Abstract
Water is the most common solvent for biochemical reactions both in vivo and in vitro in enzymological experiments. Unfortunately, synthetic reactions that can be carried out by reversing the hydrolytic action of certain enzymes as well as other biotransformations (e.g., oxidation) are difficult or even impossible to operate in water. Oxidation reactions are limited by the poor solubility of oxygen in water, and syntheses are impeded by high water activity. In order to shift the thermodynamic equilibrium in favor of the synthesis, it is necessary to use nonaqueous solvents. However, the use of solvents can be problematic because of toxicity, flammability, and increasing environmental concerns. As a result, supercritical fluids (SCFs) have attracted much attention in recent years as an alternative to organic solvents for carrying out enzymatic reactions. Up to now, SCFs have only been used in large-scale industrial processing to extract plant materials (e.g., coffee, hops). Nevertheless, interest in the use of SCF as a solvent for biocatalysis is growing rapidly (see reviews in refs. 1-9).
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Aaltonen O. and Rantakylä, M. (1991) Biocatalysis in supercritical CO2. CHEMTECH 240–248.
Perrut, M. (1994) Enzymatic reactions and cell behaviour in supercritical fluids. Chem. Biochem. Eng. Quart. 8(1), 25–30.
Russell, A. J., Beckman, E. J., and Chaudhary, A. K. (1994) Studying enzyme activity in supercritical fluids. CHEMTECH 24, 33–37.
Jarzebski, A. B. and Malinowski, J. J. (1995) Potentials and prospects for application of supercritical fluid technology in bioprocessing. Process Biochem. 30, 343–352.
Kamat, S., Beckman, E. J., and Russell, A. J. (1995) Enzyme activity in supercritical fluids, Crit. Rev. Biotechnol. 15, 41–71.
Ballesteros, A., Bornscheuer, U., Capewell, A., Combes, D., Condoret, J. S., Koenig, K., et al. (1995) Enzymatic reaction in non conventional media. Biocatal. Biotransform. 13, 1–42.
Nakamura, K. (1996) Enzymic synthesis in supercritical fluids. Supercrit. Fluid Technol. Oil Lipid.
Cernia, E. and Palocci, C. (1997) Lipases in supercritical fluids. Methods Enzymol. 286 (Lipases, Part B), 495–508.
Ikushima, Y. (1997) Supercritical fluids: an interesting medium for chemical and biochemical processes. Adv. Colloid Interf. Sci. 71-72, 259–280.
King, M. B. and Bott, T. R. (1983)Extraction of Natural Products Using Near Critical Solvents. Blackie Academic and Professional/Chapman & Hall, London.
Erickson, J. C., Schyns, P., and Cooney, C. L. (1990) Effect of pressure on an enzymatic reaction in a supercritical fluid. AIChE J. 36, 299–301.
van Eijs, A. M. M., de Jong, J. P. J., Doddema, H. J., and Lindeboom, D. R. (1988) Enzymatic transesterification in supercritical carbon dioxide. Proceedings of the International Symposium on Supercritical Fluids (Nice, France) (Perrut, M., ed.), pp. 933–942.
Ely, J. F., Haynes, W. M., and Bain, B. C. (1989) Isochoric measurements on CO2 and on (0.982 CO2+0.018 N2) from 250 to 330 K at pressures to 35 MPA. J. Chem. Thermodynam. 21, 879–894.
Wiebe, R. and Gaddy, V. L. (1941) Vapour phase composition of carbon dioxide-water mixtures at various temperature and at pressures to 700 atmosphere. J. Am. Chem. Soc. 63, 475–477.
Chrastil, J. (1982) Solubility of solids and liquids in supercritical gases. J. Phys. Chem. 86, 3016–3021.
Giddings, J. C., Meyers, M. N., McLaren, L., and Keller, R. A. (1968) High pressure gas chromatography of nonvolatile species. Science 162, 67.
King, J. W. and Friedrich, J. P. (1990) Quantitive correlations between solute molecular-structure and solubility in supercritical fluids. J. Chromatogr. Sci. 517, 449–458.
Peng, D. Y. and Robinson, D. B. (1976) A new two constant equation of state. Eng. Chem. Fundam. 15, 59.
Valle, J. M. and Aguilera J. M. (1988) An improved equation for predicting the solubility of vegetable oils in supercritical CO2. Eng. Chem. Res. 27, 1551–1553.
Castillo, E., Marty, A., Combes, D., and Condoret, J. S. (1994) Polar substrates for enzymatic reactions in supercritical CO2. How to overcome the solubility limitation. Biotechnol. Lett. 16, 169–174.
Hammond, D. A., Karel, M., Klibanov, A. M., and Krukonis, V. J. (1985) Enzymatic reactions in supercritical gases. Appl. Biochem. Biotechnol.11, 393–400.
Miller, D. A., Blanch, H. W., and Prausnitz, J. M. (1991) Enzyme-catalyzed interesterification of triglycerides in supercritical carbon dioxide. Ind. Eng. Chem. Res. 30, 939–946.
Randolph, T. W., Blanch, H. W., and Prausnitz, J. M. (1988) Enzyme-catalyzed oxidation of cholesterol in supercritical carbon dioxide. AIChE J. 34, 1354–1360.
Marty, A., Combes, D., and Condoret, J. S. (1994) Continuous reaction-separation process for enzymatic esterification in supercritical carbon dioxide. Biotechnol. Bioeng. 43, 497–504.
Marty, A., Chulalaksananukul, W., Condoret, J. S., Willemot, R. M., and Durand, G. (1990) Comparison of lipase-catalyzed esterification in supercritical carbon dioxide and in n-hexane. Biotechnol. Lett. 12, 11–16.
Dumont, T., Barth, D., Corbier, C., Branlant, G., and Perrut, M. (1992) Enzymatic reaction kinetic: comparison in an organic solvent and in supercritical carbon dioxide. Biotechnol. Bioeng. 40, 329–333.
Marty, A., Dossat, V., and Condoret, J. S. (1997) Continuous operation of lipase-catalyzed reactions in non-aqueous solvents: influence of the production of hydrophilic compounds. Biotechnol. Bioeng. 56, 232–237.
Halling, P. (1994) Thermodynamic predictions for biocatalysis in non-conventional media: theory, tests and recommendations for experimental design and analysis. Enzyme Microb. Technol. 16, 178–206.
Colombier, S., Tweddell, R., Condoret, J. S., and Marty, A. (1998) Water activity control: a way to improve the efficiency of a continuous lipase esterification. Biotechnol. Bioeng. 60, 362–368.
Marty, A., Chulalaksananukul, W., Willemot, W., and Condoret, J. S. (1992) Kinetics of lipase-catalyzed esterification in supercritical CO2. Biotechnol. Bioeng. 39, 273–280.
Condoret, J. S., Vankan, S., Joulia, X., and Marty, A. (1997) Prediction of water adsorption curves for heterogeneous biocatalysis in organic and supercritical solvents. Chem. Eng. Sci. 52, 213–220.
Wong, J. M. and Johnston, K. P. (1986) Solubilization of biomolecules in carbon dioxide based supercritical fluids. Biotechnol. Process. 2, 29–38.
Marty, A., Manon, S., Ju, D. P., Combes, D., and Condoret, J. S. (1995) The enzymatic reaction-fractionation process in supercritical carbon dioxide. Enzyme Engineering XII, Vol. 750, (Dordick, J. S. and Russell, A. J., eds.), New York Academy of Sciences, New York, pp. 408–411.
Doddema, H. J., Janssens, R. J. J, de Jong, J. P. J., van der Lugt, J. P., and Oostrom, H. H. M. (1990) Enzymatic reactions in supercritical carbon dioxide and integrated product-recovery, 5th European Congress on Biotechnology, Copenhagen (Christiansen, et al., eds.), pp. 239–242.
Adshiri, T., Akiya, H., Chin, L. C., Arai, K., and Fujimoto, K. (1992) Lipase-catalyzed interesterification of triglycerides with supercritical carbon dioxide. J. Chem. Eng. Jpn. 25, 104–105.
Taniguchi, M., Kamihira, M., and Kobayashi, T. (1987) Effect of treatment with supercritical carbon dioxide on enzymatic activity. Agric. Biol. Chem. 51(2), 593–594.
Cernia, E., Palocci, C., Gasparrin, F., Misiti, D., and Fagano, N. (1994) Enantioselectivity and reactivity of immobilized lipase in supercritical carbon dioxide. J. Mol. Catal. 89, L11–L18.
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Marty, A., Condoret, JS. (2001). Enzymatic Transformations in Supercritical Fluids. In: Vulfson, E.N., Halling, P.J., Holland, H.L. (eds) Enzymes in Nonaqueous Solvents. Methods in Biotechnology, vol 15. Humana Press. https://doi.org/10.1385/1-59259-112-4:587
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DOI: https://doi.org/10.1385/1-59259-112-4:587
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