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Volumn , Issue , 2008, Pages 349-386

Biocatalysis in microemulsions

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EID: 85057373562     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9781420089608     Document Type: Chapter
Times cited : (5)

References (198)
  • 1
    • 0022349981 scopus 로고
    • Kinetic properties of a-chymotrypsin in water-in-oil microemulsions: Studies with a variety of substrates and microemulsion systems
    • Fletcher, P.D.I., Rees, G.D., Robinson, B.H., Freedman, R.B. 1985. Kinetic properties of a-chymotrypsin in water-in-oil microemulsions: Studies with a variety of substrates and microemulsion systems. Biochem. Biophys. Acta 832, 204–214.
    • (1985) Biochem. Biophys. Acta , vol.832 , pp. 204-214
    • Fletcher, P.D.I.1    Rees, G.D.2    Robinson, B.H.3    Freedman, R.B.4
  • 4
    • 4243106964 scopus 로고
    • Micellar solubilization of proteins in aprotic solvents and their spectroscopic characterization
    • Luisi, P.L., Bonner, F.J., Pellegrini, A., Wiget, P., Wolf, R. 1979. Micellar solubilization of proteins in aprotic solvents and their spectroscopic characterization. Helv. Chim. Acta 62, 740–753.
    • (1979) Helv. Chim. Acta , vol.62 , pp. 740-753
    • Luisi, P.L.1    Bonner, F.J.2    Pellegrini, A.3    Wiget, P.4    Wolf, R.5
  • 6
    • 0022437125 scopus 로고
    • Solubilization of enzymes and nucleic acids in hydrocarbon micellar solutions
    • Luisi, P.L., Magid, L. 1986. Solubilization of enzymes and nucleic acids in hydrocarbon micellar solutions. CRC Crit. Rev. Biochem. 20, 409–474.
    • (1986) CRC Crit. Rev. Biochem , vol.20 , pp. 409-474
    • Luisi, P.L.1    Magid, L.2
  • 7
    • 0019887698 scopus 로고
    • Micellar solubilization of biopolymers in organic solvents. Activity and conformation of lysozymes in isooctane reverse micelles
    • Grandi, C., Smith, R.E., Luisi, P.L. 1981. Micellar solubilization of biopolymers in organic solvents. Activity and conformation of lysozymes in isooctane reverse micelles. J. Biol. Chem. 256, 837–843.
    • (1981) J. Biol. Chem , vol.256 , pp. 837-843
    • Grandi, C.1    Smith, R.E.2    Luisi, P.L.3
  • 8
    • 0033398404 scopus 로고    scopus 로고
    • Bioorganic reactions in microemulsions: The case of lipases
    • Stamatis, H., Xenakis, A., Kolisis, F.N. 1999. Bioorganic reactions in microemulsions: The case of lipases. Biotechnol. Adv. 17, 293–318.
    • (1999) Biotechnol. Adv , vol.17 , pp. 293-318
    • Stamatis, H.1    Xenakis, A.2    Kolisis, F.N.3
  • 9
    • 0033652902 scopus 로고    scopus 로고
    • Reverse micelles as reaction media for lipases
    • Carvalho, C.M.L., Cabral, J.M.S. 2000. Reverse micelles as reaction media for lipases. Biochimie 82, 1063–1085.
    • (2000) Biochimie , vol.82 , pp. 1063-1085
    • Carvalho, C.M.L.1    Cabral, J.M.S.2
  • 10
    • 0035849650 scopus 로고    scopus 로고
    • Effects of bile salts on the solubility and activity of yeast alcohol dehydrogenase in AOT reversed micelles
    • Yang, H., Kiserowb, D.J., McGown, L.B. 2001. Effects of bile salts on the solubility and activity of yeast alcohol dehydrogenase in AOT reversed micelles. J. Mol. Catal. B: Enzymatic 14, 7–14.
    • (2001) J. Mol. Catal. B: Enzymatic , vol.14 , pp. 7-14
    • Yang, H.1    Kiserowb, D.J.2    McGown, L.B.3
  • 11
    • 12244283989 scopus 로고    scopus 로고
    • Stabilisation of tyrosinase by reversed micelles for bioelectrocatalysis in dry organic media
    • Shipovskov, S., Ferapontova, E., Ruzgas, T., Levashov, A. 2003. Stabilisation of tyrosinase by reversed micelles for bioelectrocatalysis in dry organic media. Biochim. Biophys. Acta 1620, 119–124.
    • (2003) Biochim. Biophys. Acta , vol.1620 , pp. 119-124
    • Shipovskov, S.1    Ferapontova, E.2    Ruzgas, T.3    Levashov, A.4
  • 13
    • 0032920502 scopus 로고    scopus 로고
    • Cutinase stability in AOT reversed micelles: System optimization using the factorial design methodology
    • Carvalho, C.M.L., Cabral, J.M.S., Aires-Barros, M.R. 1999. Cutinase stability in AOT reversed micelles: System optimization using the factorial design methodology. Enzyme Microb. Technol. 24, 569–576.
    • (1999) Enzyme Microb. Technol , vol.24 , pp. 569-576
    • Carvalho, C.M.L.1    Cabral, J.M.S.2    Aires-Barros, M.R.3
  • 14
    • 28244441174 scopus 로고    scopus 로고
    • Online kinetic studies on intermediates of laccase-catalyzed reaction in reversed micelle
    • Liu, Z., Shao, M., Cai, R., Shen, P. 2006. Online kinetic studies on intermediates of laccase-catalyzed reaction in reversed micelle. J. Colloid Interface Sci. 294, 122–128.
    • (2006) J. Colloid Interface Sci , vol.294 , pp. 122-128
    • Liu, Z.1    Shao, M.2    Cai, R.3    Shen, P.4
  • 18
    • 0037036695 scopus 로고    scopus 로고
    • Studies on the catalytic behavior of a cholinesterase-like abzyme in an AOT microemulsion system
    • Franqueville, E., Stamatis, H., Loutrari, H., Friboulet, A., Kolisis, F.N. 2002. Studies on the catalytic behavior of a cholinesterase-like abzyme in an AOT microemulsion system. J. Biotechnol. 97, 177–182.
    • (2002) J. Biotechnol , vol.97 , pp. 177-182
    • Franqueville, E.1    Stamatis, H.2    Loutrari, H.3    Friboulet, A.4    Kolisis, F.N.5
  • 19
    • 0030008420 scopus 로고    scopus 로고
    • The effect of linoic acid on pH inside sodium bis(2-ethylhexyl)sulfosuccinate reverse micelles in isooctane and on the enzymatic activity of soybean lipogenase
    • Rodakiewiecz-Nowak, J., Maslakiewicz, P., Haber, J. 1996. The effect of linoic acid on pH inside sodium bis(2-ethylhexyl)sulfosuccinate reverse micelles in isooctane and on the enzymatic activity of soybean lipogenase. Eur. J. Biochem. 238, 549–553.
    • (1996) Eur. J. Biochem , vol.238 , pp. 549-553
    • Rodakiewiecz-Nowak, J.1    Maslakiewicz, P.2    Haber, J.3
  • 20
    • 0031829838 scopus 로고    scopus 로고
    • Reverse micelle systems composed of water, Triton X100 and phospholipids in organic solvents. 1. Phase boundary titrations and dynamic light scattering analysis
    • Rodriguez, R., Vargas, S., Fernandez-Velasko, D.A. 1998. Reverse micelle systems composed of water, Triton X100 and phospholipids in organic solvents. 1. Phase boundary titrations and dynamic light scattering analysis. J. Colloid Interface Sci. 197, 21.
    • (1998) J. Colloid Interface Sci , vol.197 , pp. 21
    • Rodriguez, R.1    Vargas, S.2    Fernandez-Velasko, D.A.3
  • 21
    • 0031854652 scopus 로고    scopus 로고
    • Reverse micelle systems composed of water, Triton X100 and phospholipids in organic solvents. 2. Catalysis and thermostability of hexokinase
    • Fernandez-Velasko, D.A., Rodriguez, R., Vargas, S., de Gomez-Puyou, M.T., Gomez-Puyou, A. 1998. Reverse micelle systems composed of water, Triton X100 and phospholipids in organic solvents. 2. Catalysis and thermostability of hexokinase. J. Colloid Interface Sci. 197, 29–35.
    • (1998) J. Colloid Interface Sci , vol.197 , pp. 29-35
    • Fernandez-Velasko, D.A.1    Rodriguez, R.2    Vargas, S.3    De Gomez-Puyou, M.T.4    Gomez-Puyou, A.5
  • 22
    • 0034042583 scopus 로고    scopus 로고
    • Entrapment of enzyme in waterrestricted microenvironment—amyloglucosidase in reverse micelles
    • Shah, C., Sellappan, S., Madamwar, D. 2000. Entrapment of enzyme in waterrestricted microenvironment—amyloglucosidase in reverse micelles. Proc. Biochem. 35, 971–975.
    • (2000) Proc. Biochem , vol.35 , pp. 971-975
    • Shah, C.1    Sellappan, S.2    Madamwar, D.3
  • 24
    • 0027112469 scopus 로고
    • Mechanisms of protein solubilization in reverse micelles. Biotechnol
    • Matzke, S.F., Creagh, A.L., Haynes, C.A., Blanch, H.W., Prausnitz, J.M. 1992. Mechanisms of protein solubilization in reverse micelles. Biotechnol. Bioeng. 40, 91–102.
    • (1992) Bioeng , vol.40 , pp. 91-102
    • Matzke, S.F.1    Creagh, A.L.2    Haynes, C.A.3    Blanch, H.W.4    Prausnitz, J.M.5
  • 26
    • 0000366965 scopus 로고
    • Enzymes entrapped in reversed micelles of surfactants in organic solvents: A theoretical treatment of the catalytic activity regulation
    • Kabanov, A.V., Levashov, A.V., Klyachko, N.L., Namyotkin, S.N., Pshezhetsky, A.V. 1988. Enzymes entrapped in reversed micelles of surfactants in organic solvents: A theoretical treatment of the catalytic activity regulation. J. Theor. Biol. 133, 327–343.
    • (1988) J. Theor. Biol , vol.133 , pp. 327-343
    • Kabanov, A.V.1    Levashov, A.V.2    Klyachko, N.L.3    Namyotkin, S.N.4    Pshezhetsky, A.V.5
  • 27
    • 34247198430 scopus 로고    scopus 로고
    • Higher order structure of Mucor miehei lipase and micelle size in cetyltrimethylammonium bromide reverse micellar system
    • Naoe, K., Takeuchi, C., Kawagoe, M., Nagayama, K., Imai, M. 2007. Higher order structure of Mucor miehei lipase and micelle size in cetyltrimethylammonium bromide reverse micellar system. J. Chromatography B 850, 277–284.
    • (2007) J. Chromatography B , vol.850 , pp. 277-284
    • Naoe, K.1    Takeuchi, C.2    Kawagoe, M.3    Nagayama, K.4    Imai, M.5
  • 28
    • 29844456515 scopus 로고    scopus 로고
    • Geometric constraints at the surfactant headgroup: Effect on lipase activity in cationic reverse micelles
    • Mitra, R.N., Dasgupta, A., Das, D., Roy, S., Debnath, S., Das, P.K. 2005. Geometric constraints at the surfactant headgroup: Effect on lipase activity in cationic reverse micelles. Langmuir 21, 12115–12123.
    • (2005) Langmuir , vol.21 , pp. 12115-12123
    • Mitra, R.N.1    Dasgupta, A.2    Das, D.3    Roy, S.4    Debnath, S.5    Das, P.K.6
  • 29
    • 33745432728 scopus 로고    scopus 로고
    • Effect of aprotic solvents on the enzymatic activity of lipase in AOT reverse micelles
    • Moniruzzaman, M., Hayashi, Y., Talukder, M.M.R., Saito, E., Kawanishi, T. 2006. Effect of aprotic solvents on the enzymatic activity of lipase in AOT reverse micelles. Biochem. Engin. J. 30, 237–244.
    • (2006) Biochem. Engin. J , vol.30 , pp. 237-244
    • Moniruzzaman, M.1    Hayashi, Y.2    Talukder, M.M.R.3    Saito, E.4    Kawanishi, T.5
  • 30
    • 33947675351 scopus 로고    scopus 로고
    • Lipasecatalyzed esterification of fatty acid in DMSO (Dimethyl sulfoxide) modified AOT reverse micellar systems
    • Moniruzzaman, M., Hayashi, Y., Talukder, E., Kawanishi, T. 2007. Lipasecatalyzed esterification of fatty acid in DMSO (dimethyl sulfoxide) modified AOT reverse micellar systems. Biocatal. Biotransform. 25, 51–58.
    • (2007) Biocatal. Biotransform , vol.25 , pp. 51-58
    • Moniruzzaman, M.1    Hayashi, Y.2    Talukder, E.3    Kawanishi, T.4
  • 31
    • 34147133377 scopus 로고    scopus 로고
    • Solubilization of enzymes in water-in-oil microemulsions and their rapid and efficient release through use of a pH-degradable surfactant
    • Rairkar, M.E., Hayes, D.G., Harris, Ζ.J.M. 2007. Solubilization of enzymes in water-in-oil microemulsions and their rapid and efficient release through use of a pH-degradable surfactant. Biotechnol. Lett. 29, 767–771.
    • (2007) Biotechnol. Lett , vol.29 , pp. 767-771
    • Rairkar, M.E.1    Hayes, D.G.2    Harris, Ζ.J.M.3
  • 32
    • 0032550818 scopus 로고    scopus 로고
    • Sucrose enhances the recovery and activity of ribonuclease A during reversed micelle extraction
    • Spirovska, G., Chaudhuri, J.B. 1998. Sucrose enhances the recovery and activity of ribonuclease A during reversed micelle extraction. Biotechnol. Bioeng. 58, 374–379.
    • (1998) Biotechnol. Bioeng , vol.58 , pp. 374-379
    • Spirovska, G.1    Chaudhuri, J.B.2
  • 33
    • 0033192975 scopus 로고    scopus 로고
    • Effect of hydration degree of aerosolOT reversed micelles and surfactant concentration in heptane on spectral and catalytic properties of catalase
    • Eryomin, A.N., Metelitza, D.I. 1999. Effect of hydration degree of aerosolOT reversed micelles and surfactant concentration in heptane on spectral and catalytic properties of catalase. Biochemistry (Moscow) 64, 1049–1060.
    • (1999) Biochemistry (Moscow) , vol.64 , pp. 1049-1060
    • Eryomin, A.N.1    Metelitza, D.I.2
  • 34
    • 0343953095 scopus 로고    scopus 로고
    • Effects of ionic surfactants used in reversed micelles on cutinase activity and stability
    • Goncalves, A.M., Serrob, A.P., Aires-Barros, M.R., Cabral, J.M. 2000. Effects of ionic surfactants used in reversed micelles on cutinase activity and stability. Biochim. Biophys. Acta 1480, 92–106.
    • (2000) Biochim. Biophys. Acta , vol.1480 , pp. 92-106
    • Goncalves, A.M.1    Serrob, A.P.2    Aires-Barros, M.R.3    Cabral, J.M.4
  • 35
    • 0036357694 scopus 로고    scopus 로고
    • Enzyme catalysis in reverse micelles
    • Scheper Th (Ed.), Heidelberg: Springer-Verlag
    • Orlich, B., Schomacker, R. 2002. Enzyme catalysis in reverse micelles. In Scheper Th (Ed.), Advances in Biochemical Engineering/Biotechnology, Vol. 75, pp. 185–209. Heidelberg: Springer-Verlag.
    • (2002) Advances in Biochemical Engineering/Biotechnology , vol.75 , pp. 185-209
    • Orlich, B.1    Schomacker, R.2
  • 36
    • 0000135323 scopus 로고
    • Micellar enzymnology: Potentialities in applied areas (biotechnology). Coll. Czechoslovak
    • Martinek, K., Berezin, I.V., Khmelnitsky, Y.L., Klyachko, N.L., Levashov, A.V. 1987. Micellar enzymnology: Potentialities in applied areas (biotechnology). Coll. Czechoslovak. Chem. Commun. 52, 2589–2602.
    • (1987) Chem. Commun , vol.52 , pp. 2589-2602
    • Martinek, K.1    Berezin, I.V.2    Khmelnitsky, Y.L.3    Klyachko, N.L.4    Levashov, A.V.5
  • 37
    • 0025372085 scopus 로고
    • Kinetic theory of enzymatic reactions in reversed micellar systems. Application of the pseudophase approach for partitioning substrates
    • Khmelnitsky, Y.L., Neverova, I.N., Polyakov, V.I., Grinberg, V.Y., Levashov, A.V., Martinek, K. 1990. Kinetic theory of enzymatic reactions in reversed micellar systems. Application of the pseudophase approach for partitioning substrates. Eur. J. Biochem. 190, 155–159.
    • (1990) Eur. J. Biochem , vol.190 , pp. 155-159
    • Khmelnitsky, Y.L.1    Neverova, I.N.2    Polyakov, V.I.3    Grinberg, V.Y.4    Levashov, A.V.5    Martinek, K.6
  • 39
    • 0027912424 scopus 로고
    • Proteolytic activity in various water-in-oil microemulsions as related to the polarity of the reaction medium
    • Papadimitriou, V., Xenakis, A., Evangelopoulos, A.E. 1993. Proteolytic activity in various water-in-oil microemulsions as related to the polarity of the reaction medium. Colloids Surf. B. Biointerf. 1, 295–303.
    • (1993) Colloids Surf. B. Biointerf , vol.1 , pp. 295-303
    • Papadimitriou, V.1    Xenakis, A.2    Evangelopoulos, A.E.3
  • 40
    • 0025505642 scopus 로고
    • Enhanced enzymatic activity in reverse micelles
    • Ruckhenstein, E., Karpe, P. 1990. Enhanced enzymatic activity in reverse micelles. Eur. J. Biochem. 139, 408–436.
    • (1990) Eur. J. Biochem , vol.139 , pp. 408-436
    • Ruckhenstein, E.1    Karpe, P.2
  • 41
    • 10844238892 scopus 로고    scopus 로고
    • Microemulsions as microreactors for food applications
    • Garti, N. 2003. Microemulsions as microreactors for food applications. Curr. Opinion Colloid Interface Sci. 8, 197–211.
    • (2003) Curr. Opinion Colloid Interface Sci , vol.8 , pp. 197-211
    • Garti, N.1
  • 42
    • 0027909380 scopus 로고
    • Esterification reactions catalyzed by lipases in microemulsions. The role of enzyme localization in relation to its selectivity
    • Stamatis, H., Xenakis, A., Provelegiou, M., Kolisis, F.N. 1993. Esterification reactions catalyzed by lipases in microemulsions. The role of enzyme localization in relation to its selectivity. Biotechnol. Bioeng. 42, 103–110.
    • (1993) Biotechnol. Bioeng , vol.42 , pp. 103-110
    • Stamatis, H.1    Xenakis, A.2    Provelegiou, M.3    Kolisis, F.N.4
  • 44
    • 0000826402 scopus 로고
    • Enzymatic synthesis of hydrocarbon-soluble peptides with reverse micelles
    • Lüthi, P., Luisi, P.L. 1984. Enzymatic synthesis of hydrocarbon-soluble peptides with reverse micelles. J. Am. Chem. Soc. 106, 7285–7286.
    • (1984) J. Am. Chem. Soc , vol.106 , pp. 7285-7286
    • Lüthi, P.1    Luisi, P.L.2
  • 45
    • 0025700511 scopus 로고
    • Esterification reactions of lipase in reverse micelles
    • Hayes, D.G., Gulari, E. 1990. Esterification reactions of lipase in reverse micelles. Biotechnol. Bioeng. 35, 793–801.
    • (1990) Biotechnol. Bioeng , vol.35 , pp. 793-801
    • Hayes, D.G.1    Gulari, E.2
  • 47
    • 0027161627 scopus 로고
    • Enantiomeric selectivity of a lipase from Penicillium simplicissimum in the esterification of menthol in microemulsions
    • Stamatis, H., Kolisis, F.N., Xenakis, A. 1993. Enantiomeric selectivity of a lipase from Penicillium simplicissimum in the esterification of menthol in microemulsions. Biotechnol. Lett. 15, 471–476.
    • (1993) Biotechnol. Lett , vol.15 , pp. 471-476
    • Stamatis, H.1    Kolisis, F.N.2    Xenakis, A.3
  • 48
    • 0029635982 scopus 로고
    • Catalytic behavior of Pseudomonas cepacia lipase in w/o microemulsions
    • Stamatis, H., Xenakis, A., Dimitriadis, E., Kolisis, F.N. 1995. Catalytic behavior of Pseudomonas cepacia lipase in w/o microemulsions. Biotechnol. Bioeng. 45, 33–41.
    • (1995) Biotechnol. Bioeng , vol.45 , pp. 33-41
    • Stamatis, H.1    Xenakis, A.2    Dimitriadis, E.3    Kolisis, F.N.4
  • 49
    • 0036231930 scopus 로고    scopus 로고
    • Synthetic applications of enzymes entrapped in reverse micelles and organo-gels
    • Fadnavis, N.W., Deshpande, A. 2002. Synthetic applications of enzymes entrapped in reverse micelles and organo-gels. Curr. Org. Chem. 6, 393–410.
    • (2002) Curr. Org. Chem , vol.6 , pp. 393-410
    • Fadnavis, N.W.1    Deshpande, A.2
  • 50
    • 0021676608 scopus 로고
    • Rules for the regulation of enzyme activity in reversed micelles as illustrated by the conversion of apolar steroids by 20-b-hydroxysteroid dehydrogenase
    • Hilhorst, R., Spruijt, R., Laane, C., Verger, C. 1984. Rules for the regulation of enzyme activity in reversed micelles as illustrated by the conversion of apolar steroids by 20-b-hydroxysteroid dehydrogenase. Eur. J. Biochem. 144, 459–462.
    • (1984) Eur. J. Biochem , vol.144 , pp. 459-462
    • Hilhorst, R.1    Spruijt, R.2    Laane, C.3    Verger, C.4
  • 52
    • 3042587428 scopus 로고    scopus 로고
    • Electrontransfer reactions and functionalization of cytochrome P450cam monooxygenase system in reverse micelles
    • Ichinose, H., Michizoe, J., Maruyama, T., Kamiya, N., Goto, M. 2004. Electrontransfer reactions and functionalization of cytochrome P450cam monooxygenase system in reverse micelles. Langmuir 20, 5564–5568.
    • (2004) Langmuir , vol.20 , pp. 5564-5568
    • Ichinose, H.1    Michizoe, J.2    Maruyama, T.3    Kamiya, N.4    Goto, M.5
  • 53
    • 33846440592 scopus 로고    scopus 로고
    • Using reverse micelles as microreactor for hydrogen production by coupled systems of Nostoc/R. Palustris and Anabaena/R. palustris
    • Pandey, A., Pandey, A., Srivastava, P., Pandey, A. 2007. Using reverse micelles as microreactor for hydrogen production by coupled systems of Nostoc/R. palustris and Anabaena/R. palustris. World J. Microbiol. Biotechnol. 23, 269–274.
    • (2007) World J. Microbiol. Biotechnol , vol.23 , pp. 269-274
    • Pandey, A.1    Pandey, A.2    Srivastava, P.3    Pandey, A.4
  • 54
    • 0027909088 scopus 로고
    • Catalytic and interfacial aspects of enzymatic polymer synthesis in reversed micellar systems. Biotechnol
    • Rao, A.M., John, V.T., Gonzalez, R.D., Akkara, J.A., Kaplan, D.L. 1993. Catalytic and interfacial aspects of enzymatic polymer synthesis in reversed micellar systems. Biotechnol. Bioeng. 41, 531–540.
    • (1993) Bioeng , vol.41 , pp. 531-540
    • Rao, A.M.1    John, V.T.2    Gonzalez, R.D.3    Akkara, J.A.4    Kaplan, D.L.5
  • 55
    • 15844394205 scopus 로고
    • Enzyme catalysis in water pools
    • Menger, F.M., Yamada, K. 1979. Enzyme catalysis in water pools. J. Am. Chem. Soc. 101, 6731–6734.
    • (1979) J. Am. Chem. Soc , vol.101 , pp. 6731-6734
    • Menger, F.M.1    Yamada, K.2
  • 56
    • 0019880222 scopus 로고
    • The principles of enzyme stabilization. VI. Catalysis by water-soluble enzymes entrapped into reversed micelles of surfactants in organic solvents
    • Martinek, K., Levashov, A.V., Klyachko, N.L., Pantin, V.I., Berezin, I.V. 1981. The principles of enzyme stabilization. VI. Catalysis by water-soluble enzymes entrapped into reversed micelles of surfactants in organic solvents. Biochim. Biophys. Acta 657, 277–294.
    • (1981) Biochim. Biophys. Acta , vol.657 , pp. 277-294
    • Martinek, K.1    Levashov, A.V.2    Klyachko, N.L.3    Pantin, V.I.4    Berezin, I.V.5
  • 57
    • 0030662708 scopus 로고    scopus 로고
    • Peptide bond formation by the industrial protease, neutrase, in organic media
    • Clapes, P., Pera, E., Torres, J.L. 1997. Peptide bond formation by the industrial protease, neutrase, in organic media. Biotechnol. Lett. 19, 1023–1026.
    • (1997) Biotechnol. Lett , vol.19 , pp. 1023-1026
    • Clapes, P.1    Pera, E.2    Torres, J.L.3
  • 58
    • 27544487735 scopus 로고    scopus 로고
    • Microbial proteases in peptide synthesis. Approaches and applications
    • Kumar, D., Bhalla, T.C. 2005. Microbial proteases in peptide synthesis. Approaches and applications. Appl. Microbiol. Biotechnol. 68, 726–736.
    • (2005) Appl. Microbiol. Biotechnol , vol.68 , pp. 726-736
    • Kumar, D.1    Bhalla, T.C.2
  • 59
    • 0032143896 scopus 로고    scopus 로고
    • Protease catalyzed synthesis of precursor dipeptides of RGD with reverse micelles
    • Chen, Y.X., Zhang, X.Z., Zheng, K., Chen, S.M., Wang, Q.C., Wu, X.X. 1998. Protease catalyzed synthesis of precursor dipeptides of RGD with reverse micelles. Enzyme Microb. Technol. 23, 243–248.
    • (1998) Enzyme Microb. Technol , vol.23 , pp. 243-248
    • Chen, Y.X.1    Zhang, X.Z.2    Zheng, K.3    Chen, S.M.4    Wang, Q.C.5    Wu, X.X.6
  • 60
    • 0033179764 scopus 로고    scopus 로고
    • Kinetically controlled syntheses catalyzed by proteases in reverse micelles and separation of precursor dipeptides of RGD
    • Chen, Y.X., Zhang, X.Z., Chen, S.M., You, D.L., Wu, X.X., Yang, X.C., Guan, W.Z. 1999. Kinetically controlled syntheses catalyzed by proteases in reverse micelles and separation of precursor dipeptides of RGD. Enzyme Microb. Technol. 25, 310–315.
    • (1999) Enzyme Microb. Technol , vol.25 , pp. 310-315
    • Chen, Y.X.1    Zhang, X.Z.2    Chen, S.M.3    You, D.L.4    Wu, X.X.5    Yang, X.C.6    Guan, W.Z.7
  • 61
    • 33748226769 scopus 로고
    • Protease-catalyzed kinetically controlled peptide synthesis
    • Schellenberger, V., Jakube, H.D. 1991. Protease-catalyzed kinetically controlled peptide synthesis. Angew. Chem. Int. Ed. Engl. 30, 1437-1449.
    • (1991) Angew. Chem. Int. Ed. Engl , vol.30 , pp. 1437-1449
    • Schellenberger, V.1    Jakube, H.D.2
  • 63
    • 0026816712 scopus 로고
    • Optimization and kinetic studies of the enzymatic synthesis of Ac-Phe-Leu-NH2 in reversed micelles
    • Jorba, X., Clapés, P., Xaus, N., Calvet, S., Torres, J.L., Valencia, G., Mata, J. 1992. Optimization and kinetic studies of the enzymatic synthesis of Ac-Phe-Leu-NH2 in reversed micelles. Enzyme Microb. Technol. 14, 117–124.
    • (1992) Enzyme Microb. Technol , vol.14 , pp. 117-124
    • Jorba, X.1    Clapés, P.2    Xaus, N.3    Calvet, S.4    Torres, J.L.5    Valencia, G.6    Mata, J.7
  • 64
    • 0001866641 scopus 로고
    • Ethyl acetate modified AOT water-in-oil microemulsions for the α-chymotrypsin catalyzed synthesis of a model dipeptide derivative
    • Jorba, X., Clapés, P., Torres, J.L., Valencia, G., Mata-Alvarez, J. 1995. Ethyl acetate modified AOT water-in-oil microemulsions for the α-chymotrypsin catalyzed synthesis of a model dipeptide derivative. Colloids Surf. A 96, 47–52.
    • (1995) Colloids Surf. A , vol.96 , pp. 47-52
    • Jorba, X.1    Clapés, P.2    Torres, J.L.3    Valencia, G.4    Mata-Alvarez, J.5
  • 65
    • 0028626281 scopus 로고
    • Dipeptide synthesis and separation in a reversed micellar membrane reactor
    • Serralheiro, M.L.M., Prazeres, D.M.F., Cabral, J.M.S. 1994. Dipeptide synthesis and separation in a reversed micellar membrane reactor. Enzyme Microb. Technol. 16, 1064–1073.
    • (1994) Enzyme Microb. Technol , vol.16 , pp. 1064-1073
    • Serralheiro, M.L.M.1    Prazeres, D.M.F.2    Cabral, J.M.S.3
  • 66
    • 0033525662 scopus 로고    scopus 로고
    • Enzymatic synthesis of oligopeptides in mixed reverse micelles
    • Xing, G.W., Liu, D.J., Ye, Y.H., Ma, J.M. 1999. Enzymatic synthesis of oligopeptides in mixed reverse micelles. Tetrahedron Lett. 40, 1971–1974.
    • (1999) Tetrahedron Lett , vol.40 , pp. 1971-1974
    • Xing, G.W.1    Liu, D.J.2    Ye, Y.H.3    Ma, J.M.4
  • 67
    • 0035182282 scopus 로고    scopus 로고
    • Enhancement of the activity of papain in mixed reverse micellar systems in the presence of Tween 80
    • Fan, K.K., Ouyang, P., Wu, X., Lu, Z.J. 2001. Enhancement of the activity of papain in mixed reverse micellar systems in the presence of Tween 80. Chem. Technol. Biotechnol. 76, 27–30.
    • (2001) Chem. Technol. Biotechnol , vol.76 , pp. 27-30
    • Fan, K.K.1    Ouyang, P.2    Wu, X.3    Lu, Z.J.4
  • 68
    • 33845557550 scopus 로고
    • Micellar solubilization of biopolymers in organic solvents. Activity and conformation of α-chymotrypsin in isooctane–AOT reverse micelles
    • Barbaric, S., Luisi, P.L. 1981. Micellar solubilization of biopolymers in organic solvents. Activity and conformation of α-chymotrypsin in isooctane–AOT reverse micelles. J. Am. Chem. Soc. 103, 4239–4244.
    • (1981) J. Am. Chem. Soc , vol.103 , pp. 4239-4244
    • Barbaric, S.1    Luisi, P.L.2
  • 69
    • 0025676095 scopus 로고
    • Kinetic properties of enzymes in AOT–isooctane reversed micelles
    • Ishikawa, H., Noda, K., Oka, T. 1990. Kinetic properties of enzymes in AOT–isooctane reversed micelles. J. Ferment. Bioeng. 70, 381–385.
    • (1990) J. Ferment. Bioeng , vol.70 , pp. 381-385
    • Ishikawa, H.1    Noda, K.2    Oka, T.3
  • 70
    • 0026756936 scopus 로고
    • Kinetic behavior of α-chymotrypsin in reverse micelles. A stopped-flow study
    • Mao, Q., Walde, P., Luisi, P.L. 1992. Kinetic behavior of α-chymotrypsin in reverse micelles. A stopped-flow study. Eur. J. Biochem. 208, 165–170.
    • (1992) Eur. J. Biochem , vol.208 , pp. 165-170
    • Mao, Q.1    Walde, P.2    Luisi, P.L.3
  • 72
    • 0025215312 scopus 로고
    • The behavior of proteases in lecithin reverse micelles
    • Peng, Q., Luisi, P.L. 1990. The behavior of proteases in lecithin reverse micelles. Eur. J. Biochem. 188, 471–480.
    • (1990) Eur. J. Biochem , vol.188 , pp. 471-480
    • Peng, Q.1    Luisi, P.L.2
  • 73
    • 0031348870 scopus 로고    scopus 로고
    • Trypsin in lecithin based (W/o) microemulsions. Fluorescence and enzyme activity studies. Biocatal
    • Avramiotis, S., Lianos, P., Xenakis, A. 1997. Trypsin in lecithin based (w/o) microemulsions. Fluorescence and enzyme activity studies. Biocatal. Biotransform. 14, 299–316.
    • (1997) Biotransform , vol.14 , pp. 299-316
    • Avramiotis, S.1    Lianos, P.2    Xenakis, A.3
  • 74
    • 0032299971 scopus 로고    scopus 로고
    • Reactivity of trypsin in reverse micelles: PH-effects, on the wo versus enzyme activity profiles
    • Fadnavis, N.W.; Babu, R.L., Deshpande, A. 1998. Reactivity of trypsin in reverse micelles: pH-effects, on the wo versus enzyme activity profiles. Biochimie 80, 1025–1030.
    • (1998) Biochimie , vol.80 , pp. 1025-1030
    • Fadnavis, N.W.1    Babu, R.L.2    Deshpande, A.3
  • 75
    • 27644592016 scopus 로고    scopus 로고
    • Reactivity of trypsin in reverse micelles: Neglected role of aggregate size compared to water-pool components
    • Dasgupta, A., Das, D., Das, P.K. 2005. Reactivity of trypsin in reverse micelles: Neglected role of aggregate size compared to water-pool components. Biochimie 87, 1111–1119.
    • (2005) Biochimie , vol.87 , pp. 1111-1119
    • Dasgupta, A.1    Das, D.2    Das, P.K.3
  • 77
    • 0028474144 scopus 로고
    • Stability and proteolytic activity of papain in reverse micellar and aqueous media: A kinetic and spectroscopic study
    • Vicente, L.C., Aires-Barros, R., Empis, J.M. 1994. Stability and proteolytic activity of papain in reverse micellar and aqueous media: A kinetic and spectroscopic study. J. Chem. Tech. Biotechnol. 60, 291–297.
    • (1994) J. Chem. Tech. Biotechnol , vol.60 , pp. 291-297
    • Vicente, L.C.1    Aires-Barros, R.2    Empis, J.M.3
  • 78
    • 0018890516 scopus 로고
    • Enzyme kinetics of lipolysis
    • Colowick SP, Kaplan NO (Eds.), New York: Academic Press
    • Verger, R. 1980 Enzyme kinetics of lipolysis. In Colowick SP, Kaplan NO (Eds.). Methods in Enzymology, Vol. 64B, pp. 340–92. New York: Academic Press.
    • (1980) Methods in Enzymology , vol.64B , pp. 340-392
    • Verger, R.1
  • 79
    • 0027388770 scopus 로고
    • News from the interface: The molecular structures of triacylglyceride lipases
    • Derewenda, Z.S., Sharp, A.M. 1993 News from the interface: The molecular structures of triacylglyceride lipases. Trends Biochem. Sci. 205, 20–25.
    • (1993) Trends Biochem. Sci , vol.205 , pp. 20-25
    • Derewenda, Z.S.1    Sharp, A.M.2
  • 80
    • 0027703821 scopus 로고
    • Effects of the interaction of porcine pancreatic lipase with AOT/isooctane reversed micelles on enzyme structure and function follow predictable patterns
    • Marangoni, A.G. 1993 Effects of the interaction of porcine pancreatic lipase with AOT/isooctane reversed micelles on enzyme structure and function follow predictable patterns. Enzyme Microb. Technol. 15, 944–949.
    • (1993) Enzyme Microb. Technol , vol.15 , pp. 944-949
    • Marangoni, A.G.1
  • 81
    • 0029201693 scopus 로고
    • Surfactant effects on lipase catalyzed hydrolysis of olive oil in AOT/isooctane reverse micelles
    • Tsai, S.W., Lee, K.P., Chiang, C.L. 1995. Surfactant effects on lipase catalyzed hydrolysis of olive oil in AOT/isooctane reverse micelles. Biocatal. Biotrans. 13, 89–98.
    • (1995) Biocatal. Biotrans , vol.13 , pp. 89-98
    • Tsai, S.W.1    Lee, K.P.2    Chiang, C.L.3
  • 82
    • 0027395168 scopus 로고
    • The dependence of the lipolytic activity of R. Arrhizus lipase on surfactant concentration in Aerosol-OT/isooctane reverse micelles and its relationship to enzyme structure
    • Brown, E.D., Yada, R.Y., Marangoni, A.G. 1993. The dependence of the lipolytic activity of R. arrhizus lipase on surfactant concentration in Aerosol-OT/isooctane reverse micelles and its relationship to enzyme structure. Biochim. Biophys. Acta 1161, 66–72.
    • (1993) Biochim. Biophys. Acta , vol.1161 , pp. 66-72
    • Brown, E.D.1    Yada, R.Y.2    Marangoni, A.G.3
  • 83
    • 0028798976 scopus 로고
    • Comparison of hydrolysis and esterification behavior of Humicola lanuginosa and Rhizomucor miehei lipases in AOT-stabilized water-in-oil microemulsions: II. Effect of temperature on reaction kinetics and general considerations of stability and productivity
    • Crooks, G.E., Rees, G.D., Robinson, B.H., Svensson, M., Stephenson, G.R. 1995. Comparison of hydrolysis and esterification behavior of Humicola lanuginosa and Rhizomucor miehei lipases in AOT-stabilized water-in-oil microemulsions: II. Effect of temperature on reaction kinetics and general considerations of stability and productivity. Biotechnol. Bioeng. 48, 190–196.
    • (1995) Biotechnol. Bioeng , vol.48 , pp. 190-196
    • Crooks, G.E.1    Rees, G.D.2    Robinson, B.H.3    Svensson, M.4    Stephenson, G.R.5
  • 84
    • 27644498535 scopus 로고    scopus 로고
    • Kinetics of lipase-catalyzed hydrolysis of olive oil in AOT/isooctane reversed micelles
    • Yao, C., Tang, S., Heb, Z., Deng, X. 2005. Kinetics of lipase-catalyzed hydrolysis of olive oil in AOT/isooctane reversed micelles. J. Mol. Catal. B: Enzym. 35, 108–112.
    • (2005) J. Mol. Catal. B: Enzym , vol.35 , pp. 108-112
    • Yao, C.1    Tang, S.2    Heb, Z.3    Deng, X.4
  • 85
    • 0022769859 scopus 로고
    • Characteristics of lipase-catalyzed hydrolysis of olive oil in AOT–isooctane reversed micelles
    • Han, D., Rhee, J.S. 1986. Characteristics of lipase-catalyzed hydrolysis of olive oil in AOT–isooctane reversed micelles. Biotechnol. Bioeng. 28, 1250–1255.
    • (1986) Biotechnol. Bioeng , vol.28 , pp. 1250-1255
    • Han, D.1    Rhee, J.S.2
  • 86
    • 0023400517 scopus 로고
    • Lipase reaction in AOT–isooctane reversed micelles: Effect of water on equilibria
    • Han, D., Rhee, J.S., Lee, S.B. 1987. Lipase reaction in AOT–isooctane reversed micelles: Effect of water on equilibria. Biotechnol. Bioeng. 30, 381–388.
    • (1987) Biotechnol. Bioeng , vol.30 , pp. 381-388
    • Han, D.1    Rhee, J.S.2    Lee, S.B.3
  • 87
    • 0027651846 scopus 로고
    • Kinetic study of lipase catalyzed esterification reactions in microemulsions
    • Stamatis, H., Xenakis, A., Menge, U., Kolisis, F.N. 1993. Kinetic study of lipase catalyzed esterification reactions in microemulsions. Biotechnol. Bioeng. 42, 931–937.
    • (1993) Biotechnol. Bioeng , vol.42 , pp. 931-937
    • Stamatis, H.1    Xenakis, A.2    Menge, U.3    Kolisis, F.N.4
  • 88
    • 0028910485 scopus 로고
    • Influence of the hydrophobicity of lipase isoenzymes from Candida rugosa on its hydrolytic activity in reverse micelles
    • Otero, C., Rua, M.L., Robledo, L. 1995. Influence of the hydrophobicity of lipase isoenzymes from Candida rugosa on its hydrolytic activity in reverse micelles. FEBS Lett. 360, 202–206.
    • (1995) FEBS Lett , vol.360 , pp. 202-206
    • Otero, C.1    Rua, M.L.2    Robledo, L.3
  • 89
    • 0029154825 scopus 로고
    • Macrocyclic lactone synthesis by lipases in water-in-oil microemulsions
    • Rees, G.D., Robinson, B.H., Stephenson, R.G. 1995. Macrocyclic lactone synthesis by lipases in water-in-oil microemulsions. Biochim. Biophys. Acta 1257, 239–248.
    • (1995) Biochim. Biophys. Acta , vol.1257 , pp. 239-248
    • Rees, G.D.1    Robinson, B.H.2    Stephenson, R.G.3
  • 90
    • 12744281803 scopus 로고    scopus 로고
    • Enhanced activity and stability of Chromobacterium viscosum lipase in AOT reverse micellar systems by pretreatment with acetone
    • Zaman, M.M., Hayashi, Y., Talukder, M.M.R., Kawanishi, T. 2005. Enhanced activity and stability of Chromobacterium viscosum lipase in AOT reverse micellar systems by pretreatment with acetone. J. Mol. Catal. B: Enzym. 32, 149–155.
    • (2005) J. Mol. Catal. B: Enzym , vol.32 , pp. 149-155
    • Zaman, M.M.1    Hayashi, Y.2    Talukder, M.M.R.3    Kawanishi, T.4
  • 91
    • 0023034091 scopus 로고
    • Proteins and peptides in water-restricted environments
    • Waks, M. 1986. Proteins and peptides in water-restricted environments. Proteins 1, 4–12.
    • (1986) Proteins , vol.1 , pp. 4-12
    • Waks, M.1
  • 92
    • 0027215015 scopus 로고
    • Spectroscopic and kinetic studies of lipase solubilized in reverse micelles
    • Walde, P., Han, D., Luisi, P.L. 1993. Spectroscopic and kinetic studies of lipase solubilized in reverse micelles. Biochemistry 32, 4029–4034.
    • (1993) Biochemistry , vol.32 , pp. 4029-4034
    • Walde, P.1    Han, D.2    Luisi, P.L.3
  • 93
    • 0020688462 scopus 로고
    • A new approach to the study of enzymatic reactions with the participation of waterinsoluble substrates. Pancreatic lipase enclosed in inverted micelles of surfaceactive substances in an organic solvent
    • Malakhova, E.A., Kurganov, B.I., Levashov, A.V., Berezin, I.V., Martinek, K. 1983. A new approach to the study of enzymatic reactions with the participation of waterinsoluble substrates. Pancreatic lipase enclosed in inverted micelles of surfaceactive substances in an organic solvent. Dokl. Akad. Nauk. SSSR 270, 474–477.
    • (1983) Dokl. Akad. Nauk. SSSR , vol.270 , pp. 474-477
    • Malakhova, E.A.1    Kurganov, B.I.2    Levashov, A.V.3    Berezin, I.V.4    Martinek, K.5
  • 94
    • 0000323853 scopus 로고
    • Enzymatic preparation of monoglycerides in microemulsion
    • Holmberg, K., Osterberg, E. 1988. Enzymatic preparation of monoglycerides in microemulsion. J. Am. Oil Chem. Soc. 65, 1544–1548.
    • (1988) J. Am. Oil Chem. Soc , vol.65 , pp. 1544-1548
    • Holmberg, K.1    Osterberg, E.2
  • 95
    • 0027249528 scopus 로고
    • Lipase catalyzed hydrolysis of milk fat in lecithin reverse micelles
    • Chen, J.P., Chang, K.-C. 1993. Lipase catalyzed hydrolysis of milk fat in lecithin reverse micelles. J. Ferment. Bioeng. 76, 98–104.
    • (1993) J. Ferment. Bioeng , vol.76 , pp. 98-104
    • Chen, J.P.1    Chang, K.-C.2
  • 97
    • 0025418282 scopus 로고
    • Depedence of the activity of Rhizopus lipase on microemulsion composition
    • Stark, M., Scagerlind, P., Holmberg, K., Carlfors, J. 1990. Depedence of the activity of Rhizopus lipase on microemulsion composition. Colloid Polym. Sci. 268, 384–388.
    • (1990) Colloid Polym. Sci , vol.268 , pp. 384-388
    • Stark, M.1    Scagerlind, P.2    Holmberg, K.3    Carlfors, J.4
  • 98
    • 0000819158 scopus 로고
    • Comparative studies of lipase from Rhizopus delemar in various microemulsion systems
    • Valis, T.P., Xenakis, A., Kolisis, F.N. 1992. Comparative studies of lipase from Rhizopus delemar in various microemulsion systems. Biocatalysis 6, 267–279.
    • (1992) Biocatalysis , vol.6 , pp. 267-279
    • Valis, T.P.1    Xenakis, A.2    Kolisis, F.N.3
  • 99
    • 0027661580 scopus 로고
    • Increased activity of Chromobacterium viscosum lipase in aerosol OT reverse micelles in the presence of nonionic surfactants
    • Yamada, Y., Kuboi, R., Komasawa, I. 1993. Increased activity of Chromobacterium viscosum lipase in aerosol OT reverse micelles in the presence of nonionic surfactants. Biotechnol. Prog. 9, 468–472.
    • (1993) Biotechnol. Prog , vol.9 , pp. 468-472
    • Yamada, Y.1    Kuboi, R.2    Komasawa, I.3
  • 100
    • 0027697244 scopus 로고
    • 1,3-Specific lipolysis of Lesquerella fendleri oil by immobilized and reverse-micellar encapsulated enzymes
    • Hayes, D.G., Kleiman, R. 1993. 1,3-Specific lipolysis of Lesquerella fendleri oil by immobilized and reverse-micellar encapsulated enzymes. J. Am. Oil Chem. Soc. 70, 1121–1127.
    • (1993) J. Am. Oil Chem. Soc , vol.70 , pp. 1121-1127
    • Hayes, D.G.1    Kleiman, R.2
  • 101
    • 0001104616 scopus 로고
    • Enzymatic reaction in water-in-oil microemulsions. Part 1. Rate of hydrolysis of a hydrophilic substrate: Acetylsalicylic acid
    • Miyake, Y., Owari, T., Matsuura, K, Teramoto M, 1993. Enzymatic reaction in water-in-oil microemulsions. Part 1. Rate of hydrolysis of a hydrophilic substrate: Acetylsalicylic acid. J. Chem. Soc. Faraday Trans. 89, 1993–1999.
    • (1993) J. Chem. Soc. Faraday Trans , vol.89 , pp. 1993-1999
    • Miyake, Y.1    Owari, T.2    Matsuura, K.3    Teramoto, M.4
  • 103
    • 2342631985 scopus 로고    scopus 로고
    • Hydrolysis and synthesis reactions catalysed by Thermomyces lanuginosa lipase in the AOT/isooctane reversed micellar system
    • Fernandes, M.L.M., Krieger, N., Baron, A.M., Zamora, P.P., Ramos, L.P., Mitchell, D.A. 2004. Hydrolysis and synthesis reactions catalysed by Thermomyces lanuginosa lipase in the AOT/isooctane reversed micellar system. J. Mol. Catal. B: Enzym. 30, 43–49.
    • (2004) J. Mol. Catal. B: Enzym , vol.30 , pp. 43-49
    • Fernandes, M.L.M.1    Krieger, N.2    Baron, A.M.3    Zamora, P.P.4    Ramos, L.P.5    Mitchell, D.A.6
  • 104
    • 34247366868 scopus 로고    scopus 로고
    • Nonionic surfactants: A key to enhance the enzyme activity at cationic reverse micellar interface
    • Shome, A., Roy, S., Das, P.K. 2007. Nonionic surfactants: A key to enhance the enzyme activity at cationic reverse micellar interface. Langmuir 23, 4130–4136.
    • (2007) Langmuir , vol.23 , pp. 4130-4136
    • Shome, A.1    Roy, S.2    Das, P.K.3
  • 105
    • 0000531929 scopus 로고    scopus 로고
    • Phospholipase A2-catalyzed hydrolysis of lecithin in a continuous reversed-micellar membrane bioreactor
    • Morgado, M.A.P., Cabral, J.M., Prazeres, D.M.F. 1996. Phospholipase A2-catalyzed hydrolysis of lecithin in a continuous reversed-micellar membrane bioreactor. J. Am. Oil Chem. Soc. 73, 337–346.
    • (1996) J. Am. Oil Chem. Soc , vol.73 , pp. 337-346
    • Morgado, M.A.P.1    Cabral, J.M.2    Prazeres, D.M.F.3
  • 106
    • 0027909203 scopus 로고
    • An ultrafiltration membrane bioreactor for the lipolysis of olive oil in reversed micellar media
    • Prazeres, D.M., Garcia, F.A.P., Cabral, J.M.S. 1993. An ultrafiltration membrane bioreactor for the lipolysis of olive oil in reversed micellar media. Biotechnol. Bioeng. 41, 761–770.
    • (1993) Biotechnol. Bioeng , vol.41 , pp. 761-770
    • Prazeres, D.M.1    Garcia, F.A.P.2    Cabral, J.M.S.3
  • 107
    • 0027909876 scopus 로고
    • Modeling lipolysis in a reversed micellar system: Part II. Membrane reactor
    • Prazeres, D.M., Lemos, F., Garcia, F.A.P., Cabral, J.M.S. 1993. Modeling lipolysis in a reversed micellar system: Part II. Membrane reactor. Biotechnol. Bioeng. 42, 765–771.
    • (1993) Biotechnol. Bioeng , vol.42 , pp. 765-771
    • Prazeres, D.M.1    Lemos, F.2    Garcia, F.A.P.3    Cabral, J.M.S.4
  • 108
    • 0028484252 scopus 로고
    • Organic and bioorganic reactions in microemulsions
    • Holmberg, K. 1994. Organic and bioorganic reactions in microemulsions. Adv. Colloid Interf. Sci. 51, 137–174.
    • (1994) Adv. Colloid Interf. Sci , vol.51 , pp. 137-174
    • Holmberg, K.1
  • 109
    • 0000080018 scopus 로고
    • Lipase-catalyzed reactions in reverse micelles formed by soybean lecithin
    • Schmidli, P.K., Luisi, P.L. 1990. Lipase-catalyzed reactions in reverse micelles formed by soybean lecithin. Biocatalysis 3, 367–376.
    • (1990) Biocatalysis , vol.3 , pp. 367-376
    • Schmidli, P.K.1    Luisi, P.L.2
  • 110
    • 0026417573 scopus 로고
    • Continuous glycerolysis of olive oil by Chromobacterium viscosum lipase immobilized on liposome in reversed micelles
    • Chang, P.S., Rhee, J.S., Kim, J.-J. 1991. Continuous glycerolysis of olive oil by Chromobacterium viscosum lipase immobilized on liposome in reversed micelles. Biotechnol. Bioeng. 38, 1159–1165.
    • (1991) Biotechnol. Bioeng , vol.38 , pp. 1159-1165
    • Chang, P.S.1    Rhee, J.S.2    Kim, J.-J.3
  • 111
    • 0026203834 scopus 로고
    • 1-Monoglyceride production from lipase-catalyzed esterification of glycerol and fatty acid in reverse micelles
    • Hayes, D.G., Gulari, E. 1991. 1-Monoglyceride production from lipase-catalyzed esterification of glycerol and fatty acid in reverse micelles. Biotechnol. Bioeng. 38, 507–517.
    • (1991) Biotechnol. Bioeng , vol.38 , pp. 507-517
    • Hayes, D.G.1    Gulari, E.2
  • 112
    • 0027112421 scopus 로고
    • Formation of polyol-fatty acid esters by lipases in reverse micellar media
    • Hayes, D.G., Gulari, E. 1992. Formation of polyol-fatty acid esters by lipases in reverse micellar media. Biotechnol. Bioeng. 40, 110–118.
    • (1992) Biotechnol. Bioeng , vol.40 , pp. 110-118
    • Hayes, D.G.1    Gulari, E.2
  • 113
    • 0028928130 scopus 로고
    • Substrate-induced stability of the lipase from Candida cylindracea in reversed micelles
    • Ayyagari, M.S., John, V.T. 1995. Substrate-induced stability of the lipase from Candida cylindracea in reversed micelles. Biotechnol. Lett. 17, 177–182.
    • (1995) Biotechnol. Lett , vol.17 , pp. 177-182
    • Ayyagari, M.S.1    John, V.T.2
  • 114
    • 0002578367 scopus 로고
    • Enzymatic transesterification of a triglyceride in microemulsions
    • Holmberg, K., Osterberg, E. 1987. Enzymatic transesterification of a triglyceride in microemulsions. Progr. Colloid Polym. Sci. 74, 98–102.
    • (1987) Progr. Colloid Polym. Sci , vol.74 , pp. 98-102
    • Holmberg, K.1    Osterberg, E.2
  • 115
    • 0027201601 scopus 로고
    • Enantioselective synthesis of ibuprofen esters in AOT/isooctane microemulsions by Candida cylindracea lipase
    • Hedstrom, G., Backlund, M., Slotte, P.J. 1993. Enantioselective synthesis of ibuprofen esters in AOT/isooctane microemulsions by Candida cylindracea lipase. Biotechnol. Bioeng. 42, 618–624.
    • (1993) Biotechnol. Bioeng , vol.42 , pp. 618-624
    • Hedstrom, G.1    Backlund, M.2    Slotte, P.J.3
  • 116
    • 0023655595 scopus 로고
    • Interesterification and synthesis by Candida cylindracea lipase in microemulsions
    • Bello, M., Thomas, D., Legoy, M.D. 1987. Interesterification and synthesis by Candida cylindracea lipase in microemulsions. Biochim. Biophys. Res. Commun. 146, 361–367.
    • (1987) Biochim. Biophys. Res. Commun , vol.146 , pp. 361-367
    • Bello, M.1    Thomas, D.2    Legoy, M.D.3
  • 117
    • 29444457902 scopus 로고    scopus 로고
    • Enzymatic esterification of dlmenthol with propionic acid by lipase from Candida cylindracea
    • Lu, Z., Chu, C., Han, Y., Wang, Y., Liu, J. 2005. Enzymatic esterification of dlmenthol with propionic acid by lipase from Candida cylindracea. J. Chem. Technol. Biotechnol. 80, 1365–1370.
    • (2005) J. Chem. Technol. Biotechnol , vol.80 , pp. 1365-1370
    • Lu, Z.1    Chu, C.2    Han, Y.3    Wang, Y.4    Liu, J.5
  • 118
    • 0026942135 scopus 로고
    • Strategies for enzymatic esterification in organic solvents: Comparison of microaqueous, biphasic and micellar media
    • Bozreix, F., Monot, F., Vandecasteele, J.P. 1992. Strategies for enzymatic esterification in organic solvents: Comparison of microaqueous, biphasic and micellar media. Enzyme Microb. Technol. 14, 791–797.
    • (1992) Enzyme Microb. Technol , vol.14 , pp. 791-797
    • Bozreix, F.1    Monot, F.2    Vandecasteele, J.P.3
  • 119
    • 0029636990 scopus 로고
    • Comparison of hydrolysis and esterification behavior of Humicola lanuginosa and Rhizomucor miehei lipases in AOT-stabilized water-in-oil microemulsions: I. Effect of pH and water content on reaction kinetics
    • Crooks, G.E., Rees, G.D., Robinson, B.H., Svensson, M., Stephenson, G.R. 1995. Comparison of hydrolysis and esterification behavior of Humicola lanuginosa and Rhizomucor miehei lipases in AOT-stabilized water-in-oil microemulsions: I. Effect of pH and water content on reaction kinetics. Biotechnol. Bioeng. 48, 78–88.
    • (1995) Biotechnol. Bioeng , vol.48 , pp. 78-88
    • Crooks, G.E.1    Rees, G.D.2    Robinson, B.H.3    Svensson, M.4    Stephenson, G.R.5
  • 120
    • 0027471718 scopus 로고
    • Kinetic studies of Mucor miehei lipase in phosphatidylcholine microemulsions
    • Oliveira, A.C., Cabral, J.M.S. 1993. Kinetic studies of Mucor miehei lipase in phosphatidylcholine microemulsions. J. Chem. Technol. Biotechnol. 56, 247–252.
    • (1993) J. Chem. Technol. Biotechnol , vol.56 , pp. 247-252
    • Oliveira, A.C.1    Cabral, J.M.S.2
  • 121
    • 0000972942 scopus 로고    scopus 로고
    • Structural studies of lecithin- and AOT-based water-in-oil microemulsions, in the presence of lipase
    • Avramiotis, S., Stamatis, H., Kolisis, F.N., Lianos, P., Xenakis, A. 1996. Structural studies of lecithin- and AOT-based water-in-oil microemulsions, in the presence of lipase. Langmuir 12, 6320–6328.
    • (1996) Langmuir , vol.12 , pp. 6320-6328
    • Avramiotis, S.1    Stamatis, H.2    Kolisis, F.N.3    Lianos, P.4    Xenakis, A.5
  • 122
    • 0029992502 scopus 로고    scopus 로고
    • Esterification of hydrophilic diols catalysed by lipases in microemulsions
    • Stamatis, H., Macris, J., Kolisis, F.N. 1996. Esterification of hydrophilic diols catalysed by lipases in microemulsions. Biotechnol. Lett. 18, 541–546.
    • (1996) Biotechnol. Lett , vol.18 , pp. 541-546
    • Stamatis, H.1    Macris, J.2    Kolisis, F.N.3
  • 123
    • 20144380175 scopus 로고    scopus 로고
    • A comparative study of the synthesis of n-butyl-oleate using a crude lipolytic extract of Penicillum coryophilum in water-restricted environments
    • Baron, A., Sarquis, M.I.M., Baigori, M., Mitchell, D.A., Krieger, N. 2005. A comparative study of the synthesis of n-butyl-oleate using a crude lipolytic extract of Penicillum coryophilum in water-restricted environments. J. Mol. Catal. B: Enzym. 34, 25–32.
    • (2005) J. Mol. Catal. B: Enzym , vol.34 , pp. 25-32
    • Baron, A.1    Sarquis, M.I.M.2    Baigori, M.3    Mitchell, D.A.4    Krieger, N.5
  • 124
    • 0000402125 scopus 로고
    • Enzymatic esterification and phase behavior in ionic microemulsions with different alcohols
    • Backlund, S., Eriksson, F., Karlsson, S., Lundsten, G. 1995. Enzymatic esterification and phase behavior in ionic microemulsions with different alcohols. Coloid Polym. Sci. 273, 533–538.
    • (1995) Coloid Polym. Sci , vol.273 , pp. 533-538
    • Backlund, S.1    Eriksson, F.2    Karlsson, S.3    Lundsten, G.4
  • 125
    • 0028446441 scopus 로고
    • Synthesis of mono- and diglycerides in water-in-oil microemulsions
    • Singh, C.P., Shah, D.O., Holmberg, K. 1994. Synthesis of mono- and diglycerides in water-in-oil microemulsions. J. Am. Oil Chem. Soc. 71, 583–587.
    • (1994) J. Am. Oil Chem. Soc , vol.71 , pp. 583-587
    • Singh, C.P.1    Shah, D.O.2    Holmberg, K.3
  • 126
    • 0028729418 scopus 로고
    • A comparison between lipase-catalyzed esterification of oleic acid with glycerol in monolayer and microemulsion systems
    • Singh, C.P., Skagerlind, P., Holmberg, K., Shah, D.O. 1994. A comparison between lipase-catalyzed esterification of oleic acid with glycerol in monolayer and microemulsion systems. J. Am. Oil Chem. Soc. 71, 1405–1409.
    • (1994) J. Am. Oil Chem. Soc , vol.71 , pp. 1405-1409
    • Singh, C.P.1    Skagerlind, P.2    Holmberg, K.3    Shah, D.O.4
  • 127
    • 0029101690 scopus 로고
    • Studies on enzyme reuse and product recovery in lipase-catalyzed reactions in microemulsions
    • Stamatis, H., Xenakis, A., Kolisis, F.N. 1995. Studies on enzyme reuse and product recovery in lipase-catalyzed reactions in microemulsions. Ann. NY Acad. Sci. 750, 237–241.
    • (1995) Ann. NY Acad. Sci , vol.750 , pp. 237-241
    • Stamatis, H.1    Xenakis, A.2    Kolisis, F.N.3
  • 128
    • 0028041147 scopus 로고
    • A comparison of different strategies for lipase-catalyzed synthesis of partial glycerides
    • Bornscheuer, U., Stamatis, H., Xenakis, A., Yamane, T., Kolisis, F.N. 1994. A comparison of different strategies for lipase-catalyzed synthesis of partial glycerides. Biotechnol. Lett. 16, 697–702.
    • (1994) Biotechnol. Lett , vol.16 , pp. 697-702
    • Bornscheuer, U.1    Stamatis, H.2    Xenakis, A.3    Yamane, T.4    Kolisis, F.N.5
  • 129
    • 0343539351 scopus 로고
    • Lipase catalyzed processes and reactions in microemulsions
    • Holmberg, K. 1989. Lipase catalyzed processes and reactions in microemulsions. J. Surface Sci. Technol. 5, 209–222.
    • (1989) J. Surface Sci. Technol , vol.5 , pp. 209-222
    • Holmberg, K.1
  • 130
    • 0033515889 scopus 로고    scopus 로고
    • Biocatalysis using microemulsion-based polymer gels containing lipase
    • Stamatis, H., Xenakis, A. 1999. Biocatalysis using microemulsion-based polymer gels containing lipase. J. Mol. Catal. B: Enzym. 6, 399–406.
    • (1999) J. Mol. Catal. B: Enzym , vol.6 , pp. 399-406
    • Stamatis, H.1    Xenakis, A.2
  • 131
    • 0030469879 scopus 로고    scopus 로고
    • Microemulsions as a tool for the regioselective lipase-catalysed esterification of aliphatic diols
    • Macris, J.B., Stamatis, H., Kolisis, F.N. 1996. Microemulsions as a tool for the regioselective lipase-catalysed esterification of aliphatic diols. Appl. Microbiol. Biotechnol. 46, 521–523.
    • (1996) Appl. Microbiol. Biotechnol , vol.46 , pp. 521-523
    • Macris, J.B.1    Stamatis, H.2    Kolisis, F.N.3
  • 133
    • 0032472291 scopus 로고    scopus 로고
    • Kinetic characterization of esterification catalyzed by Rhizopus delemar lipase in lecithin–AOT microemulsion systems
    • Nagayama, K., Matsura, S., Doi, T., Imai, M. 1998. Kinetic characterization of esterification catalyzed by Rhizopus delemar lipase in lecithin–AOT microemulsion systems. J. Mol. Catal. B: Enzym. 4, 25–32.
    • (1998) J. Mol. Catal. B: Enzym , vol.4 , pp. 25-32
    • Nagayama, K.1    Matsura, S.2    Doi, T.3    Imai, M.4
  • 134
    • 0001120334 scopus 로고
    • Catalysis of water soluble enzymes in organic solvents. Stabilization of enzyme against denaturation (inactivation) when they are included in inversed micelles of surface active substance
    • Martinek, K., Levashov, A.V., Klyachko, N.L., Berezin, I.V. 1977. Catalysis of water soluble enzymes in organic solvents. Stabilization of enzyme against denaturation (inactivation) when they are included in inversed micelles of surface active substance. Dokl. Akad. Nauk. SSSR 236, 920.
    • (1977) Dokl. Akad. Nauk. SSSR , vol.236 , pp. 920
    • Martinek, K.1    Levashov, A.V.2    Klyachko, N.L.3    Berezin, I.V.4
  • 135
    • 20744460064 scopus 로고    scopus 로고
    • Horseradish peroxidase activity in a reverse catanionic microemulsion
    • Mahiuddin, S., Renoncourt, A., Bauduin, P., Touraud, D., Kunz, W. 2005. Horseradish peroxidase activity in a reverse catanionic microemulsion. Langmuir 21, 5259–5262.
    • (2005) Langmuir , vol.21 , pp. 5259-5262
    • Mahiuddin, S.1    Renoncourt, A.2    Bauduin, P.3    Touraud, D.4    Kunz, W.5
  • 136
    • 0024699169 scopus 로고
    • Characteristics of tyrosinase in AOT–isooctane reverse micelles
    • Bru, R., Sanchez-Ferrer, A., Garcia-Carmona. 1989. Characteristics of tyrosinase in AOT–isooctane reverse micelles. Biotechnol. Bioeng. 34, 304–308.
    • (1989) Biotechnol. Bioeng , vol.34 , pp. 304-308
    • Bru, R.1    Sanchez-Ferrer, A.2
  • 137
    • 4243778550 scopus 로고    scopus 로고
    • Phenols oxidizing enzymes in water-restricted media
    • Rodakiewicz-Novak, J. 2000. Phenols oxidizing enzymes in water-restricted media. Top. Catal. 11/12, 419–434.
    • (2000) Top. Catal , vol.11 , Issue.12 , pp. 419-434
    • Rodakiewicz-Novak, J.1
  • 138
    • 0030714961 scopus 로고    scopus 로고
    • Formation and properties of dimeric recombinant horseradish peroxidase in a system of reversed micelles
    • Gazaryan, I.G., Klyachko, N.L., Dulkis, Y.K., Ouporov, I.V., Levashov, A.V. 1997. Formation and properties of dimeric recombinant horseradish peroxidase in a system of reversed micelles. Biochem. J. 328, 643–647.
    • (1997) Biochem. J , vol.328 , pp. 643-647
    • Gazaryan, I.G.1    Klyachko, N.L.2    Dulkis, Y.K.3    Ouporov, I.V.4    Levashov, A.V.5
  • 139
    • 0035182283 scopus 로고    scopus 로고
    • Polyphenol oxidase in reverse micelles of AOT/cyclohexane: A thermostability study
    • Rojo, M., Gomez, M., Estrada, P. 2001. Polyphenol oxidase in reverse micelles of AOT/cyclohexane: A thermostability study. J. Chem. Technol. Biotechnol. 76, 69–77.
    • (2001) J. Chem. Technol. Biotechnol , vol.76 , pp. 69-77
    • Rojo, M.1    Gomez, M.2    Estrada, P.3
  • 140
    • 28244476493 scopus 로고    scopus 로고
    • Water-in-oil microemulsions as the reaction medium for the solvent sensitive yellow laccases
    • Rodakiewicz-Novak, J., Pozdnyakova, N.N., Turkovskaya, O.V. 2005. Water-in-oil microemulsions as the reaction medium for the solvent sensitive yellow laccases. Biocat. Biotransform. 2005 23, 271–279.
    • (2005) Biocat. Biotransform , vol.2005 , Issue.23 , pp. 271-279
    • Rodakiewicz-Novak, J.1    Pozdnyakova, N.N.2    Turkovskaya, O.V.3
  • 141
    • 28244437281 scopus 로고    scopus 로고
    • Influence of Ipegal reverse micellar and micellar systems on activity and stability of heme peroxidases
    • Jurgas-Grudzinska, M., Gebicka, L. 2005. Influence of Ipegal reverse micellar and micellar systems on activity and stability of heme peroxidases. Biocat. Biotransform. 23, 293–298.
    • (2005) Biocat. Biotransform , vol.23 , pp. 293-298
    • Jurgas-Grudzinska, M.1    Gebicka, L.2
  • 142
    • 33947133257 scopus 로고    scopus 로고
    • Olive oil microemulsions: Enzymatic activities and structural characteristics
    • Papadimitriou, V., Sotiroudis, T.G., Xenakis, A. 2007. Olive oil microemulsions: Enzymatic activities and structural characteristics. Langmuir 23, 2071–2077.
    • (2007) Langmuir , vol.23 , pp. 2071-2077
    • Papadimitriou, V.1    Sotiroudis, T.G.2    Xenakis, A.3
  • 143
    • 0000163161 scopus 로고
    • Cryoenzymology in aqueous media: Micellar solubilized water clusters
    • Douzou, P., Keh, E., Balny, C. 1979. Cryoenzymology in aqueous media: Micellar solubilized water clusters. Proc. Natl. Acad. Sci. USA 76, 681–684.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 681-684
    • Douzou, P.1    Keh, E.2    Balny, C.3
  • 144
    • 0000368032 scopus 로고
    • Reduction of reversed micelle entrapped cytochrome c and cytochrome c3 by electrons generated by pulse radiolysis or by pyrene photoionization
    • Visser, A.J.W.G., Fendler, J.H. 1982. Reduction of reversed micelle entrapped cytochrome c and cytochrome c3 by electrons generated by pulse radiolysis or by pyrene photoionization. J. Phys. Chem. 86, 947–950.
    • (1982) J. Phys. Chem , vol.86 , pp. 947-950
    • Visser, A.J.W.G.1    Fendler, J.H.2
  • 145
    • 0000064497 scopus 로고
    • Photosensitized production of hydrogen by hydrogenase in reversed micelles
    • Hilhorst, R., Laane, C., Veeger, C. 1982. Photosensitized production of hydrogen by hydrogenase in reversed micelles. Proc. Natl. Acad. Sci. USA 79, 3927–3930.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3927-3930
    • Hilhorst, R.1    Laane, C.2    Veeger, C.3
  • 146
    • 0000647672 scopus 로고
    • Enzymatic conversion of apolar compounds in organic media using an NADH-regenerating system and dihydrogen as reductant
    • Hilhorst, R., Laane, C., Veeger, C. 1983. Enzymatic conversion of apolar compounds in organic media using an NADH-regenerating system and dihydrogen as reductant. FEBS Lett. 159, 225–228.
    • (1983) FEBS Lett , vol.159 , pp. 225-228
    • Hilhorst, R.1    Laane, C.2    Veeger, C.3
  • 147
    • 0023378105 scopus 로고
    • Activity and stability of horse liver alcohol dehydrogenase in sodium dioctylsulfosuccinate/cyclohexane reverse micelles
    • Larsson, K.M., Adlercreutz, P., Mattiasson, B. 1987. Activity and stability of horse liver alcohol dehydrogenase in sodium dioctylsulfosuccinate/cyclohexane reverse micelles. Eur. J. Biochem. 166, 157–161.
    • (1987) Eur. J. Biochem , vol.166 , pp. 157-161
    • Larsson, K.M.1    Adlercreutz, P.2    Mattiasson, B.3
  • 148
    • 0028764790 scopus 로고
    • Two-step biocatalytic conversion of an ester to an aldehyde in reverse micelles
    • Yang, F., Russell, A.J. 1994. Two-step biocatalytic conversion of an ester to an aldehyde in reverse micelles. Biotech. Bioeng. 43, 232–241.
    • (1994) Biotech. Bioeng , vol.43 , pp. 232-241
    • Yang, F.1    Russell, A.J.2
  • 149
    • 0029135581 scopus 로고
    • Xanthine oxidase reactivity in reversed micellar systems: A contribution to the prediction of enzymatic activity in organized media
    • Bommarius, A.S., Hatton, T.A., Wang, D.I.C. 1995. Xanthine oxidase reactivity in reversed micellar systems: A contribution to the prediction of enzymatic activity in organized media. J. Am. Chem. Soc. 117, 4515–4523.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 4515-4523
    • Bommarius, A.S.1    Hatton, T.A.2    Wang, D.I.C.3
  • 150
    • 0033527817 scopus 로고    scopus 로고
    • Enzymatic reduction of a less water soluble ketone in reverse micelles with NADH regeneration
    • Orlich, B., Schomaecker, R. 1999. Enzymatic reduction of a less water soluble ketone in reverse micelles with NADH regeneration. Biotech. Bioeng. 65, 357–362.
    • (1999) Biotech. Bioeng , vol.65 , pp. 357-362
    • Orlich, B.1    Schomaecker, R.2
  • 151
    • 0034694931 scopus 로고    scopus 로고
    • Stability and activity of alcohol dehydrogenases in w/o-microemulsions: Enantioselective reduction including cofactor regeneration
    • Orlich, B., Berger, H., Lade, M., Schomacker, R. 2000. Stability and activity of alcohol dehydrogenases in w/o-microemulsions: Enantioselective reduction including cofactor regeneration. Biotech. Bioeng. 70, 638–646.
    • (2000) Biotech. Bioeng , vol.70 , pp. 638-646
    • Orlich, B.1    Berger, H.2    Lade, M.3    Schomacker, R.4
  • 152
    • 0034667529 scopus 로고    scopus 로고
    • Activity and conformation of yeast alcohol dehydrogenase (YADH) entrapped in reverse micelles
    • Das, S., Mozumdar, S., Maitra, A.J. 2000. Activity and conformation of yeast alcohol dehydrogenase (YADH) entrapped in reverse micelles. Colloid Interf. Sci. 230, 328–333.
    • (2000) Colloid Interf. Sci , vol.230 , pp. 328-333
    • Das, S.1    Mozumdar, S.2    Maitra, A.J.3
  • 154
    • 0037009173 scopus 로고    scopus 로고
    • Hydrogen evolution and consumption in AOT–isooctane reverse micelles by Desulfovibrio gigas hydrogenase
    • Andrade, S., Moura, J.J.G. 2002. Hydrogen evolution and consumption in AOT–isooctane reverse micelles by Desulfovibrio gigas hydrogenase. Enzyme Microb. Technol. 31, 398–402.
    • (2002) Enzyme Microb. Technol , vol.31 , pp. 398-402
    • Andrade, S.1    Moura, J.J.G.2
  • 155
    • 0024174511 scopus 로고
    • Characteristic properties of lecithin as a surfactant
    • Shinoda, K., Kaneko, T.J. 1988. Characteristic properties of lecithin as a surfactant. J. Dispers. Sci. Technol. 9, 555–559.
    • (1988) J. Dispers. Sci. Technol , vol.9 , pp. 555-559
    • Shinoda, K.1    Kaneko, T.J.2
  • 156
    • 0001682070 scopus 로고
    • Lecitihnbased microemulsions: Phase behavior and microstructure
    • Shinoda, K., Araki, M., Sadaghiani, A., Khan, A., Lindman, B. 1991. Lecitihnbased microemulsions: Phase behavior and microstructure. J. Phys. Chem. 95, 989–993.
    • (1991) J. Phys. Chem , vol.95 , pp. 989-993
    • Shinoda, K.1    Araki, M.2    Sadaghiani, A.3    Khan, A.4    Lindman, B.5
  • 157
    • 0001000390 scopus 로고
    • Preparing microemulsions with lecithins
    • Kahlweit, M., Busse, G., Faulhaber, B. 1995. Preparing microemulsions with lecithins. Langmuir 11, 1576–1583.
    • (1995) Langmuir , vol.11 , pp. 1576-1583
    • Kahlweit, M.1    Busse, G.2    Faulhaber, B.3
  • 159
    • 0031572755 scopus 로고    scopus 로고
    • Structural and dynamic properties of lecithin–alcohol based (W/o) microemulsions. A luminescence quenching study
    • Avramiotis, S., Bekiari, V., Lianos, P., Xenakis, A. 1997. Structural and dynamic properties of lecithin–alcohol based (w/o) microemulsions. A luminescence quenching study. J. Colloid Interface Sci. 194, 326–331.
    • (1997) J. Colloid Interface Sci , vol.194 , pp. 326-331
    • Avramiotis, S.1    Bekiari, V.2    Lianos, P.3    Xenakis, A.4
  • 160
    • 33845281004 scopus 로고
    • Micromechanics of surfactant microstructures
    • Wormuth, K.R., Kaler, E.W. 1987. Micromechanics of surfactant microstructures. J. Phys. Chem., 1987 91, 611–617.
    • (1987) J. Phys. Chem , vol.1987 , Issue.91 , pp. 611-617
    • Wormuth, K.R.1    Kaler, E.W.2
  • 161
    • 0028145622 scopus 로고
    • Investigations into the formation and characterization of phospholipid microemulsions. III. Pseudo-ternary phase diagrams of systems containing water-lecithin-isopropyl myristate and either an alkanoic acid, amine, alkanediol, polyethylene glycol alkyl ether or alcohol as cosurfactant
    • Aboofazeli, R., Lawrence, C.B., Wicks, S.R., Lawrence, M. 1994. Investigations into the formation and characterization of phospholipid microemulsions. III. Pseudo-ternary phase diagrams of systems containing water-lecithin-isopropyl myristate and either an alkanoic acid, amine, alkanediol, polyethylene glycol alkyl ether or alcohol as cosurfactant. Int. J. Pharm. 111, 63–72.
    • (1994) Int. J. Pharm , vol.111 , pp. 63-72
    • Aboofazeli, R.1    Lawrence, C.B.2    Wicks, S.R.3    Lawrence, M.4
  • 162
    • 0000501005 scopus 로고
    • Principles of attaining very large solubilization (Microemulsion): Inclusive understanding of the solubilization of oil and water in aqueous and hydrocarbon media
    • Shinoda, K., Kunieda, H., Arai, T., Saijo, H. 1984. Principles of attaining very large solubilization (microemulsion): Inclusive understanding of the solubilization of oil and water in aqueous and hydrocarbon media. J. Phys. Chem. 88, 5126–5129.
    • (1984) J. Phys. Chem , vol.88 , pp. 5126-5129
    • Shinoda, K.1    Kunieda, H.2    Arai, T.3    Saijo, H.4
  • 163
    • 33750429923 scopus 로고    scopus 로고
    • Exploring the potential of N-methyl pyrrolidone as a cosurfactant in the microemulsion systems
    • Bachhav, Y.G., Date, A.A., Patravale, V.B. 2006. Exploring the potential of N-methyl pyrrolidone as a cosurfactant in the microemulsion systems. Int. J. Pharm. 326, 186–189.
    • (2006) Int. J. Pharm , vol.326 , pp. 186-189
    • Bachhav, Y.G.1    Date, A.A.2    Patravale, V.B.3
  • 164
    • 0027112228 scopus 로고
    • Protein extraction and activity in reverse micelles of a nonionic detergent
    • Ayala, G.A., Kamat, S., Beckman, E.J., Russel, A.G. 1992. Protein extraction and activity in reverse micelles of a nonionic detergent. Biotech. Bioeng. 39, 806–814.
    • (1992) Biotech. Bioeng , vol.39 , pp. 806-814
    • Ayala, G.A.1    Kamat, S.2    Beckman, E.J.3    Russel, A.G.4
  • 165
    • 0030834788 scopus 로고    scopus 로고
    • Formulation and physical characterization of water-in-oil microemulsions containing long versus medium chain glycerides
    • Constantinides, P.P., Scalart, J.P. 1997. Formulation and physical characterization of water-in-oil microemulsions containing long versus medium chain glycerides. Int. J. Pharm. 158, 57–68.
    • (1997) Int. J. Pharm , vol.158 , pp. 57-68
    • Constantinides, P.P.1    Scalart, J.P.2
  • 167
    • 0033799723 scopus 로고    scopus 로고
    • Some characteristics of sugar ester non-ionic microemulsions in view of possible food applications
    • Garti, N., Clement, V., Fanun, M., Leser, M.E. 2000. Some characteristics of sugar ester non-ionic microemulsions in view of possible food applications. J. Agric. Food Chem. 48, 3945–3956.
    • (2000) J. Agric. Food Chem , vol.48 , pp. 3945-3956
    • Garti, N.1    Clement, V.2    Fanun, M.3    Leser, M.E.4
  • 168
    • 36549080170 scopus 로고    scopus 로고
    • The self-organization properties of n-dodecylammonium α-glutamate/n-C5H11OH/water system
    • Wang, Y., Guo, R., Guo, X. 2007. The self-organization properties of n-dodecylammonium α-glutamate/n-C5H11OH/water system. Colloid Polym. Sci. 285, 1423–1431.
    • (2007) Colloid Polym. Sci , vol.285 , pp. 1423-1431
    • Wang, Y.1    Guo, R.2    Guo, X.3
  • 169
    • 0033849510 scopus 로고    scopus 로고
    • Preparation of biodegradable insulin nanocapsules from biocompatible microemulsions
    • Watnasirichaikul, S., Davies, N.M., Rades, T., Tucker, I.G. 2000. Preparation of biodegradable insulin nanocapsules from biocompatible microemulsions. Pharmac. Res. 17, 684–689.
    • (2000) Pharmac. Res , vol.17 , pp. 684-689
    • Watnasirichaikul, S.1    Davies, N.M.2    Rades, T.3    Tucker, I.G.4
  • 170
    • 3042540700 scopus 로고    scopus 로고
    • Biocompatible lipidic formulations: Phase behavior and microstructure
    • Mele, S., Murgia, S., Caboi, F., Monduzzi, M. 2004. Biocompatible lipidic formulations: Phase behavior and microstructure. Langmuir 20, 5241–5246.
    • (2004) Langmuir , vol.20 , pp. 5241-5246
    • Mele, S.1    Murgia, S.2    Caboi, F.3    Monduzzi, M.4
  • 174
    • 0002012179 scopus 로고
    • Three-component non-ionic oil-in-water microemulsions using polyethylene ether surfactants
    • Malcolmson, C., Lawrence, M.J. 1995. Three-component non-ionic oil-in-water microemulsions using polyethylene ether surfactants. Colloids Surf. B: Biointerfaces 4, 97–109.
    • (1995) Colloids Surf. B: Biointerfaces , vol.4 , pp. 97-109
    • Malcolmson, C.1    Lawrence, M.J.2
  • 175
    • 0034732053 scopus 로고    scopus 로고
    • Nonionic oil-in-water microemulsions: The effect of oil type on phase behaviour
    • Warisnoicharoen, W., Lansley, A.B., Lawrence, M.J. 2000. Nonionic oil-in-water microemulsions: The effect of oil type on phase behaviour. Int. J. Pharm. 198, 7–27.
    • (2000) Int. J. Pharm , vol.198 , pp. 7-27
    • Warisnoicharoen, W.1    Lansley, A.B.2    Lawrence, M.J.3
  • 176
    • 2142820722 scopus 로고    scopus 로고
    • Structural characterization of water–Tween 40/Imwitor 308–isopropyl myristate microemulsions using different experimental methods
    • Podlogar, F., Gasperlin, M., Tomsic, M., Jamnik, A., Rogac, M.B. 2004. Structural characterization of water–Tween 40/Imwitor 308–isopropyl myristate microemulsions using different experimental methods. Int. J. Pharm. 276, 115–128.
    • (2004) Int. J. Pharm , vol.276 , pp. 115-128
    • Podlogar, F.1    Gasperlin, M.2    Tomsic, M.3    Jamnik, A.4    Rogac, M.B.5
  • 177
    • 12844249391 scopus 로고    scopus 로고
    • Formation and investigation of microemulsiuons based on jojoba oil and nonionic surfactants
    • Shevachman, M., Shani, A., Garti, N. 2004. Formation and investigation of microemulsiuons based on jojoba oil and nonionic surfactants. J. Am. Oil Chem. Soc. 81, 1143–1152.
    • (2004) J. Am. Oil Chem. Soc , vol.81 , pp. 1143-1152
    • Shevachman, M.1    Shani, A.2    Garti, N.3
  • 178
    • 30344488412 scopus 로고    scopus 로고
    • Olive oil microemulsions as a biomimetic medium for enzymatic studies. Oxidation of oleuropein
    • Papadimitriou, V., Sotiroudis, T.G., Xenakis, A. 2005. Olive oil microemulsions as a biomimetic medium for enzymatic studies. Oxidation of oleuropein. J. Am. Oil Chem. Soc. 82, 1–6.
    • (2005) J. Am. Oil Chem. Soc , vol.82 , pp. 1-6
    • Papadimitriou, V.1    Sotiroudis, T.G.2    Xenakis, A.3
  • 179
    • 0037032189 scopus 로고    scopus 로고
    • Food-grade microemulsions based on nonionic emulsifiers: Media to enhance lycopene solubilization
    • Spernath, A., Yaghmur, A., Aserin, A., Hoffman, R.E., Garti, N. 2002. Food-grade microemulsions based on nonionic emulsifiers: Media to enhance lycopene solubilization. J. Agric. Food Chem. 50, 6917–6922.
    • (2002) J. Agric. Food Chem , vol.50 , pp. 6917-6922
    • Spernath, A.1    Yaghmur, A.2    Aserin, A.3    Hoffman, R.E.4    Garti, N.5
  • 180
    • 0037427224 scopus 로고    scopus 로고
    • Self-diffusion nuclear magnetic resonance microstructure transitions a solubilization capacity of phytosterols and cholesterol in Winsor IV food-grade microemulsions
    • Spernath, A., Yaghmur, A., Aserin, A., Hoffman, R.E., Garti, N. 2003. Self-diffusion nuclear magnetic resonance microstructure transitions a solubilization capacity of phytosterols and cholesterol in Winsor IV food-grade microemulsions. J. Agric. Food Chem. 51, 2359–2364.
    • (2003) J. Agric. Food Chem , vol.51 , pp. 2359-2364
    • Spernath, A.1    Yaghmur, A.2    Aserin, A.3    Hoffman, R.E.4    Garti, N.5
  • 182
    • 0026471803 scopus 로고
    • Enzyme-catalyzed esterifi- cations in microemulsion-based organo gels
    • Nascimento, M.G., Rezende, M.C., Vecchia, R.D. 1992. Enzyme-catalyzed esterifi- cations in microemulsion-based organo gels. Tetrahedron Let. 33, 5891–5894.
    • (1992) Tetrahedron Let , vol.33 , pp. 5891-5894
    • Nascimento, M.G.1    Rezende, M.C.2    Vecchia, R.D.3
  • 184
    • 0028823532 scopus 로고
    • Preparative-scale kinetic resolutions catalysed by microbial lipases immobilised in AOT-stabilised microemulsion- based organo-gels: Cryoenzymology as a tool for improving enantioselectivity
    • Rees, G.D., Robinson, B.H., Stephenson, G.R. 1995. Preparative-scale kinetic resolutions catalysed by microbial lipases immobilised in AOT-stabilised microemulsion- based organo-gels: Cryoenzymology as a tool for improving enantioselectivity. Biochim. Biophys. Acta 1259, 73–81.
    • (1995) Biochim. Biophys. Acta , pp. 73-81
    • Rees, G.D.1    Robinson, B.H.2    Stephenson, G.R.3
  • 185
    • 0022480030 scopus 로고
    • Solubilization of enzymes in apolar solvents via reverse micelles
    • Luisi, P.L., Laane, C. 1986. Solubilization of enzymes in apolar solvents via reverse micelles. Trends Biotechnol. 4, 153–161.
    • (1986) Trends Biotechnol , vol.4 , pp. 153-161
    • Luisi, P.L.1    Laane, C.2
  • 186
    • 0032944832 scopus 로고    scopus 로고
    • Continuous production and simultaneous precipitation of a dipeptide in a reversed micellar membrane reactor
    • Serralheiro, M.L.M., Prazeres, D.M.F., Cabral, J.M.S. 1999. Continuous production and simultaneous precipitation of a dipeptide in a reversed micellar membrane reactor. Enzyme Microb. Technol. 24, 507–513.
    • (1999) Enzyme Microb. Technol , vol.24 , pp. 507-513
    • Serralheiro, M.L.M.1    Prazeres, D.M.F.2    Cabral, J.M.S.3
  • 187
    • 0029955809 scopus 로고    scopus 로고
    • Electroultrafiltration bioreactor for enzymatic reaction in reversed micelles
    • Hakoda, M., Enomoto, A., Hoshino, T., Shiragami, N. 1996. Electroultrafiltration bioreactor for enzymatic reaction in reversed micelles. J. Ferment. Bioeng. 82, 361–365.
    • (1996) J. Ferment. Bioeng , vol.82 , pp. 361-365
    • Hakoda, M.1    Enomoto, A.2    Hoshino, T.3    Shiragami, N.4
  • 188
    • 0025439801 scopus 로고
    • Enzymatic catalysis in microemulsions: Enzyme reuse and product recovery
    • Larsson, K.M., Adlercreutz, P., Mattiasson, B. 1990. Enzymatic catalysis in microemulsions: Enzyme reuse and product recovery. Biotechnol. Bioeng. 36, 135–141.
    • (1990) Biotechnol. Bioeng , vol.36 , pp. 135-141
    • Larsson, K.M.1    Adlercreutz, P.2    Mattiasson, B.3
  • 189
    • 33845373617 scopus 로고
    • Hydrocarbon gels from water-in-oil microemulsions
    • Haering, G., Luisi, P.L. 1986. Hydrocarbon gels from water-in-oil microemulsions. J. Phys. Chem. 90, 5892–5895.
    • (1986) J. Phys. Chem , vol.90 , pp. 5892-5895
    • Haering, G.1    Luisi, P.L.2
  • 190
    • 0001183109 scopus 로고
    • Mutual gelation of gelatin and water-in-oil microemulsions
    • Quellet, C., Eicke, H.-F. 1986. Mutual gelation of gelatin and water-in-oil microemulsions. Chimia 40, 233–238.
    • (1986) Chimia , vol.40 , pp. 233-238
    • Quellet, C.1    Eicke, H.-F.2
  • 193
    • 0031033717 scopus 로고    scopus 로고
    • Biocatalysis using gelatine microemulsion-based organogels containing immobilized Chromobacterium viscosum lipase
    • Jenta, T.R.-J., Batts, G., Rees, G.D., Robinson, B.H. 1997. Biocatalysis using gelatine microemulsion-based organogels containing immobilized Chromobacterium viscosum lipase. Biotech. Bioeng. 53, 121–131.
    • (1997) Biotech. Bioeng , vol.53 , pp. 121-131
    • Jenta, T.R.1    Batts, G.2    Rees, G.D.3    Robinson, B.H.4
  • 194
    • 28944453689 scopus 로고    scopus 로고
    • The novel hexadecyltrimethylammonium bromide (CTAB) based organogel as reactor for ester synthesis by entrapped Candida rugosa lipase
    • Lopez, F., Venditti, F., Giuseppe Cinelli, G., Ceglie, A. 2006. The novel hexadecyltrimethylammonium bromide (CTAB) based organogel as reactor for ester synthesis by entrapped Candida rugosa lipase. Proc. Biochem. 41, 114–119.
    • (2006) Proc. Biochem , vol.41 , pp. 114-119
    • Lopez, F.1    Venditti, F.2    Giuseppe Cinelli, G.3    Ceglie, A.4
  • 195
    • 0033021381 scopus 로고    scopus 로고
    • An unusual reversible sol–gel transition phenomenon in organogels and its application for enzyme immobilization in gelatin membranes
    • Fadnavis, N.W., Koteshwar, K. 1999. An unusual reversible sol–gel transition phenomenon in organogels and its application for enzyme immobilization in gelatin membranes. Biotechnol. Prog. 15, 98–104.
    • (1999) Biotechnol. Prog , vol.15 , pp. 98-104
    • Fadnavis, N.W.1    Koteshwar, K.2
  • 196
    • 0035819411 scopus 로고    scopus 로고
    • Enzyme immobilization in silica-hardened organogels
    • Schuleit, M., Luisi, P.L. 2001. Enzyme immobilization in silica-hardened organogels. Biotechnol. Bioeng. 72, 249–253.
    • (2001) Biotechnol. Bioeng , vol.72 , pp. 249-253
    • Schuleit, M.1    Luisi, P.L.2
  • 197
    • 0034435069 scopus 로고    scopus 로고
    • Microemulsion-based organogels containing lipase: Application in the synthesis of esters
    • Pastou, A., Stamatis, H., Xenakis, A. 2000. Microemulsion-based organogels containing lipase: Application in the synthesis of esters. Prog. Colloid Polym. Sci. 115, 192–195.
    • (2000) Prog. Colloid Polym. Sci , vol.115 , pp. 192-195
    • Pastou, A.1    Stamatis, H.2    Xenakis, A.3
  • 198
    • 0036788038 scopus 로고    scopus 로고
    • Activity and stability studies of mucor miehei lipase immobilized in novel microemulsion-based organogels
    • Delimitsou, C., Zoumpanioti, M., Xenakis, A., Stamatis, H. 2002. Activity and stability studies of mucor miehei lipase immobilized in novel microemulsion-based organogels. Biocatal. Biotransf. 20, 319–327.
    • (2002) Biocatal. Biotransf , vol.20 , pp. 319-327
    • Delimitsou, C.1    Zoumpanioti, M.2    Xenakis, A.3    Stamatis, H.4


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