JBiSE  Vol.6 No.10 , October 2013
How can aprotic ionic liquids affect enzymatic enantioselectivity?
ABSTRACT
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)

Cite this paper
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.
References
[1]   Klibanov, A.M. (2001) Improving enzymes by using them in organic solvents. Nature, 409, 241-246. http://dx.doi.org/10.1038/35051719

[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.
http://dx.doi.org/10.1016/j.bej.2006.10.024

[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. http://dx.doi.org/10.1002/(SICI)1097-0290(19960705)51:1<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. http://dx.doi.org/10.1021/ja961394q

[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. http://dx.doi.org/10.1016/0168-1656(90)90110-W

[6]   Kokorin, A. (2011) Ionic liquids: Applications and perspectives. InTech, Rijeka.
http://dx.doi.org/10.5772/1782

[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.
http://dx.doi.org/10.1016/j.bej.2009.10.002

[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. http://dx.doi.org/10.1007/s10529-007-9416-4

[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.
http://dx.doi.org/10.1016/j.bej.2009.06.010

[10]   Kumar, A. and Venkatesu, P. (2012) Overview of the stability of α-chymotrypsin in different solvent media. Chemical Reviews, 112, 4283-4307. http://dx.doi.org/10.1021/cr2003773

[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.
http://dx.doi.org/10.4236/jbise.2011.42013

[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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