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At low water activity α-chymotrypsin is more active in an ionic liquid than in non-ionic organic solvents

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Abstract

The kinetics of the α-chymotrypsin catalysed transesterification of N-acetyl-l-phenylalanine ethyl ester with 1-butanol and the competing hydrolysis were evaluated at fixed water activity in two ionic liquids and two non-ionic organic solvents. In most respects the four solvents behaved similarly. However, at a water activity of 0.33, higher catalytic activity was observed in the ionic liquid, 1-butyl-3-methylimidazolium bis[(trifluoromethyl)sulfonyl]amide, than in the other solvents, and at aw=0.11 catalysis was only observed in this solvent.

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References

  • Adlercreutz P (1991) On the importance of the support material for enzymic synthesis in organic media. Support effects at controlled water activity. Eur. J. Biochem. 199: 609-614.

    Google Scholar 

  • Adlercreutz P (1993) Activation of enzymes in organic media at low water activity by polyols and saccharides. Biochim. Biophys. Acta 1163: 144-148.

    Google Scholar 

  • Affleck R, Xu Z-F, Suzawa V, Focht K, Clark DS, Dordick JS (1992) Enzymatic catalysis and dynamics in low-water environments. Proc. Natl. Acad. Sci. USA 89: 1100-1104.

    Google Scholar 

  • Aki S, Brenneke J, Samanta A (2001) How polar are roomtemperature ionic liquids? Chem. Comm.: 413-414.

  • Barzana E, Karel M, Klibanov AM (1989) Enzymatic oxidation of ethanol in the gaseous phase. Biotechnol. Bioeng. 34: 1178-1185.

    Google Scholar 

  • Björup P, Wehtje E, Adlercreutz P (1996) Effects of acetonitrilewater mixtures on alpha-chymotrypsin catalyzed dipeptide synthesis. Biocatal. Biotransform. 13: 189-200.

    Google Scholar 

  • Bonhôte P, Dias AP, Papageorgiou K, Grätzel M (1996) Hydrophobic, highly conductive ambient-temperature molten salts. Inorg. Chem. 35: 1168-1178.

    Google Scholar 

  • Carmichael AJ, Seddon KR (2000) Polarity study of some 1-alkyl-3-methylimidazolium ambient temperature ionic liquids with the solvatochromic dye, Nile red. J. Phys. Org. Chem. 13: 591-595.

    Google Scholar 

  • Erbeldinger M, Mesiano AJ, Russell AJ (2000) Enzymatic catalysis of formation of Z-aspartame in ionic liquid-an alternative to enzymatic catalysis in organic solvents. Biotechnol. Prog. 16: 1129-1131.

    Google Scholar 

  • Halling PJ (1994) Thermodynamic predictions for biocatalysis in non-conventional media: theory, tests and recommendations for experimental design and analysis. Enzyme Microb. Technol. 16: 178-206.

    Google Scholar 

  • Husum TL, Jørgensen CT, Christensen MW, Kirk O (2001) Enzyme catalysed synthesis in ambient temperature ionic liquids. Biocatal. Biotransfor. 19: 331-338.

    Google Scholar 

  • Kim K-W, Song B, Choi M-Y, Kim M-J (2001) Biocatalysis in ionic liquids: markedly enhanced enantioselectivity of lipase. Org. Lett. 3: 1507-1509.

    Google Scholar 

  • Klibanov AM (2001) Improving enzymes by using them in organic solvents. Nature 409: 241-246.

    Google Scholar 

  • Kragl U, Kaftzik N, Schöfer SH, Eckstein M, Wasserscheid P, Hilgers C (2001) Enzyme catalysis in the presence of ionic liquids. Chimica Oggi/Chemistry Today (July/August): 22-24.

  • Laszlo JA, Compton DL (2001) α-Chymotrypsin catalysis in imidazolium-based ionic liquids. Biotechnol. Bioeng. 75: 181-186.

    Google Scholar 

  • Lau RM, van Rantwijk F, Seddon KR, Sheldon RA (2000) Lipase catalysed reactions in ionic liquids. Organ. Lett. 26: 4189-4191.

    Google Scholar 

  • Lozano P, de Diego T, Guegan J-P, Vaultier M, Iborra JL (2001a) Stabilization of α-Chymotrypsin by ionic liquids in transesterifi-cation reactions. Biotechnol. Bioeng. 75: 563-569.

    Google Scholar 

  • Lozano P, de Diego T, Carrié D, Vaultier M, Iborra JL (2001b) Overstabilization of Candida antarctica lipase B by ionic liquids in ester synthesis. Biotechnol. Lett. 23: 1529-1533.

    Google Scholar 

  • Nakamura K (1990) Biochemical reactions in supercritical fluids. Trends Biotechnol. 8: 288-292.

    Google Scholar 

  • Park S, Kazlauskas RJ (2001) Improved preparation and use of room-temperature ionic liquids in lipase-catalyzed enantio-and regioselective acylations. J. Org. Chem. 66: 8395.

    Google Scholar 

  • Riddick JA, Bunger WB, Sakano TK (1986) Organic Solvents-Physical Properties and Methods of Purification. Techniques of Chemistry, Vol II, 4th edn. New York: Wiley.

    Google Scholar 

  • Russell AJ, Yang FX (1996) Catalyze gas-phase reactions with enzymes. Chemtech. 1996: 24-27.

    Google Scholar 

  • Ryu K, Dordick JS (1992) How do organic solvents affect peroxidase structure and function? Biochemistry 31: 2588-2598.

    Google Scholar 

  • Schmitke JL, Wescott CR, Klibanov AM (1996) The mechanistic dissection of the plunge in enzymatic activity upon transition from water to anhydrous solvents. J. Am. Chem. Soc. 118: 3360-3365.

    Google Scholar 

  • Schöfer SH, Kaftzik N, Wasserscheid P, Kragl U (2001) Enzyme catalysis in ionic liquids: lipase catalysed resolution of 1-phenylethanol with improved enantioselectivity. Chem. Comm.: 425-426.

  • Valivety RH, Halling PJ, Macrae AR (1992) Reaction rate with suspended lipase catalyst shows similar dependence on water activity in different organic solvents. Biochim. Biophys. Acta 1118: 218-222.

    Google Scholar 

  • Wasserscheid P, Keim W (2000) Ionic liquids-New 'solutions' for transition metal catalysis. Angew. Chem. Int. Ed. 39: 3773-3789.

    Google Scholar 

  • Zaks A, Klibanov A (1988) The effect of water on enzyme action in organic media. J. Biol. Chem. 263: 8017-8021.

    Google Scholar 

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Eckstein, M., Sesing, M., Kragl, U. et al. At low water activity α-chymotrypsin is more active in an ionic liquid than in non-ionic organic solvents. Biotechnology Letters 24, 867–872 (2002). https://doi.org/10.1023/A:1015564608261

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