메뉴 건너뛰기




Volumn 50, Issue 23, 2011, Pages 12975-12983

Kinetic modeling and statistical optimization of lipase catalyzed enantioselective resolution of (R,S)-2-pentanol

Author keywords

[No Author keywords available]

Indexed keywords

2-PENTANOL; ACYL DONORS; AMYLOID PEPTIDES; BOX-BEHNKEN DESIGN; CHIRAL INTERMEDIATES; EFFICIENT CATALYSTS; ENANTIOMERIC EXCESS; ENANTIOSELECTIVE; ENZYME LOADING; INITIAL RATE; KINETIC MODELING; KINETIC RESOLUTION; KINETICS AND MECHANISM; LIPASE-CATALYZED; MOLAR RATIO; NOVOZYME 435; PING-PONG BI-BI MECHANISM; PROCESS PARAMETERS; PROGRESS CURVES; RESPONSE SURFACE METHODOLOGY; STATISTICAL OPTIMIZATION; VINYL ACETATES;

EID: 82555165512     PISSN: 08885885     EISSN: 15205045     Source Type: Journal    
DOI: 10.1021/ie2012032     Document Type: Article
Times cited : (27)

References (35)
  • 2
    • 0037010695 scopus 로고    scopus 로고
    • Desymmetrisation of prochiral ketones using lipases
    • Carnell, A. J. Desymmetrisation of prochiral ketones using lipases J. Mol. Catal. B: Enzym. 2002, 19-20, 83
    • (2002) J. Mol. Catal. B: Enzym. , vol.1920 , pp. 83
    • Carnell, A.J.1
  • 3
    • 63249106284 scopus 로고    scopus 로고
    • Optimization of (R,S)-1-phenylethanol kinetic resolution over Candida antarctica lipase B in ionic liquids
    • Habulin, M.; Knez, Ž. Optimization of (R,S)-1-phenylethanol kinetic resolution over Candida antarctica lipase B in ionic liquids J. Mol. Catal. B: Enzym. 2009, 58, 24
    • (2009) J. Mol. Catal. B: Enzym. , vol.58 , pp. 24
    • Habulin, M.1    Knez, Ž.2
  • 4
    • 0000088021 scopus 로고
    • Lipase catalysis and its applications
    • In; Plenum Press, New York.
    • John, V. T.; Abraham, G.; Dordick, J. S. Lipase catalysis and its applications. In Biocatalysts for Industry; Plenum Press, New York, 1991, 193.
    • (1991) Biocatalysts for Industry , pp. 193
    • John, V.T.1    Abraham, G.2    Dordick, J.S.3
  • 5
    • 0031023666 scopus 로고    scopus 로고
    • "interfacial activation" of lipases: Facts and artifacts
    • Verger, R. "Interfacial activation" of lipases: facts and artifacts Trends Biotechnol 1997, 15, 32
    • (1997) Trends Biotechnol , vol.15 , pp. 32
    • Verger, R.1
  • 6
    • 2342489872 scopus 로고    scopus 로고
    • Enzyme-catalysed optical resolution of mandelic acid via RS(±)-methyl mandelate in non-aqueous media
    • Yadav, G. D.; Sivakumar, P. Enzyme-catalysed optical resolution of mandelic acid via RS(±)-methyl mandelate in non-aqueous media Biochem. Eng. J. 2004, 19, 101
    • (2004) Biochem. Eng. J. , vol.19 , pp. 101
    • Yadav, G.D.1    Sivakumar, P.2
  • 7
    • 0035303164 scopus 로고    scopus 로고
    • A kinetic model for the enzyme-catalysed self epoxidation of oleic acid
    • Yadav, G. D. A kinetic model for the enzyme-catalysed self epoxidation of oleic acid J. Am. Oil Chem. Soc. 2001, 78, 347
    • (2001) J. Am. Oil Chem. Soc. , vol.78 , pp. 347
    • Yadav, G.D.1
  • 8
    • 0036208210 scopus 로고    scopus 로고
    • Enzymatic synthesis of perlauric acid using Novozyme 435
    • Yadav, G. D.; Devi, K. M. Enzymatic synthesis of perlauric acid using Novozyme 435 Biochem. Eng. J. 2002, 10, 93
    • (2002) Biochem. Eng. J. , vol.10 , pp. 93
    • Yadav, G.D.1    Devi, K.M.2
  • 9
    • 0142089984 scopus 로고    scopus 로고
    • Kinetics and mechanism of synthesis of butyl isobutyrate over immobilised lipases
    • Yadav, G. D.; Lathi, P. S. Kinetics and mechanism of synthesis of butyl isobutyrate over immobilised lipases Biochem. Eng. J. 2003, 16, 245
    • (2003) Biochem. Eng. J. , vol.16 , pp. 245
    • Yadav, G.D.1    Lathi, P.S.2
  • 10
    • 0347915737 scopus 로고    scopus 로고
    • Kinetic of hydrolysis of tetrahydrofurfuryl butyrate in a three phase system containing immobilized lipase from Candida antarctica
    • Yadav, G. D.; Devi, K. M. Kinetic of hydrolysis of tetrahydrofurfuryl butyrate in a three phase system containing immobilized lipase from Candida antarctica Biochem. Eng. J. 2004, 17, 57
    • (2004) Biochem. Eng. J. , vol.17 , pp. 57
    • Yadav, G.D.1    Devi, K.M.2
  • 11
    • 0942291113 scopus 로고    scopus 로고
    • Immobilized lipase-catalysed esterification and transesterication reactions in non-aqueous media for the synthesis of tetrahydrofurfuryl butyrate: Comparison and kinetic modeling
    • Yadav, G. D.; Devi, K. M. Immobilized lipase-catalysed esterification and transesterication reactions in non-aqueous media for the synthesis of tetrahydrofurfuryl butyrate: comparison and kinetic modeling Chem. Eng. Sci. 2004, 59, 373
    • (2004) Chem. Eng. Sci. , vol.59 , pp. 373
    • Yadav, G.D.1    Devi, K.M.2
  • 12
    • 0038735357 scopus 로고    scopus 로고
    • Kinetic modeling of immobilized-lipase catalyzed transesterification of n -octanol with vinyl acetate in non-aqueous media
    • Yadav, G. D.; Trivedi, A. H. Kinetic modeling of immobilized-lipase catalyzed transesterification of n -octanol with vinyl acetate in non-aqueous media Enzyme Microb. Technol. 2003, 32, 783
    • (2003) Enzyme Microb. Technol. , vol.32 , pp. 783
    • Yadav, G.D.1    Trivedi, A.H.2
  • 14
    • 10744226218 scopus 로고    scopus 로고
    • Kinetic resolution of rac-2-pentanol catalyzed by Candida antartica lipase in the ionic liquid, 1-butyl-3-methylimidazolium bis[(trifluromethyl) sulfonyl] amide
    • Noël, M.; Lozano, P.; Vaultier, M; Iborra, J. L. Kinetic resolution of rac-2-pentanol catalyzed by Candida antartica lipase in the ionic liquid, 1-butyl-3-methylimidazolium bis[(trifluromethyl)sulfonyl] amide Biotechnol. Lett. 2004, 24, 301
    • (2004) Biotechnol. Lett. , vol.24 , pp. 301
    • Noël, M.1    Lozano, P.2    Vaultier, M.3    Iborra, J.L.4
  • 15
    • 41949130878 scopus 로고    scopus 로고
    • On the development of an integrated membrane process with ionic liquids for the kinetic resolution of rac-2-pentanol
    • Hernández-Fernández, F. J.; de los Ríos, A. P.; Tomás-Alonso, F.; Gómez, D.; Víllora, G. On the development of an integrated membrane process with ionic liquids for the kinetic resolution of rac-2-pentanol J. Membr. Sci. 2008, 314, 238
    • (2008) J. Membr. Sci. , vol.314 , pp. 238
    • Hernández-Fernández, F.J.1    De Los Ríos, A.P.2    Tomás-Alonso, F.3    Gómez, D.4    Víllora, G.5
  • 16
    • 9644264173 scopus 로고    scopus 로고
    • Enantioselective acylation of R-2-pentanol in a solid/gas reactor catalysed by lipase B from Candida antatrtica
    • Leonard, V.; Lamare, S.; Legoy, M. D.; Graber, M. Enantioselective acylation of R-2-pentanol in a solid/gas reactor catalysed by lipase B from Candida antatrtica J. Mol. Catal. B. Enzym. 2004, 32, 53
    • (2004) J. Mol. Catal. B. Enzym. , vol.32 , pp. 53
    • Leonard, V.1    Lamare, S.2    Legoy, M.D.3    Graber, M.4
  • 17
    • 7444245720 scopus 로고    scopus 로고
    • Lipase-mediated chiral resolution of racemates in organic solvents
    • Ghanem, A.; Aboul-Enein, H. Y. Lipase-mediated chiral resolution of racemates in organic solvents Tetrahedron: Asymmetry 2004, 15, 3331
    • (2004) Tetrahedron: Asymmetry , vol.15 , pp. 3331
    • Ghanem, A.1    Aboul-Enein, H.Y.2
  • 18
    • 13344277260 scopus 로고    scopus 로고
    • Enantioselective enzymatic desymmetrizations in organic synthesis
    • García-Urdiales, E.; Alfonso, I.; Gotor, V. Enantioselective enzymatic desymmetrizations in organic synthesis Chem. Rev. 2005, 105, 313
    • (2005) Chem. Rev. , vol.105 , pp. 313
    • García-Urdiales, E.1    Alfonso, I.2    Gotor, V.3
  • 19
    • 0029872834 scopus 로고    scopus 로고
    • Enantioselective synthesis through enzymatic asymmetrization
    • Schoffers, E.; Golebiowski, A.; Johnson, C. R. Enantioselective synthesis through enzymatic asymmetrization Tetrahedron 1996, 52, 3769
    • (1996) Tetrahedron , vol.52 , pp. 3769
    • Schoffers, E.1    Golebiowski, A.2    Johnson, C.R.3
  • 20
    • 0141507063 scopus 로고    scopus 로고
    • Reagents for (ir) reversible enzymatic acylations
    • Hanefeld, U. Reagents for (ir) reversible enzymatic acylations Org. Biomol. Chem. 2003, 1, 2405
    • (2003) Org. Biomol. Chem. , vol.1 , pp. 2405
    • Hanefeld, U.1
  • 21
    • 66149171355 scopus 로고    scopus 로고
    • Lipase-mediated enantioselective acylation of alcohols with functionalized vinyl esters: Acyl donor tolerance and applications
    • Chnevert, R.; Pelchat, N.; Morin, P. Lipase-mediated enantioselective acylation of alcohols with functionalized vinyl esters: acyl donor tolerance and applications Tetrahedron: Asymmetry 2009, 20, 1191
    • (2009) Tetrahedron: Asymmetry , vol.20 , pp. 1191
    • Chnevert, R.1    Pelchat, N.2    Morin, P.3
  • 22
    • 33646867639 scopus 로고    scopus 로고
    • Lipases: Useful biocatalysts for the preparation of pharmaceuticals
    • Gotor-Fernandez, V.; Brieva, R.; Gotor, V. Lipases: Useful biocatalysts for the preparation of pharmaceuticals J. Mol. Catal. B: Enzym. 2006, 40, 111
    • (2006) J. Mol. Catal. B: Enzym. , vol.40 , pp. 111
    • Gotor-Fernandez, V.1    Brieva, R.2    Gotor, V.3
  • 23
    • 0026674657 scopus 로고
    • Enzyme-catalyzed irreversible acyl transfer
    • Faber, K.; Riva, S. Enzyme-catalyzed irreversible acyl transfer Synthesis 1992, 10, 895
    • (1992) Synthesis , vol.10 , pp. 895
    • Faber, K.1    Riva, S.2
  • 24
    • 0025733902 scopus 로고
    • "immunization" of lipase against acetaldehyde emerging in acyl transfer reactions from vinyl acetate
    • Berger, B.; Faber, K. "Immunization" of lipase against acetaldehyde emerging in acyl transfer reactions from vinyl acetate J. Chem. Soc., Chem. Commun. 1991, 1198
    • (1991) J. Chem. Soc., Chem. Commun. , pp. 1198
    • Berger, B.1    Faber, K.2
  • 25
    • 0001463261 scopus 로고
    • Irreversible and highly enantioselective acylation of 2-halo-1-arylethanols in organic solvents catalyzed by a lipase from Pseudomonas fluorescens
    • Hiratake, J.; Inagaki, M.; Nishioka, T.; Oda, J. Irreversible and highly enantioselective acylation of 2-halo-1-arylethanols in organic solvents catalyzed by a lipase from Pseudomonas fluorescens J. Org. Chem. 1988, 53, 6130
    • (1988) J. Org. Chem. , vol.53 , pp. 6130
    • Hiratake, J.1    Inagaki, M.2    Nishioka, T.3    Oda, J.4
  • 26
    • 67651098843 scopus 로고    scopus 로고
    • Influence of temperature on the activity and enantioselectivity of Burkholderia cepacia lipase in the kinetic resolution of mandelic acid enantiomers
    • D'bkowska, K.; Szewczyk, K. W. Influence of temperature on the activity and enantioselectivity of Burkholderia cepacia lipase in the kinetic resolution of mandelic acid enantiomers Biochem. Eng. J. 2009, 46, 147
    • (2009) Biochem. Eng. J. , vol.46 , pp. 147
    • D'bkowska, K.1    Szewczyk, K.W.2
  • 27
    • 0037018905 scopus 로고    scopus 로고
    • Effects of solvent, water activity, and temperature on lipase and hydroxynitrile lyase enantioselectivity
    • Persson, M.; Costes, D.; Wehtje, E.; Adlercreutz, P. Effects of solvent, water activity, and temperature on lipase and hydroxynitrile lyase enantioselectivity Enzyme Microb. Technol. 2002, 30, 916
    • (2002) Enzyme Microb. Technol. , vol.30 , pp. 916
    • Persson, M.1    Costes, D.2    Wehtje, E.3    Adlercreutz, P.4
  • 28
    • 2942652790 scopus 로고    scopus 로고
    • The effect of temperature on the lipase catalyzed asymmetric protonation of 1-acetoxy-2-methylcyclohexane giving (R)-2-methylcyclohexanone
    • Sakai, T.; Matsuda, A.; Tanaka, Y.; Korenaga, T.; Ema, T. The effect of temperature on the lipase catalyzed asymmetric protonation of 1-acetoxy-2-methylcyclohexane giving (R)-2-methylcyclohexanone Tetrahedron: Asymmetry 2004, 15, 1929
    • (2004) Tetrahedron: Asymmetry , vol.15 , pp. 1929
    • Sakai, T.1    Matsuda, A.2    Tanaka, Y.3    Korenaga, T.4    Ema, T.5
  • 29
    • 29844443252 scopus 로고    scopus 로고
    • Kinetic modeling of lipase catalyzed hydrolysis of (R/S)-1-methoxy-3- propyl-acetate as a model reaction for production of chiral secondary alcohols
    • Berendsen, W. R.; Gendrot, G.; Resnick, S.; Reuss, M. Kinetic modeling of lipase catalyzed hydrolysis of (R/S)-1-methoxy-3-propyl-acetate as a model reaction for production of chiral secondary alcohols J. Biotechnol. 2006, 121, 213
    • (2006) J. Biotechnol. , vol.121 , pp. 213
    • Berendsen, W.R.1    Gendrot, G.2    Resnick, S.3    Reuss, M.4
  • 30
    • 79953726278 scopus 로고    scopus 로고
    • Optimization and kinetic modeling of lipase catalyzed enantioselective N-acetylation of (±)-1-phenylethylamine under microwave irradiation
    • Sontakke, J. B.; Yadav, G. D. Optimization and kinetic modeling of lipase catalyzed enantioselective N-acetylation of (±)-1-phenylethylamine under microwave irradiation J. Chem. Technol. Biotechnol. 2011, 86, 739
    • (2011) J. Chem. Technol. Biotechnol. , vol.86 , pp. 739
    • Sontakke, J.B.1    Yadav, G.D.2
  • 31
    • 32844467268 scopus 로고    scopus 로고
    • Intensification of enzymatic synthesis of propylene glycol monolaurate from 1,2-propanediol and lauric acid under microwave irradiation: Kinetics of forward and reverse reactions
    • Yadav, G. D.; Lathi, P. S. Intensification of enzymatic synthesis of propylene glycol monolaurate from 1,2-propanediol and lauric acid under microwave irradiation: Kinetics of forward and reverse reactions Enzyme Microb Technol. 2006, 38, 814
    • (2006) Enzyme Microb Technol. , vol.38 , pp. 814
    • Yadav, G.D.1    Lathi, P.S.2
  • 32
    • 69949161220 scopus 로고    scopus 로고
    • Kinetic and mechanistic investigation of microwave-assisted lipase catalyzed synthesis of citronellyl acetate
    • Yadav, G. D.; Borkar, I. V. Kinetic and mechanistic investigation of microwave-assisted lipase catalyzed synthesis of citronellyl acetate Ind. Eng. Chem. Res. 2009, 48, 7915
    • (2009) Ind. Eng. Chem. Res. , vol.48 , pp. 7915
    • Yadav, G.D.1    Borkar, I.V.2
  • 33
    • 80052590105 scopus 로고    scopus 로고
    • Optimization of chiral resolution of (±)-1-phenylethanol by statistical methods
    • Yadav, G. D.; Sontakke, J. B. Optimization of chiral resolution of (±)-1-phenylethanol by statistical methods Int. J. Chem. React. Eng. 2011, 9, A77
    • (2011) Int. J. Chem. React. Eng. , vol.9 , pp. 77
    • Yadav, G.D.1    Sontakke, J.B.2
  • 34
    • 0003518480 scopus 로고
    • Wiley Interscience: New York.
    • Segel, I. H. Enzyme Kinetics; Wiley Interscience: New York, 1975.
    • (1975) Enzyme Kinetics
    • Segel, I.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.