Novel nanohybrid biocatalyst: application in the kinetic resolution of secondary alcohols

Autor:	L. R. B. Golçalves, J. C. S. dos Santos, Felipe Bohn, M. C. de Mattos, Thiago de Sousa Fonseca, Bruna B. Pinheiro, Wesley dos Santos Galvão, Marcio Assolin Correa, Pierre Basílio Almeida Fechine, Davila Zampieri, Luelc S. Costa, T. Regis
Rok vydání:	2018
Předmět:	Materials science Immobilized enzyme biology 010405 organic chemistry Mechanical Engineering 02 engineering and technology Buffer solution 021001 nanoscience & nanotechnology 01 natural sciences 0104 chemical sciences Kinetic resolution chemistry.chemical_compound chemistry Mechanics of Materials Biocatalysis biology.protein General Materials Science Lipase Enantiomer 0210 nano-technology Enantiomeric excess Selectivity Nuclear chemistry
Zdroj:	Journal of Materials Science. 53:14121-14137
ISSN:	1573-4803 0022-2461
DOI:	10.1007/s10853-018-2641-5
Popis:	In this work, a nanohybrid material was developed and used for the first time to the kinetic resolution of secondary alcohols as rac-indanol, rac-1-phenylethanol (rac-1), rac-1-(3-bromophenyl)-1-ethanol (rac-2) and rac-1-(3-methylphenyl)-1-ethanol (rac-3). Chiral indanol is used as a precursor intermediate for the synthesis of enantiomeric drugs, such as (+)-Indatraline, Irindalone, Indinavir, (+)-Sertraline and Rasagiline mesylate. Chiral 1-phenylethanol is used as an ophthalmic preservative, a solvatochromic dye and an inhibitor of cholesterol absorption and as a mild floral fragrance. For this purpose, the ultrasound irradiation was used to couple APTES on the superparamagnetic nanoparticles surface. Then, the system was activated with glutaraldehyde and used as a support for immobilization of lipase from Pseudomonas fluorescens. Thermal stability analysis was performed in buffer and hexane, showing an excellent stability in buffer solution at 60 °C, holding 72% of the initial activity, even after 7 h. In hexane (40 °C), the immobilized enzyme retained 100% of activity with 693 min of half-life time at 50 °C. The high thermal stability is mainly related to the covalent bonding between enzymes and support. Immobilized lipase on magnetic support proved to be a robust biocatalyst in the kinetic resolution, leading to (S)-indanol with high selectivity (e.e. > 99%, E > 200) in 1.75 h at 50 °C, being reused five times without significant loss of the activity and selectivity. The kinetic resolution of rac-1, via acetylation reaction, catalyzed by lipase from Pseudomonas fluorescens immobilized on magnetic support, led to (R)-acetate with enantiomeric excess > 99% and to the remaining (S)-alcohol with enantiomeric excess of 94%, conversion of 49% and E > 200, after 48 h of reaction at 40 °C. Under the same reactions conditions, rac-2 and rac-3 were slightly less reactive, since the corresponding (R)-acetates were obtained with conversion values of 44%, but with high enantioselectivity (enantiomeric excesses > 99% and E values > 200). These results correspond to an important step in heterogeneous catalysis due to the ability to obtain important precursors for the synthesis of enantiomerically pure chiral drugs and other bioactive substances.
Databáze:	OpenAIRE
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