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Year 2019, Issue: 5, 58 - 64, 21.06.2019

Abstract

References

  • Palomo, J.M., Fernández-Lorente, G., Segura, R.L., Ortiz, C., Fernandez-Lafuente, R., Guisán, J.M. Purification, immobilization, hyperactivation, and stabilization of lipases by selective adsorption on hydrophobic supports, in: J.M. Guisán (Ed.), Immobilization of Enzymes and Cells, Humana Press, New York, 2006, pp.143-152. Liu, Y.Y., Xu, J.H., Hu, H.Y., Shen, D. Integration of purification with immobilization of Candida rugosa lipase for kinetic resolution of racemic ketoprofen, J. Biotechnol. 110 (2004) 209-217. Torres, R., Ortiz, C., Pessela, B.C., Palomo, J.M., Mateo, C., Guisán, J.M., Fernandez-Lafuente, R. Improvement of the enantioselectivity of lipase (fraction B) from Candida Antarctica via adsorption on polyethylenimine-agarose under different experimental conditions., Enzyme. Microb. Technol. 39 (2006) 167-171. Palomo, J.M., Fernández-Lorente, G., Mateo, C., Ortiz, C., Fernandez-Lafuente, R., Guisán, J.M. Modulation of the enantioselectivity of lipases via controlled immobilization and medium engineering: hydrolytic resolution of mandelic acid esters, Enzyme. Microb. Technol. 31 (2002) 775-783. Miled, N., Beisson, F., de Caro, J., de Caro, A., Arondel, V., Verger, R. Interfacial catalysis by lipases, J. Mol. Catal. B: Enzym. 11 (2001) 165-171. Palomo, J.M., Fernández-Lorente, G., Mateo, C., Ortiz, C., Fernandez-Lafuente, R., Guisán, J.M. Interfacial adsorption of lipases on very hydrophobic support (octadecyl-sepabeads): immobilization, hyperactivation and stabilization of the open form of lipases, J. Mol. Cat. B: Enzym. 19-20 (2002) 279-286. Palomo, J.M., Fernández-Lorente, G., Mateo, C., Fuentes, M., Fernandez-Lafuente, R., Guisán, J.M. Conformational engineering of lipase from Candida antarctica B via directed immobilization and medium engineering. Hydrolysis of chiral mandelic acid esters, Tetrahed. Asymm. 13 (2002) 1337-1345. Oladepo, D.K., Halling, P.J., Larsen, V.F. Effect of different supports on the reaction rate of Rizomucor miehei lipase in organic media, Biocatal. Biotrans. 12 (1995) 47-54. Machado, A.C.O. Obtenção de intermediários quirais utilizando lipases em reatores assistidos por membranas. Doctoral Thesis. UFRJ – Universidade Federal do Rio de Janeiro, Faculdade de Engenharia Química, Rio de Janeiro, RJ – Brazil (2011). Cao, Y., Wu, S., Li, J., He, B. Highly efficient resolution of mandelic acid using lipase from Pseudomonas stutzeri LC2-8 and a molecular modeling approach to rationalize its enantioselectivity, J. Mol. Catal. B: Enzym. 99 (2014) 108-113. Yao, C.J., Cao, Y., Wu, S.S., Li, D., He, B.F. An organic solvent and thermally stable lipase from Burkholderia ambifaria YCJ01: Purification, characteristics and application for chiral resolution of mandelic acid, J. Mol. Catal. B: Enzym. 85-86 (2013) 105-110. Zingg, S.P., Arnett, E.M., McPhail, A.T., Bothner, A.A., Gilkerson, W.R. Chiral discrimination in the structures and energetics of association of stereoisomeric salts of mandelic acid with alpha.-phenethylamine, ephedrine, and pseudoephedrine, J. Am. Chem. Soc. 110 (1988) 1565-1580. Whitesell, J.K., Reynolds, D. Resolution of chiral alcohols with mandelic acid, J. Org. Chem. 48 (1983) 3548-3551. Yadav, G.D., Sivakumar, P. Enzyme-catalysed optical resolution of mandelic acid via (R,S)-methyl mandelate in non-aqueous media, Biochem. Eng. J. 19 (2004) 101-107. Morais Junior, W.G., Kamimura, E.S., Ribeiro, E.J., Pessela, B.C., Cardoso, V.L., Resende, M.M. Optimization of the production and characterization of lipase from Candida rugosa and Geotrichum candidum in soybean molasses by submerged fermentation, Protein. Express. Purif. 123 (2016) 26-34.

Immobilization of Candida rugosa Lipase on Different Ionic Supports to Improve the Enantioselectivity on Mandelic Acid Resolution

Year 2019, Issue: 5, 58 - 64, 21.06.2019

Abstract

This
work describes the improvement in enantioselectivity on the resolution of
mandelic acid catalyzed by the Candida
rugosa
lipase (CRL) immobilized and stabilized on two different ionic
supports. CRL was quickly immobilized on anionic diethylaminoethyl (DEAE)
support and, due to the low content of positive charges on enzyme surface; the
enzyme could only be successfully immobilized on cationic carboxymethyl support
after chemical amination. Immobilized the enzyme presented higher thermal
stability and higher stability to pH than the free enzyme. In relation to the
free-enzyme, the DEAE derivative was 2-fold more stable in acid pH, while the
carboxymethyl derivative was 2-fold more stable in alkaline pH. When incubated at
pH 7.0 and 50 ºC, the carboxymethyl derivative was more stable retaining 80% of
activity even after 7 h incubation, and the DEAE derivative presented half-life
of 6.6 h. Due to this promising characteristics, both CRL derivatives were
evaluated on the hydrolysis of (R,S)-mandelic acid ethyl ester under different
pH. The CRL immobilized on DEAE support presented stereochemical preference for
the R isomer in pH 5.0 and 7.0, while in pH 9.0 the hydrolysis of the S isomer
hydrolysis was faster with a higher E-value of 21.2. On the other hand, the
carboxymethyl derivative showed opposite results regarding stereochemical
preference with higher E-value at pH 5.0 (E > 200) demonstrating excellent
enantioselective transesterification towards the S-isomer of mandelic acid with
a theoretical 50% conversion yield and a 99.9% enantiomeric excess. 

References

  • Palomo, J.M., Fernández-Lorente, G., Segura, R.L., Ortiz, C., Fernandez-Lafuente, R., Guisán, J.M. Purification, immobilization, hyperactivation, and stabilization of lipases by selective adsorption on hydrophobic supports, in: J.M. Guisán (Ed.), Immobilization of Enzymes and Cells, Humana Press, New York, 2006, pp.143-152. Liu, Y.Y., Xu, J.H., Hu, H.Y., Shen, D. Integration of purification with immobilization of Candida rugosa lipase for kinetic resolution of racemic ketoprofen, J. Biotechnol. 110 (2004) 209-217. Torres, R., Ortiz, C., Pessela, B.C., Palomo, J.M., Mateo, C., Guisán, J.M., Fernandez-Lafuente, R. Improvement of the enantioselectivity of lipase (fraction B) from Candida Antarctica via adsorption on polyethylenimine-agarose under different experimental conditions., Enzyme. Microb. Technol. 39 (2006) 167-171. Palomo, J.M., Fernández-Lorente, G., Mateo, C., Ortiz, C., Fernandez-Lafuente, R., Guisán, J.M. Modulation of the enantioselectivity of lipases via controlled immobilization and medium engineering: hydrolytic resolution of mandelic acid esters, Enzyme. Microb. Technol. 31 (2002) 775-783. Miled, N., Beisson, F., de Caro, J., de Caro, A., Arondel, V., Verger, R. Interfacial catalysis by lipases, J. Mol. Catal. B: Enzym. 11 (2001) 165-171. Palomo, J.M., Fernández-Lorente, G., Mateo, C., Ortiz, C., Fernandez-Lafuente, R., Guisán, J.M. Interfacial adsorption of lipases on very hydrophobic support (octadecyl-sepabeads): immobilization, hyperactivation and stabilization of the open form of lipases, J. Mol. Cat. B: Enzym. 19-20 (2002) 279-286. Palomo, J.M., Fernández-Lorente, G., Mateo, C., Fuentes, M., Fernandez-Lafuente, R., Guisán, J.M. Conformational engineering of lipase from Candida antarctica B via directed immobilization and medium engineering. Hydrolysis of chiral mandelic acid esters, Tetrahed. Asymm. 13 (2002) 1337-1345. Oladepo, D.K., Halling, P.J., Larsen, V.F. Effect of different supports on the reaction rate of Rizomucor miehei lipase in organic media, Biocatal. Biotrans. 12 (1995) 47-54. Machado, A.C.O. Obtenção de intermediários quirais utilizando lipases em reatores assistidos por membranas. Doctoral Thesis. UFRJ – Universidade Federal do Rio de Janeiro, Faculdade de Engenharia Química, Rio de Janeiro, RJ – Brazil (2011). Cao, Y., Wu, S., Li, J., He, B. Highly efficient resolution of mandelic acid using lipase from Pseudomonas stutzeri LC2-8 and a molecular modeling approach to rationalize its enantioselectivity, J. Mol. Catal. B: Enzym. 99 (2014) 108-113. Yao, C.J., Cao, Y., Wu, S.S., Li, D., He, B.F. An organic solvent and thermally stable lipase from Burkholderia ambifaria YCJ01: Purification, characteristics and application for chiral resolution of mandelic acid, J. Mol. Catal. B: Enzym. 85-86 (2013) 105-110. Zingg, S.P., Arnett, E.M., McPhail, A.T., Bothner, A.A., Gilkerson, W.R. Chiral discrimination in the structures and energetics of association of stereoisomeric salts of mandelic acid with alpha.-phenethylamine, ephedrine, and pseudoephedrine, J. Am. Chem. Soc. 110 (1988) 1565-1580. Whitesell, J.K., Reynolds, D. Resolution of chiral alcohols with mandelic acid, J. Org. Chem. 48 (1983) 3548-3551. Yadav, G.D., Sivakumar, P. Enzyme-catalysed optical resolution of mandelic acid via (R,S)-methyl mandelate in non-aqueous media, Biochem. Eng. J. 19 (2004) 101-107. Morais Junior, W.G., Kamimura, E.S., Ribeiro, E.J., Pessela, B.C., Cardoso, V.L., Resende, M.M. Optimization of the production and characterization of lipase from Candida rugosa and Geotrichum candidum in soybean molasses by submerged fermentation, Protein. Express. Purif. 123 (2016) 26-34.
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Details

Primary Language English
Journal Section Articles
Authors

Wilson Galvão De Moraıs Junıor

Glória Fernandez-lorente

Benevides Costa Pessela

Publication Date June 21, 2019
Published in Issue Year 2019Issue: 5

Cite

APA Moraıs Junıor, W. G. D., Fernandez-lorente, G., & Pessela, B. C. (2019). Immobilization of Candida rugosa Lipase on Different Ionic Supports to Improve the Enantioselectivity on Mandelic Acid Resolution. The Eurasia Proceedings of Science Technology Engineering and Mathematics(5), 58-64.