recombinant Candida antarctica lipase B on pore-expanded SBA-15 and its application in the kinetic resolution of ( R , S )-Phenylethyl acetate
| Autor: | Thiago de Sousa Fonseca, José C. S. dos Santos, Nathalia Saraiva Rios, Luciana Rocha Barros Gonçalves, Marcos Carlos de Mattos, Maísa Pessoa Pinheiro, Elena Rodríguez-Aguado, Ivanildo J. Silva, Denise M. G. Freire, Leandro Bezerra de Lima |
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| Rok vydání: | 2016 |
| Předmět: |
biology
010405 organic chemistry Process Chemistry and Technology Bioengineering 02 engineering and technology 021001 nanoscience & nanotechnology biology.organism_classification 01 natural sciences Biochemistry Catalysis 0104 chemical sciences Kinetic resolution Pichia pastoris chemistry.chemical_compound chemistry Biocatalysis Covalent bond Organic chemistry Candida antarctica Thermal stability Glutaraldehyde 0210 nano-technology Bifunctional |
| Zdroj: | Journal of Molecular Catalysis B: Enzymatic. 133:246-258 |
| ISSN: | 1381-1177 |
| DOI: | 10.1016/j.molcatb.2016.08.009 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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