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Volumn 31, Issue 5, 2002, Pages 648-655

Chain-length selectivity of various lipases during hydrolysis, esterification and alcoholysis in biphasic aqueous medium

Author keywords

Bioconversion; Biphasic aqueous medium; Lipase; Multicompetitive enzymatic reaction; Substrate specificity; Transesterification

Indexed keywords

ESTERIFICATION; ESTERS; FATTY ACIDS; HYDROLYSIS; SYNTHESIS (CHEMICAL);

EID: 0037015410     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(02)00166-7     Document Type: Article
Times cited : (84)

References (38)
  • 1
    • 0031051033 scopus 로고    scopus 로고
    • Predicting the behaviour of lipases in low-water media
    • Halling P.J. Predicting the behaviour of lipases in low-water media. Biochem. Soc. Trans. 25:1997;170-174.
    • (1997) Biochem. Soc. Trans. , vol.25 , pp. 170-174
    • Halling, P.J.1
  • 2
    • 0024653016 scopus 로고
    • Enzymatic catalysis in anhydrous organic solvents
    • Klibanov A.M. Enzymatic catalysis in anhydrous organic solvents. Trends Biochem. Sci. 14:1989;141-144.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 141-144
    • Klibanov, A.M.1
  • 3
    • 0026942135 scopus 로고
    • Strategies for enzymatic esterification in organic solvents - Comparison of microaqueous, biphasic, and micellar systems
    • Borzeix F., Monot F., Vandecasteele J.P. Strategies for enzymatic esterification in organic solvents - comparison of microaqueous, biphasic, and micellar systems. Enzyme Microb. Technol. 14:1992;791-797.
    • (1992) Enzyme Microb. Technol. , vol.14 , pp. 791-797
    • Borzeix, F.1    Monot, F.2    Vandecasteele, J.P.3
  • 5
    • 0029073556 scopus 로고
    • Factors influencing ester synthesis catalysed in aqueous media by the lipase from Candida deformans (Zach) Langeron and Guerra
    • Boutur O., Dubreucq E., Galzy P. Factors influencing ester synthesis catalysed in aqueous media by the lipase from Candida deformans (Zach) Langeron and Guerra. J. Biotechnol. 42:1995;23-33.
    • (1995) J. Biotechnol. , vol.42 , pp. 23-33
    • Boutur, O.1    Dubreucq, E.2    Galzy, P.3
  • 6
    • 0000584821 scopus 로고
    • Lipase catalysed synthesis of esters by reverse hydrolysis
    • Mc Neill G.P., Berger R. Lipase catalysed synthesis of esters by reverse hydrolysis. O.C.L. 2:1995;359-363.
    • (1995) O.C.L. , vol.2 , pp. 359-363
    • Mc Neill, G.P.1    Berger, R.2
  • 7
    • 0030817480 scopus 로고    scopus 로고
    • Lipase catalysed biosynthesis of propanediol monoesters in biphasic aqueous medium
    • Chevandier F., Dubreucq E., Galzy P. Lipase catalysed biosynthesis of propanediol monoesters in biphasic aqueous medium. Biotechnol. Lett. 19:1997;913-917.
    • (1997) Biotechnol. Lett. , vol.19 , pp. 913-917
    • Chevandier, F.1    Dubreucq, E.2    Galzy, P.3
  • 8
    • 0029737033 scopus 로고    scopus 로고
    • Ester synthesis in aqueous media in the presence of various lipases
    • Lecointe C., Dubreucq E., Galzy P. Ester synthesis in aqueous media in the presence of various lipases. Biotechnol. Lett. 18:1996;869-874.
    • (1996) Biotechnol. Lett. , vol.18 , pp. 869-874
    • Lecointe, C.1    Dubreucq, E.2    Galzy, P.3
  • 9
    • 0019879061 scopus 로고
    • Enzymatic synthesis in biphasic aqueous-organic systems. I. Chemical equilibrium shift
    • Martinek K., Semenov A.N., Berezin I.V. Enzymatic synthesis in biphasic aqueous-organic systems. I. Chemical equilibrium shift. Biophys. Biochim. Acta. 658:1981;76-89.
    • (1981) Biophys. Biochim. Acta , vol.658 , pp. 76-89
    • Martinek, K.1    Semenov, A.N.2    Berezin, I.V.3
  • 10
    • 0021518195 scopus 로고
    • Effects of water on equilibria catalysed by hydrolytic enzymes in biphasic reaction systems
    • Halling P.J. Effects of water on equilibria catalysed by hydrolytic enzymes in biphasic reaction systems. Enzyme Microb. Technol. 6:1984;513-516.
    • (1984) Enzyme Microb. Technol. , vol.6 , pp. 513-516
    • Halling, P.J.1
  • 11
    • 0028396938 scopus 로고
    • Thermodynamic predictions for biocatalysis in nonconventional media - Theory, tests, and recommendations for experimental design and analysis
    • Halling P.J. Thermodynamic predictions for biocatalysis in nonconventional media - theory, tests, and recommendations for experimental design and analysis. Enzyme Microb. Technol. 16:1994;178-206.
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 178-206
    • Halling, P.J.1
  • 12
    • 0028817612 scopus 로고
    • Functioning and regioselectivity of the lipase of Candida parapsilosis (Ashford) Langeron and Talice in aqueous medium. New interpretation of regioselectivity taking acyl migration into account
    • Briand D., Dubreucq E., Galzy P. Functioning and regioselectivity of the lipase of Candida parapsilosis (Ashford) Langeron and Talice in aqueous medium. New interpretation of regioselectivity taking acyl migration into account. Eur. J. Biochem. 228:1995;169-175.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 169-175
    • Briand, D.1    Dubreucq, E.2    Galzy, P.3
  • 13
    • 0031042565 scopus 로고    scopus 로고
    • Essential dynamics of lipase binding sites: The effect of inhibitors of different chain length
    • Peters G.H., van Aalten D.M.F., Svendsen A., Bywater R. Essential dynamics of lipase binding sites: the effect of inhibitors of different chain length. Prot. Eng. 10:1997;149-158.
    • (1997) Prot. Eng. , vol.10 , pp. 149-158
    • Peters, G.H.1    Van Aalten, D.M.F.2    Svendsen, A.3    Bywater, R.4
  • 14
    • 0032103791 scopus 로고    scopus 로고
    • Anatomy of lipase binding sites: The scissile fatty acid binding site
    • Pleiss J., Fischer M., Schmid R.D. Anatomy of lipase binding sites: the scissile fatty acid binding site. Chem. Phys. Lipids. 93:1998;67-80.
    • (1998) Chem. Phys. Lipids , vol.93 , pp. 67-80
    • Pleiss, J.1    Fischer, M.2    Schmid, R.D.3
  • 15
    • 0035919135 scopus 로고    scopus 로고
    • Alteration of lipase chain length specificity in the hydrolysis of esters by random mutagenesis
    • Gaskin D.J.H., Romojaro A., Turner N.A., Jenkins J., Vulfson E.N. Alteration of lipase chain length specificity in the hydrolysis of esters by random mutagenesis. Biotechnol. Bioeng. 73:2001;433-441.
    • (2001) Biotechnol. Bioeng. , vol.73 , pp. 433-441
    • Gaskin, D.J.H.1    Romojaro, A.2    Turner, N.A.3    Jenkins, J.4    Vulfson, E.N.5
  • 16
    • 0025870882 scopus 로고
    • Lipases in organic solvents: The fatty acid chain length profile
    • Berger M., Schneider M.P. Lipases in organic solvents: the fatty acid chain length profile. Biotechnol. Lett. 13:1991;641-645.
    • (1991) Biotechnol. Lett. , vol.13 , pp. 641-645
    • Berger, M.1    Schneider, M.P.2
  • 17
    • 84980339403 scopus 로고
    • Specificity of Mucor miehei lipase on methyl ester substrates
    • Aggelis G., Komaitis M., Pina M., Graille J. Specificity of Mucor miehei lipase on methyl ester substrates. Grasas Aceites. 44:1993;331-334.
    • (1993) Grasas Aceites , vol.44 , pp. 331-334
    • Aggelis, G.1    Komaitis, M.2    Pina, M.3    Graille, J.4
  • 18
    • 0029922329 scopus 로고    scopus 로고
    • Substrate specificity and kinetics of Candida rugosa lipase in organic media
    • Janssen A., Vaidya A.M., Halling P.J. Substrate specificity and kinetics of Candida rugosa lipase in organic media. Enzyme Microb. Technol. 18:1996;340-346.
    • (1996) Enzyme Microb. Technol. , vol.18 , pp. 340-346
    • Janssen, A.1    Vaidya, A.M.2    Halling, P.J.3
  • 19
    • 0030288983 scopus 로고    scopus 로고
    • Solvent polarity influences product selectivity of lipase-mediated esterification reactions in microaqueous media
    • Kuo S.J., Parkin K.L. Solvent polarity influences product selectivity of lipase-mediated esterification reactions in microaqueous media. J. Am. Oil Chem. Soc. 73:1996;1427-1433.
    • (1996) J. Am. Oil Chem. Soc. , vol.73 , pp. 1427-1433
    • Kuo, S.J.1    Parkin, K.L.2
  • 21
    • 0033180384 scopus 로고    scopus 로고
    • Comparative selectivities of immobilized lipases from Pseudomonas cepacia and Candida antarctica (fraction B) for esterification reactions with glycerol and glycerol analogues in organic media
    • Chang Q-L., Lee C-H., Parkin K.L. Comparative selectivities of immobilized lipases from Pseudomonas cepacia and Candida antarctica (fraction B) for esterification reactions with glycerol and glycerol analogues in organic media. Enzyme Microb. Technol. 25:1999;290-297.
    • (1999) Enzyme Microb. Technol. , vol.25 , pp. 290-297
    • Chang, Q-L.1    Lee, C-H.2    Parkin, K.L.3
  • 22
    • 0034691712 scopus 로고    scopus 로고
    • Selectivity of Rhizomucor miehei lipase as affected by choice of cosubstrate system in ester modification reactions in organic media
    • Arsan J., Parkin K.L. Selectivity of Rhizomucor miehei lipase as affected by choice of cosubstrate system in ester modification reactions in organic media. Biotechnol. Bioeng. 69:2000;222-226.
    • (2000) Biotechnol. Bioeng. , vol.69 , pp. 222-226
    • Arsan, J.1    Parkin, K.L.2
  • 23
    • 0033996907 scopus 로고    scopus 로고
    • Specificity of papaya lipase in esterification with respect to the chemical structure of substrates
    • Gandhi N.N., Mukherjee K.D. Specificity of papaya lipase in esterification with respect to the chemical structure of substrates. J. Agric. Food Chem. 48:2000;566-570.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 566-570
    • Gandhi, N.N.1    Mukherjee, K.D.2
  • 24
    • 0024399931 scopus 로고
    • Multicompetitive enzymatic reactions in organic media: A simple test for the determination of lipase fatty acid specificity
    • Rangheard M.S., Langrand G., Triantaphylides C., Baratti J.C. Multicompetitive enzymatic reactions in organic media: a simple test for the determination of lipase fatty acid specificity. Biochim. Biophys. Acta. 1004:1989;20-28.
    • (1989) Biochim. Biophys. Acta , vol.1004 , pp. 20-28
    • Rangheard, M.S.1    Langrand, G.2    Triantaphylides, C.3    Baratti, J.C.4
  • 26
    • 0027388770 scopus 로고
    • News from the interface - The molecular structures of triacylglyceride lipases
    • Derewenda Z.S., Sharp A.M. News from the interface - the molecular structures of triacylglyceride lipases. Trends Biochem. Sci. 18:1993;20-25.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 20-25
    • Derewenda, Z.S.1    Sharp, A.M.2
  • 27
    • 0028075638 scopus 로고
    • Elucidating structure-mechanism relationships in lipases: Prospects for predicting and engineering catalytic properties
    • Kazlauskas R.J. Elucidating structure-mechanism relationships in lipases: prospects for predicting and engineering catalytic properties. Trends Biotechnol. 12:1994;464-472.
    • (1994) Trends Biotechnol. , vol.12 , pp. 464-472
    • Kazlauskas, R.J.1
  • 28
    • 0032168569 scopus 로고    scopus 로고
    • Catalytic triads and their relatives
    • Dodsen G., Wlodawer A. Catalytic triads and their relatives. Trends Biochem. Sci. 23:1998;347-352.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 347-352
    • Dodsen, G.1    Wlodawer, A.2
  • 29
    • 0036227421 scopus 로고    scopus 로고
    • The lipase/acyltransferase from Candida parapsilosis: Molecular cloning and characterization of purified recombinant enzymes
    • Neugnot V., Moulin G., Dubreucq E., Bigey F. The lipase/acyltransferase from Candida parapsilosis: molecular cloning and characterization of purified recombinant enzymes. Eur. J. Biochem. 269:2002;1734-1745.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1734-1745
    • Neugnot, V.1    Moulin, G.2    Dubreucq, E.3    Bigey, F.4
  • 30
    • 0029165493 scopus 로고
    • Substrate specificity of the lipase from Candida parapsilosis
    • Briand D., Dubreucq E., Grimaud J., Galzy P. Substrate specificity of the lipase from Candida parapsilosis. Lipids. 30:1995;747-754.
    • (1995) Lipids , vol.30 , pp. 747-754
    • Briand, D.1    Dubreucq, E.2    Grimaud, J.3    Galzy, P.4
  • 31
    • 0035852885 scopus 로고    scopus 로고
    • How do lipases and esterases work: The electrostatic contribution
    • Petersen M.T.N., Fojan P., Petersen S.B. How do lipases and esterases work: the electrostatic contribution. J. Biotechnol. 85:2001;115-147.
    • (2001) J. Biotechnol. , vol.85 , pp. 115-147
    • Petersen, M.T.N.1    Fojan, P.2    Petersen, S.B.3
  • 32
    • 0032946805 scopus 로고    scopus 로고
    • Kinetics of lipase-catalyzed esterification in organic media: Correct model and solvent effects on parameters
    • Janssen A.E.M., Sjursnes B.J., Vakurov A.V., Halling P.J. Kinetics of lipase-catalyzed esterification in organic media: correct model and solvent effects on parameters. Enzyme Microb. Technol. 24:1999;463-470.
    • (1999) Enzyme Microb. Technol. , vol.24 , pp. 463-470
    • Janssen, A.E.M.1    Sjursnes, B.J.2    Vakurov, A.V.3    Halling, P.J.4
  • 34
    • 0034606989 scopus 로고    scopus 로고
    • The nature of fatty acid modifies the equilibrium position in the esterification catalyzed by lipase
    • Flores M.V., Sewalt J.J.W., Janssen A.E.M., van der Padt A. The nature of fatty acid modifies the equilibrium position in the esterification catalyzed by lipase. Biotechnol. Bioeng. 67:2000;364-371.
    • (2000) Biotechnol. Bioeng. , vol.67 , pp. 364-371
    • Flores, M.V.1    Sewalt, J.J.W.2    Janssen, A.E.M.3    Van der Padt, A.4
  • 35
    • 33751385630 scopus 로고
    • Tailoring lipase specificity by solvent and substrate chemistries
    • Parida S., Dordick J.S. Tailoring lipase specificity by solvent and substrate chemistries. J. Org. Chem. 58:1993;3238-3244.
    • (1993) J. Org. Chem. , vol.58 , pp. 3238-3244
    • Parida, S.1    Dordick, J.S.2
  • 36
    • 0028155415 scopus 로고
    • Specificities of enzymes "corrected for solvation" depend on the choice of the standard state
    • Janssen A.E.M., Halling P.J. Specificities of enzymes "corrected for solvation" depend on the choice of the standard state. J. Am. Chem. Soc. 116:1994;9827-9830.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 9827-9830
    • Janssen, A.E.M.1    Halling, P.J.2
  • 37
    • 0034731605 scopus 로고    scopus 로고
    • Lipase protein engineering
    • Svendsen A. Lipase protein engineering. Biochim. Biophys. Acta. 1543:2000;223-238.
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 223-238
    • Svendsen, A.1
  • 38
    • 0033963834 scopus 로고    scopus 로고
    • Molecular modeling and biocatalysis: Explanations, predictions, limitations, and opportunities
    • Kazlauskas R.J. Molecular modeling and biocatalysis: explanations, predictions, limitations, and opportunities. Curr. Opin. Chem. Biol. 4:2000;81-88.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 81-88
    • Kazlauskas, R.J.1


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