M. Guncheva et al. / Journal of Molecular Catalysis B: Enzymatic 102 (2014) 72–80
79
Table 4
Effect of immobilization of lipase from Rhizopus delemar on nanosized tin dioxide (pure and amino-functionalized) on enantioselectivity.
Enzyme preparation
(
) Menthol conversion, %
Enantiomeric excess (P ), %
Enantiomeric ratio
Native lipase from Rhizopus delemar
Nano-SnO2-RhD
+MOPyrroBF4
+MOPyrroNTf2
+MOPyrroPF6
NH2-nano-SnO2-RhD
+MOPyrroBF4
+MOPyrroNTf2
0.7
–
NA
20.5 0.8
9.6 0.4
8.7 0.3
12.3 0.3
20.4 0.7
7.8 0.2
7.8 0.2
10.5 0.3
93.6
96.8
95.5
98.4
97.0
97.5
97.4
97.3
38.8 1.1
67.4 2.6
47.8 1.8
140.0 5.3
84.0 3.3
80.0 3.6
85.0 3.5
83.0 3.4
+MOPyrroPF6
Reaction conditions: ( )menthol (4 mmol), vinyl acetate (4 mmol) and native or immobilized lipase (5 U), 25 ◦C, 200 rpm, 20 h, hexane, 1 mmol ionic liquid, aw 0.33.
ionic liquids (Table 4). In the studied reaction, [MOPyrro][BF4],
[MOPyrro][PF6], and [MOPyrro][NTf2] did not influence the enan-
tioselectivity of NH2-nano-SnO2-RhD preparation as compared to
no-additive conditions. In contrast, the physically adsorbed on
nano-SnO2 lipase from R. delemar exhibited up to 3.7-fold higher
enantioselectivity in presence of ILs. Mohile et al. observed similar
effect of imidazolium-based ILs on the C. rugosa lipase-catalyzed
kinetic resolution of butyl 2-(4-chlorophenoxy) propionate, i.e,
decrease in reaction rate and substrate conversion and notable
in the reaction mixture [59]. Similarly, an excellent enantioselec-
tivity (E > 500) of immobilized C. antarctica B in imidazolium-based
ILs in reaction of acylation of 1-phenylethylamine, at very low con-
version (5–18%) was reported [60].
[13] P. Lozano, Green Chem. 12 (2010) 555–569.
[14] C. Garcia-Galan, A. Berenguer-Murcia, R. Fernandez-Lafuente, R. Rodrigues,
Adv. Synth. Catal. 353 (2011) 2885–2904.
[15] M. Guncheva, M. Dimitrov, D. Zhiryakova, Catal. Commun. 16 (2011) 205–209.
[16] M. Guncheva, M. Dimitrov, D. Zhiryakova, Process Biochem. 46 (2011)
2170–2177.
[17] A. David, N. Wang, V. Yang, A. Yang, J. Biotechnol. 125 (2006) 395–407.
[18] T. Terentyeva, A. Matras, W. Rossom, J. Hill, Q. Ji, K. Ariga, J. Mater. Chem. B 1
(2013) 3248–3256.
[19] A. Mayoral, R. Arenal, V. Gascón, C. Márquez-Álvarez, R. Blanco, I. Díaz, Chem-
CatChem 5 (2013) 903–909.
[20] R. Sanz, G. Calleja, A. Arencibia, E. Sanz-Pérez, Micropor. Mesopor. Mater. 158
(2012) 309–317.
[21] H. Yoshitake, T. Yokoi, T. Tatsumi, Chem. Mater. 14 (2002) 4603–4610.
[22] X. Wang, K. Lin, J. Chan, S. Cheng, J. Phys. Chem. B 109 (2005) 1763–1769.
[23] X. Wang, J. Chan, Y.-H. Tseng, S. Chen, Micropor. Mesopor. Mater. 95 (2006)
57–65.
[24] H. Ritter, D. Bru¨ hwiler, J. Phys. Chem. C 113 (2009) 10667–10674.
[25] Y. Shimada, M. Suenaga, A. Sugihara, S. Nakai, Y. Tominaga, J. Am. Oil Chem.
Soc. 76 (1999) 189–193.
4. Conclusions
[26] P.A. Nunes, P. Pires-Cabral, M. Guillen, F. Valero, S. Ferreira-Dias, J. Am. Oil Chem.
Soc. 89 (2012) 1287–1295.
[27] R. Jala, P. Hu, T. Yang, Y. Jiang, Y. Zheng, X. Xu, in: Georgina Sandoval (Ed.),
Lipases and Phospholipases: Methods and Protocols, Methods in Molecular
Biology, vol. 861, Springer Science + Business Media, New York, 2012, pp.
403–431.
[28] M. Haas, D. Bailey, W. Baker, T. Berka, D. Cichowicz, Z. Derewenda, R.
Genuario, R. Joeger, R. Klein, K. Scott, D. Woolf, Fett/Lipid 101 (1999)
364–370.
The synthesized novel hybrid materials on the basis of nanosized
tin dioxide and lipase from R. delemar demonstrated improved
activity and stability than the native enzyme. The two preparations,
The conversion of the target enantiomer exceeded 38% (e.e.(P )
[29] C. Gray, J. Narang, S. Barker, Enzyme Microb. Technol. 12 (1990) 800–807.
[30] M. Dimitrov, T. Tsoncheva, S. Shao, R. Köhn, Appl. Catal. B: Environ. 94 (2010)
158–165.
[31] C. Hammond, The diffraction of X-rays, in: The Basics of Crystallography and
Diffraction, Oxford Science Publications, New York, 2001, pp. 203–242.
[32] E. Soto-Cantu, R. Cueto, J. Koch, P. Russo, Langmuir 28 (2012) 5562–5569.
[33] G. Chatel, C. Goux-Henry, A. Mirabaud, T. Rossi, N. Kardos, B. Andrioletti, M.
Draye, J. Catal. 291 (2012) 127–132.
−
89.5%) when glyceryl triacetate was used as an acylating reagent.
Although not as good as the results given at the literature for the
lipases from Candida sp.[61,62], the results in terms of conversion
(%) and enantiomeric excess (e.e.(P )%) are the best than any previ-
−
ously reported in the literature for R. delemar lipase. We estimated
that three pyrrolidinium-based ionic liquids have positive effect on
the enantioselectivity of the nano-SnO2-RhD and their interactions
with other lipases should be thoroughly examined.
[34] B. Al-Duri, Y.P. Yong, J. Mol. Catal. B: Enzym. 3 (1997) 177–188.
[35] O.H. Lowry, N.J. Rosebrough, A.L. Farr, R.J. Randall, J. Biol. Chem. 193 (1951)
265–275.
[36] P. Halling, Biotechnol. Tech. 6 (1992) 271–276.
[37] A. Straathof, J. Jongejan, Enzyme Microb. Technol. 21 (1997) 559–571.
[38] M. Thommes, Chem. Ing. Tech. 82 (2010) 1059–1073.
[39] U. Derewenda, L. Swenson, Y. Wei, R. Green, P.M. Kobos, R. Joerger, M.J. Haas,
Z.S. Derewenda, J. Lipid Res. 35 (1994) 524–534.
[40] J. Lewis, J. Am. Ceram. Soc. 83 (2000) 2341–2359.
[41] J. Palomo, C. Ortiz, M. Fuentes, G. Fernandez-Lorente, J. Guisan, R. Fernandez-
Lafuente, J. Chromatogr. A 1038 (2004) 267–273.
Acknowledgement
The authors thank the National Science Fund of Bulgaria (project
DMU 02/20) for the financial support.
[42] A. Mendes, R. Giordano, R. de, L.C. Giordano, H. de Castro, J. Mol. Catal. B: Enzym.
68 (2011) 109–115.
References
[43] L.N. de Lima, C. Aragon, C. Mateo, J. Palomo, R. Giordano, P. Tardioli, J. Guisan,
G. Fernandez-Lorente, Process Biochem. 48 (2013) 118–123.
[44] D. Rodrigues, A. Mendes, M. Filice, R. Fernandez-Lafuente, J. Guisan, J. Palomo,
J. Mol. Catal. B: Enzym. 58 (2009) 36–40.
[45] S. Hwang, K.-T. Lee, J.-W. Park, B.-R. Min, S. Haam, I.-S. Ahn, J.-K. Jung, Biochem.
Eng. J. 17 (2004) 85–90.
[1] P. Reis, K. Holmberg, H. Watzke, M. Leser, R. Miller, Adv. Colloid Interface Sci.
147–148 (2009) 237–250.
[2] Z.S. Derewenda, A.M. Sharp, Trends Biochem. Sci. 18 (1993) 20–25.
[3] R. Schmid, R. Verger, Angew. Chem. Int. Ed. 37 (1998) 1608–1633.
[4] F. Hasan, A. Shah, A. Hameed, Enzyme Microb. Technol. 39 (2006) 235–251.
[5] A. Houde, A. Kademi, D. Leblanc, Appl. Biochem. Biotechnol. 118 (2004)
155–170.
[46] S. Pahujani, S. Kanwar, G. Chauhan, R. Gupta, Bioresour. Technol. 99 (2008)
2566–2570.
[47] S. Koshiro, K. Sonomoto, A. Tanaka, S. Fukui, J. Biotechnol. 2 (1985) 47–57.
[48] J. Kaar, A. Jesionowski, J. Berberich, R. Moulton, A. Russell, J. Am. Chem. Soc. 125
(2003) 4125–4131.
[49] Z. Yang, W. Pan, Enzyme Microb. Technol. 37 (2005) 19–28.
[50] S. Park, R. Kazlauskas, Curr. Opin. Biotech. 14 (2003) 432–437.
[51] F. Deive, A. Rodriguez, L. Rebelo, I. Marrucho, Sep. Purif. Technol. 97 (2012)
205–210.
[6] M. Kapoor, M. Gupta, Process Biochem. 47 (2012) 555–569.
[7] J.-F. Cai, Z. Guan, Y.-H. He, J. Mol. Catal. B: Enzym. 68 (2011) 240–244.
[8] B. Liu, X. Qian, Q. Wu, X. Lin, Enzyme Microb. Technol. 43 (2008) 375–380.
[9] A. Bastida, P. Sabuquillo, P. Armisen, R. Fernandez-Lafuente, J. Huguet, J. Guisan,
Biotechnol. Bioeng. 58 (1998) 486–493.
[10] B. Vaidya, G. Ingavle, S. Ponrathnam, B. Kulkarni, S. Nene, Bioresour. Technol.
99 (2008) 3623–3629.
[52] F. Deive, A. Rodriguez, A. Pereiro, J. Araujo, M. Longo, M. Coelho, J. Canon-
gia Lopes, J. Esperanca, L. Rebelo, I. Marrucho, Green Chem. 13 (2011)
390–396.
[11] J. Lu, K. Nie, F. Wang, T. Tan, Bioresour. Technol. 99 (2008) 6070–6074.
[12] N. Ognjanovic, D. Bezbradica, Z. Knezevic-Jugovic, Bioresour. Technol. 100
(2009) 5146–5154.