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Quintana, P.G.; Canet, A.; Marciello, M.; Valero, F.; Palomo, J.M.; Baldessari, A. "Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase" (2015) Journal of Molecular Catalysis B: Enzymatic. 118:36-42
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Abstract:

A lipase-catalyzed preparation of ethyl and stearyl esters of chenodeoxycholic acid is described. Stearyl chenodeoxycholate is a new product and both bile acid esters were prepared through an enzymatic approach for the first time. The heterologous Rhizopus oryzae lipase, immobilized on two different supports proved to be an efficient catalyst, even more active than Candida antarctica lipase, in the esterification reaction using a complex substrate such as a bile acid. The immobilization of the enzyme on Octadecyl Sepabeads at pH 7 and 25°C was the best choice to catalyze the esterification reaction. The influence of various reaction parameters, such as nature of the alcohol, alcohol:substrate ratio, enzyme:substrate ratio, solvent and temperature, was evaluated. Using the response surface methodology and a central composite rotatable design, the conversion of stearyl chenodeoxycholate was optimized by means of the study of the effect of enzyme:substrate ratio and alcohol:substrate ratio. The value 20 for ratios (E/S) and (A/S) was predicted as the optimal value to reach the maximum conversion. However, including economic aspects these ratios can be reduced up to 15. The well-known advantages of biocatalysis and the activity shown by the immobilized heterologous lipase make the reported procedure a convenient way to prepare chenodeoxycholic esters. © 2015 Elsevier B.V. All rights reserved.

Registro:

Documento: Artículo
Título:Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase
Autor:Quintana, P.G.; Canet, A.; Marciello, M.; Valero, F.; Palomo, J.M.; Baldessari, A.
Filiación:Laboratorio de Biocatálisis, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón 2, Piso 3, Ciudad Universitaria, Buenos Aires, C1428EGA, Argentina
Departament d'Enginyeria Química, EE, Universitat Autònoma de Barcelona, Bellaterra, Barcelona 08193, Spain
Departamento de Biocatálisis, Instituto de Catálisis (CSIC), Campus UAM Cantoblanco, Madrid, 28049, Spain
Palabras clave:Chenodeoxycholic acid; Esterification; Heterologous Rhizopus oryzae Lipase; Immobilization; Body fluids; Catalysis; Enzyme immobilization; Enzymes; Esters; Radioactive waste vitrification; Substrates; Candida antarctica lipase; Central composite rotatable design; Chenodeoxycholic acid; Efficient catalysts; Esterification reactions; Reaction parameters; Response surface methodology; Rhizopus oryzae lipase; Esterification; alcohol; bile acid; Candida antarctica lipase; chenodeoxycholic acid; chenodeoxycholic ester; ester; fungal enzyme; Rhizopus oryzae lipase; triacylglycerol lipase; unclassified drug; Article; controlled study; enzyme immobilization; esterification; nonhuman; pH; response surface method; solvent effect; temperature; Candida antarctica; Rhizopus oryzae
Año:2015
Volumen:118
Página de inicio:36
Página de fin:42
DOI: http://dx.doi.org/10.1016/j.molcatb.2015.05.008
Título revista:Journal of Molecular Catalysis B: Enzymatic
Título revista abreviado:J. Mol. Catal. B Enzym.
ISSN:13811177
CODEN:JMCEF
CAS:alcohol, 64-17-5; chenodeoxycholic acid, 474-25-9; triacylglycerol lipase, 9001-62-1
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13811177_v118_n_p36_Quintana

Referencias:

  • Ruggles, K.V., Turkish, A., Sturley, S.L., (2013) Annu. Rev. Nutr., 33, pp. 413-451
  • Small, D.M., (1968) Adv. Chem. Ser., 84, pp. 31-52
  • Liang, D., Zhou, Q., Zhang, J., Gong, W., Xu, C.H., Li, B., Wang, Y., Li, J., (2012) Steroids, 77, pp. 1381-1390
  • Zhang, J., Wang, H., Pi, H., Ruan, H., Zhang, P., Wu, J., (2009) Steroids, 74, pp. 424-434
  • Zhichuan, S., Zhao, Z., Liu, M., Wang, X., (2013) C. R Chimie, 16, pp. 977-984
  • Sepe, V., Ummarino, R., D'Auria, M.V., Chini, M.G., Bifulco, G., Renga, B., D'Amore, C., Zampella, A., (2012) J. Med. Chem., 55, pp. 84-93
  • Sharma, R., Majer, F., Peta, V.L., Wang, J., Keaveney, R., Kelleyer, D., Long, A., Gilmer, J.F., (2010) Bioorg. Med. Chem., 18, pp. 6886-6895
  • Uekawa, T., Ishigami, K., Kitahara, T., (2004), 68, pp. 1332-1337; Bai, X., Barnes, C.H., Dias, J.R., (2009) Tetrahedron Lett., 50, pp. 503-505
  • Dayal, B., Keshava, R., Salen, G., (1995) Steroids, 60, pp. 453-457
  • Faber, K., (2011) Biotransformations in Organic Chemistry, , sixth ed. Springer Verlag Heidelberg
  • Whitthall, J., Sutton, P.W., (2012) Practical Methods for Biocatalysis and Biotransformations, 2. , John Wiley & Sons Ltd. New York
  • Gotor, V., Alfonso, I., García-Urdiales, E., (2007) Asymmetric Organic Synthesis with Enzymes, , Wiley-VCH Weinheim
  • Hall, M., Kroutil, W., Faber, K., (2013) The Evolving Role of Biocatalysis in Asymmetric Synthesis II: More Methods and Applications, , Wiley-VCH New York
  • Tao, J., Lin, G.-Q., Liese, A., (2009) Biocatalysis for the Pharmaceutical Industry: Discovery, Development and Manufacturing, , John Wiley & Sons Ltd. New York
  • Carrea, G., Riva, S., (2008) Organic Synthesis with Enzymes in Non-aqueous Media, , Wiley-VCH Weinheim
  • Baldessari, A., (2012) Lipases and Phospholipases, Methods and Protocols, pp. 445-456. , G. Sandoval, Humana Press New York
  • Monsalve, L.N., Machado Rada, M.Y., Ghini, A.A., Baldessari, A., (2008) Tetrahedron, 64, pp. 1721-1730
  • Quintana, G.P., Baldessari, A., (2009) Steroids, 74, pp. 1007-1014
  • Quintana, P.G., Guillén, M., Marciello, M., Palomo, J.M., Valero, F., Baldessari, A., (2012) Eur. J. Org. Chem., pp. 4306-4312
  • Quintana, P.G., Romero, S.M., Vaamonde, G., Baldessari, A., (2013) J. Mol. Catal. B: Enzym., 97, pp. 110-117
  • Baldessari, A., Iglesias, L.E., (2012) Lipases and Phospholipases, Methods and Protocols, pp. 457-470. , G. Sandoval, Humana Press New York
  • Riva, S., Bovara, R., Ottolina, G., Secundo, F., Carrea, G., (1989) J. Org. Chem., 54, pp. 3161-3164
  • Sugai, T., Takizawa, M., Bakke, M., Ohtsuka, Y., (1996) Biosci. Biotechnol. Biochem., 60, pp. 2059-2063
  • Bhandari, K., Chaurasia, S.P., Dalai, A.K., Gupta, A., Singh, K., (2013) J. Mol. Catal. B: Enzym., 94, pp. 104-110
  • Oliveira, P., Jares, F., Ikegaki, M., (2006) Braz. J. Microbiol., 37, pp. 329-337
  • Méndes, J., Oromi, M., Cervero, M., Balell, M., Torres, M., Canela, R., (2007) Chirality, 19, pp. 44-50
  • Cos, O., Resina, D., Ferrer, P., Montesinos, J.L., Valero, F., (2005) Biochem. Eng. J., 26, pp. 86-94
  • Arnau, C., Ramón, R., Casas, C., Valero, F., (2010) Enzyme Microb. Technol., 46, pp. 494-500
  • Barrigón, J.M., Montesinos, J.L., Valero, F., (2013) Biochem. Eng. J., 75, pp. 47-54
  • Ferrer, P., Alarcón, M., Ramón, R., Benaiges, M.D., Valero, F., (2009) Biochem. Eng. J., 43, pp. 271-277
  • Brabcova, J., Demianova, Z., Vondrasek, J., Jagr, M., Zarevucka, M., Palomo, J.M., (2013) J. Mol. Catal. B: Enzym., 98, pp. 62-72
  • Godoy, C.A., Romero, O., De Las Rivas, B., Mateo, C., Fernandez-Lorente, G., Guisan, J.M., Palomo, J.M., (2013) J. Mol. Catal. B: Enzym., 87, pp. 121-127
  • Cabrera, Z., Fernández-Lorente, G., Fernandez-Lafuente, R., Palomo, J.M., Guisan, J.M., (2009) J. Mol. Catal. B: Enzym., 57, pp. 171-176
  • Simoes, T., Valero, F., Tecelao, C., Ferreira-Dias, S., (2014) J. Am. Oil Chem. Soc., 91, pp. 411-419
  • Guillén, M., Benaiges, M.J., Valero, F., (2012) Biochem. Eng. J., 65, pp. 1-9
  • Canet, A., Benaiges, M.D., Valero, F., (2014) J. Am. Oil Chem. Soc., 91, pp. 1499-1506
  • Bradford, M.M., (1976) Anal. Biochem., 72, pp. 248-254
  • Yang, L., Dordick, J.S., Garde, S., (2004) Biophys. J., 87, pp. 812-821
  • Bruttomesso, A.C., Baldessari, A., (2004) J. Mol. Catal. B: Enzym., 29, pp. 149-153
  • Da Silva, M.R., De Mattos, M.C., Ferreira De Oliveira, M.C., Gomes De Lemos, T.L., Pontes Silva, N.M., De Gonzalo, G., Lavandera, I., Gotor, V., (2014) Tetrahedron, 70, pp. 2264-2271
  • De Diego, T., Manjón, A., Iborra, J.L., (2013) Biocatal. Biotransform., 31, pp. 175-180

Citas:

---------- APA ----------
Quintana, P.G., Canet, A., Marciello, M., Valero, F., Palomo, J.M. & Baldessari, A. (2015) . Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase. Journal of Molecular Catalysis B: Enzymatic, 118, 36-42.
http://dx.doi.org/10.1016/j.molcatb.2015.05.008
---------- CHICAGO ----------
Quintana, P.G., Canet, A., Marciello, M., Valero, F., Palomo, J.M., Baldessari, A. "Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase" . Journal of Molecular Catalysis B: Enzymatic 118 (2015) : 36-42.
http://dx.doi.org/10.1016/j.molcatb.2015.05.008
---------- MLA ----------
Quintana, P.G., Canet, A., Marciello, M., Valero, F., Palomo, J.M., Baldessari, A. "Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase" . Journal of Molecular Catalysis B: Enzymatic, vol. 118, 2015, pp. 36-42.
http://dx.doi.org/10.1016/j.molcatb.2015.05.008
---------- VANCOUVER ----------
Quintana, P.G., Canet, A., Marciello, M., Valero, F., Palomo, J.M., Baldessari, A. Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase. J. Mol. Catal. B Enzym. 2015;118:36-42.
http://dx.doi.org/10.1016/j.molcatb.2015.05.008