How can aprotic ionic liquids affect enzymatic enantioselectivity?


The enantioselectivity of α-chymotrypsin in the esterification of N-acetyl-tryptophan with ethanol was examined in aprotic ionic liquids. The enantioselectivity was found to be strongly affected by a kind of solvent, water content, and reaction temperature. The (kcatKM)L/(kcat/KM)D ratio in 1-ethyl-3-methylimidazolium bis(fluorosulfonyl)imide ([C2mim][FSI]) containing 1.0% (v/v) water at 25°C exhibits 32,000, while that in 1-ethyl-3-methylimidazolium tetrafluoroborate ([C2mim][BF4]) containing 1.0% (v/v) water at 25°C shows 190. The (kcat/KM)L/(kcat/KM)D ratio in [C2mim] [BF4] at 25°C varies from 190 at 1.0% (v/v) water to 65000 at 5.0% (v/v) water. Moreover, the (kcat/KM)L/ (kcat/KM)

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Noritomi, H. , Chiba, H. , Kikuta, M. and Kato, S. (2013) How can aprotic ionic liquids affect enzymatic enantioselectivity?. Journal of Biomedical Science and Engineering, 6, 954-959. doi: 10.4236/jbise.2013.610117.

Conflicts of Interest

The authors declare no conflicts of interest.


[1] Klibanov, A.M. (2001) Improving enzymes by using them in organic solvents. Nature, 409, 241-246.
[2] Noritomi, H., Sasanuma, A., Kato, S. and Nagahama, K. (2007) Catalytic properties of cross-linked enzyme crystals in organic media. Biochemical Engineering Journal, 33, 228-231.
[3] Noritomi, H., Almarsson, O., Barletta, G.L. and Klibanov, A.M. (1996) The influence of the mode of enzyme preparation on enzymatic enantioselectivity in organic solvents and its temperature dependence. Biotechnology and Bioengineering, 51, 95-99.<95::AID-BIT11>3.0.CO;2-3
[4] Wescott, C.R., Noritomi, H. and Klibanov, A.M. (1996) Rational control of enzymatic enantioselectivity through solvation thermodynamics. Journal of the American Chemical Society, 118, 10365-10370.
[5] Kise, H., Hayakawa, A. and Noritomi, H. (1990) Protease-catalyzed synthetic reactions and immobilization-activation of the enzymes in hydrophilic organic solvents. Journal of Biotechnology, 14, 239-254.
[6] Kokorin, A. (2011) Ionic liquids: Applications and perspectives. InTech, Rijeka.
[7] Moniruzzaman, M., Nakashima, K., Kamiya, N. and Goto, M. (2010) Recent advances of enzymatic reactions in ionic liquids. Biochemical Engineering Journal, 48, 295-314.
[8] Noritomi, H., Nishida, S. and Kato, S. (2007) Protease-catalyzed esterification of amino acid in water-miscible ionic liquid. Biotechnology Letters, 29, 1509-1512.
[9] Noritomi, H., Suzuki, K., Kikuta, M. and Kato, S. (2007) Catalytic activity of α-chymotrypsin in enzymatic peptide synthesis in ionic liquids. Biochemical Engineering Journal, 47, 27-30.
[10] Kumar, A. and Venkatesu, P. (2012) Overview of the stability of α-chymotrypsin in different solvent media. Chemical Reviews, 112, 4283-4307.
[11] Fersht, A. (1999) Structure and mechanism in protein science: A guide to enzyme catalysis and protein folding. W. H. Freeman and Company, New York.
[12] Segel, I.H. (1993) Enzyme kinetics: Behavior and analysis of rapid equilibrium and steady-state enzyme systems. John Wiley & Sons, Inc., New York.
[13] Noritomi, H., Minamisawa, K., Kamiya, R. and Kato, S. (2011) Thermal stability of proteins in the presence of aprotic ionic liquids. Journal of Biomedical Science and Engineering, 4, 94-99.
[14] Zaks, A. and Klibanov, A.M. (1988) The effect of water on enzyme action in organic media. The Journal of Biological Chemistry, 263, 8017-8021.
[15] Klibanov, A.M. (1986) Enzymes that work in organic solvents. Chemtech, 16, 354-359.

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