Abstract
Efficient functioning of enzymes in organic solvents by any means opens up new possibilities of applications in biocatalysis. Different methods have been proposed for retaining the catalytic power of enzymes and making them functional in organic solvents. One such promising approach is to investigate the properties of enzymes in water-restricted environment, which is based on enzyme entrapment in reverse micelles.
In reverse micelles enzyme molecules are solubilized in discrete hydrated micelles formed by surfactants within a continuous phase i.e. non-polar organic solvent. Under appropriate conditions these solutions are homogenous, thermodynamically stable and optically transparent. However, there are very few examples of preparative scale enzymatic synthesis in water-in-oil microemulsion. One reason for this is that despite the advantages offered by microemulsion media, product isolation and enzyme reuse from such single-phase liquid medium is more complex than in competing methodologies in which the catalyst is present as a separate solid phase. Therefore, the approach simplifying product isolation, and enzyme reuse from microemulsion based media has been the use of gelled microemulsion system. The potential scope will be discussed.
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References
Buckland B.C., Dunhill P., Lilly M.D. (1975) Biotechnol. Bioeng. 17, 815–826.
Borzeix F., Monot F., Vandecasteele T.P.(1992) Enzyme Microb. Technol. 14, 791–797.
Soni K., Madamwar D. (2001) Process Biochemistry. 36 (7) 607–611
Dabulis K., Klibnov A.M. (1993) Biotechnol. Bioeng. 41, 566–571.
Dordick J.S. (1989) Enzyme Microb. Technol. 11, 194–211.
Janssen A.E.M., Van der Padt A., Van Sonsbeck H.M., Van’t Reit K. (1993) Biotechnol. Bioeng. 41, 95–103.
Svensson I., Wehtje E., Adlercruetz P., Mattiason B. (1994) Biotechnol. Bioeng. 44, 549–559.
Claudia S., Sellapan S., Madamwar D. (1997) Appl. Biochem. Biotechnol. 62, 183–189.
Jaeger K.E., Reetz, M.T. (1998) Tibtech. 16, 396–403.
Khmelnistsky Y.L., Levashov A.V., Klyachko N.L., Martinek K. (1988) Enzyme Microb. Technol. 10,710–724.
Klibnov A.M. (1989) Trends Biochem. Sci. 14, 141–144.
Soni K., Shah C., Madamwar D., (2000) Biocatalysis Biotransformation. 18, 331–341.
Antonini E., Carrea G., Cremonesi P. (1981) Enzyme Microb. Technol. 3, 291–296.
Hedstrom G., Backlund S., Eriksson F., Karlsson S. (1998) Colloids Surf. B. Biointerface, 10, 379–384.
Kamiya N., Murakami E., Goto M., Nakashio F. (1996) J. Ferment. Bioeng. 1, 37–41.
Avramiotis S., Stamatis S., Kolisis F.N., Lianos P., Xenakis A. (1996) Langmuir, 12, 6320–6325.
Fletcher P.D.I., Horsup D.I. (1992) J. Chem. Soc. Faraday Trans, 88, 855–864.
Yang F., Russell A.J. (1994) Biotechnol. Bioeng. 47, 60–70.
Luisi P.L., Giomini M.P., Robinson B.H. (1998) Biochem. Biophys Acta. 947, 209–246.
Martinek K., Levashov A.V., Klyachko N.L., Khmelnitski Y.L., Berezin I.V. (1986) Eur. J. Biochem. 155,453–468.
Winsor P.A. (1968) Chem. Rev. 68, 1–40.
Luisi P.L., Magid L.J. (1986) Crit. Rev. Biochem. 20, 409–474.
Lalitha J., Mulimani V.H. (1996) Biochem. Mol. Boil. Int. 40, 571–598.
Hanahan D.J. (1952) J. Biol. Chem. 195, 199–206.
Bansal V.K., Shah D.O., O’ Connell J.P. (1980) J. Coll. Interf. Sci., 75, 462–469.
Douzou P. (1980) In: Advances in Enzymology, Ed. Meister, A., New York, 51, 30–69.
Rahman R.S., Hatton T.A. (1991) J. Phys. Chem. 95, 1799–1811.
Matzke S.F., Creagh A.L., Hayner C.A., Pransntiz J.M., Blanch H.W. (1992) Biotechnol. Bioeng., 40,91–102.
Wong M., Thomas J.K., Gratzel M. (1976) J. Amer. Chem. Soc, 98, 2391–2397.
Zulauf M., Eicke H.F. (1979) J. Phys. Chem., 83, 480–486.
Douzou P., Keh E., Balny C. (1979) Proc. Nat. Acad. Sci. U.S.A 76, 681–685.
Poon P.H., Wells M.A. (1974) Biochem. J. 13, 4928–4936.
El Seoud O.A. (1984) In: Reverse Micelles: Biological and Technological Relevance of Amphilic Structures in Apolar Media, Ed. Luisi P.L. and Straub B.E. Plenum Press, New York, pp. 81–85.
Fletcher P.D.I., Howe A., Robinson B.H. (1987) J. Chem. Soc. Faraday Trans. 83, 985–1006.
Luis G. P., Valencia-Gonzalez M. J., Diaz-Garcia E.M. (1996) Anales De Quimica Int. 92, 312–319.
Paradkar V.M., Dordick J.S. (1991) Biotechnol. Prog. 7, 330–334.
Lye G.J., Asenjo J.A., Pyle D.L. (1995) Biotechnol. Bioeng. 47, 509–519.
Bru R., Sanchez Ferrer A., Garcia-Carmona F. (1989) Biochem. J. 259, 355–361.
Oldfield C. (1990) Biochem. J. 272, 15–22.
Varhaert R.M.D., Halhorst R., Vermue M., Schaatsma T. J., Veeger G. (1990) Eur. J.Biochem. 187, 59–72.
Klyachko N.L., Levashov A.V., Pshezhetsky A.V., Bogdanova N.G., Berezin I.V., Martinek K. (1986) Eur. J.Biochem. 161, 149–154.
Bru R., Sanchez-Ferrer A., Garcia-Carmona F. (1990) Biochem. J. 268, 679–684.
Volkin D.B., Staubli A., Langer R., Klibanov A.M. (1991) Biotechnol. Bioeng. 37, 843–853.
Barbaric S., Luisi P.L. (1981) J. Am. Chem. Soc. 103, 4239–4244.
Vicente L.C., Aires-Barros R., Empis J.M.A. (1994) J. Chem. Tech. Biotechnol. 60, 291–297.
Martinek K., Levashov A.V., Klyachko N.L., Pantin V.J., Berezin I.V. (1981) Biochem. Biophys. Acta. 657, 227–294.
Hayer D.G., Gulari E. (1991) Biotechnol. Bioeng. 38, 507–517.
Vos K., Lanne C., Vanhoek A., Veeger C., Visser A. (1987) Eur. J. Biochem. 169, 275–282.
Luisi P.L., Luthi P., Tomka I., Prenosil J., Pande A. (1984) Ann. N.Y. Acad. Sci. 434, 549–557.
Hilhorst R., Lanne C., Veeger C. (1983) FEBS Lett. 159, 225–228.
Gajjar L., Singh A., Dubey R.S., Srivastava R.C. (1997) Appl.Biochem. Biotechnol. 66, 159–172.
Hochkoeppler A., Luisi P.L. (1989) Biotechnol. Bioeng. 33, 1477–1481.
Gordana S., Julian, C.B. (1998) Biotechnol. Bioeng. 38, 374–379.
Soni K., Madamwar D. (2000) Process Biochem. 36, 311–315.
Dekker M., Van’triet K., Weijers S.R., Baltussen J.W.A., Laane C., Bijsterbosh B.H. (1986) Chem. Eng. J., 3, 27–33.
Bratko D., Luzar A., Chen S.H. (1988) Bioelectrochem. Bioeng., 20, 291–296.
Oldfield C. (1994) Biotechnol. Genetic. Engg. Rev., 12, 255–327.
Hearing G., Luisi P.L. (1986) J. Phys. Chem., 90, 5892–5895.
Atkinson P.J. (1991) Characterization of microemulsion-based organogels, Ph.D Thesis, University of East Anglia, Norwich, U.K..
Rees G.D., Robinson B.H., Stephenson G.R. (1995) Biochem. Biophys. Acta, 1259, 73–81.
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Madamwar, D., Soni, K. (2003). Biocatalysis in Non-Conventional Media by Entrapment of the Enzyme in Water-Restricted Microenvironment. In: Roussos, S., Soccol, C.R., Pandey, A., Augur, C. (eds) New Horizons in Biotechnology. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-0203-4_10
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DOI: https://doi.org/10.1007/978-94-017-0203-4_10
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