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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

2016; Elsevier BV; Volume: 133; Linguagem: Inglês

10.1016/j.molcatb.2016.08.009

1873-3158

Nathália Saraiva Rios, Maísa Pessoa Pinheiro, José Cleiton Sousa dos Santos, Thiago de Sousa Fonseca, Lara Dias Lima, Marcos Carlos de Mattos, Denise Maria Guimarães Freire, Ivanildo José da Silva, Elena Rodríguez‐Aguado, Luciana Rocha Barros Gonçalves,

Electrochemical sensors and biosensors

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.