Enantioselective catalysis from Pseudomonas cepacia on the kinetic resolution by different reactors

Enantioselective catalysis from Pseudomonas cepacia on the kinetic resolution by different reactors

Manoel*, Evelin A.; Coelho, Maria Alice Z.; Souza, Rodrigo O. M. A de; Simas, Alessandro B.C.; Freire, Denise M.G.

Abstract:

Enantioselective catalysis is an area of expertise that has been receiving increasingly attention. Its success depends on several factors, such as specificity of the biocatalyst, type of immobilization, substrate, solvent, and reactor systems. Currently, most of the studies in the literature report the use of reactors in small scale stirred tank on batch system. In this way, the phosphorylated myo-inositols appear as interesting substrates, to be studied due to their potential in the development of new drugs. The phosphorylated myo-inositols play key roles in fundamental biological phenomena such as cellular signal transduction. The present work aims at the use from immobilized Pseudomonas cepacia lipase on the efficient kinetic resolution of (±)-1,3,6-tri-O-benzil-myo-inositol (mio-I), a precursor known of 1D-2,4,5-myo-inositol trisphosphate4, a bioactive substance and a potential one for other inositol bisphosphates and trisphosphates. The biocatalytic continuous flow process and the batch process by alcoholysis reaction were investigated (Figure 1).

Enantioselective catalysis is an area of expertise that has been receiving increasingly attention. Its success depends on several factors, such as specificity of the biocatalyst, type of immobilization, substrate, solvent, and reactor systems. Currently, most of the studies in the literature report the use of reactors in small scale stirred tank on batch system. In this way, the phosphorylated myo-inositols appear as interesting substrates, to be studied due to their potential in the development of new drugs. The phosphorylated myo-inositols play key roles in fundamental biological phenomena such as cellular signal transduction. The present work aims at the use from immobilized Pseudomonas cepacia lipase on the efficient kinetic resolution of (±)-1,3,6-tri-O-benzil-myo-inositol (mio-I), a precursor known of 1D-2,4,5-myo-inositol trisphosphate4, a bioactive substance and a potential one for other inositol bisphosphates and trisphosphates. The biocatalytic continuous flow process and the batch process by alcoholysis reaction were investigated (Figure 1).

Palavras-chave:

DOI: 10.5151/chempro-15bmos-BMOS2013_201383123328

Referências bibliográficas

• [1] 1Manoel, E.A.; Paes, K.C.; Cunha, A.G.; Coelho, M.A.Z.; Freire, D.M.G. e Simas, A.B.C., Tetrahedron: Asymm., 2012, 23, 47.
• [2] 2Manoel, E.A., Pais, K.C., Flores, M.C., Miranda, L.S.M., Coelho, M.A.Z., Simas, A.B.C., Freire, D.M.G. e Souza, R.O.M.A. J. Mol.Cat. B: Enzym., 2013, 87, 139.
• [3] 3Boros, Z.; Falus, P.; Márkus, M.; Weiser, D.; Oláh, M.; Hornyánszky, G.; Nagy, J. e Poppea, L. J. Mol.Cat.B: Enzym., 2013, 85–86, 119.
• [4] 4Almeida, M.V., Silva, D.S., Souza, M.V.N. e Benício, A.A.A. Quim. Nova, 2003, 26, 105.
• [5] 5Oliveira, M.M.; Einicker-Lamas, M. Anais da Academia Brasileira de Ciências, Brasil, 2000, 72, 413.

Como citar:

Manoel*, Evelin A.; Coelho, Maria Alice Z.; Souza, Rodrigo O. M. A de; Simas, Alessandro B.C.; Freire, Denise M.G.; "Enantioselective catalysis from Pseudomonas cepacia on the kinetic resolution by different reactors", p-61-61. In: In Blucher Chemistry Proceedings, São Paulo, v. 1, n. 2, Dezembro.2013. São Paulo: Blucher, 2013.
ISSN 23184043, DOI 10.5151/chempro-15bmos-BMOS2013_201383123328