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Volumn 48, Issue 5-6, 2013, Pages 819-830

Immobilized Pseudomonas sp. lipase: A powerful biocatalyst for asymmetric acylation of (±)-2-amino-1-phenylethanols with vinyl acetate

Author keywords

Asymmetric acylation; Box Behnken design; Enantiopure 2 amino 1 phenylethanols; Response surface methodology

Indexed keywords

ASYMMETRIC ACYLATION; BOX-BEHNKEN DESIGN; ENANTIOPURE; OPTIMIZED CONDITIONS; PSEUDOMONAS SP. LIPASE; RESPONSE SURFACE METHODOLOGY; SCHIFF BASE FORMATION; SODIUM CYANOBOROHYDRIDE;

EID: 84878693702     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2013.04.019     Document Type: Article
Times cited : (19)

References (61)
  • 1
    • 77956174740 scopus 로고    scopus 로고
    • Single enantiomeric β-blockers - The existing technologies
    • J. Agustian, A.H. Kamaruddin, and S. Bhatia Single enantiomeric β-blockers - the existing technologies Process Biochem 45 2010 1587 1604
    • (2010) Process Biochem , vol.45 , pp. 1587-1604
    • Agustian, J.1    Kamaruddin, A.H.2    Bhatia, S.3
  • 2
    • 84878682587 scopus 로고    scopus 로고
    • Beta-blockers in the treatment of cardiovascular disease
    • D. Cullington, A. Yassin, and J. Cleland Beta-blockers in the treatment of cardiovascular disease Prescriber 19 2008 31 39
    • (2008) Prescriber , vol.19 , pp. 31-39
    • Cullington, D.1    Yassin, A.2    Cleland, J.3
  • 3
    • 0038725683 scopus 로고    scopus 로고
    • Beta-adrenergic blockers
    • W.H. Frishman Beta-adrenergic blockers Circulation 107 2003 117 119
    • (2003) Circulation , vol.107 , pp. 117-119
    • Frishman, W.H.1
  • 4
    • 0035794898 scopus 로고    scopus 로고
    • Current utilisation trends for beta blockers in cardiovascular disease
    • H.L. Kennedy Current utilisation trends for beta blockers in cardiovascular disease Am J Med 110 2001 2 6
    • (2001) Am J Med , vol.110 , pp. 2-6
    • Kennedy, H.L.1
  • 5
    • 0035735019 scopus 로고    scopus 로고
    • Stereospecific pharmacokinetics and pharmacodynamics of beta-adrenergic blockers in humans
    • R. Mehvar, and D.R. Brocks Stereospecific pharmacokinetics and pharmacodynamics of beta-adrenergic blockers in humans J Pharm Sci 4 2001 185 200
    • (2001) J Pharm Sci , vol.4 , pp. 185-200
    • Mehvar, R.1    Brocks, D.R.2
  • 6
    • 0022344552 scopus 로고
    • Cardio beta-adrenoceptor blockade: The guest for selectivity
    • A.M. Barret Cardio beta-adrenoceptor blockade: the guest for selectivity J Pharm Sci 2 1985 95 108
    • (1985) J Pharm Sci , vol.2 , pp. 95-108
    • Barret, A.M.1
  • 7
    • 77949915679 scopus 로고    scopus 로고
    • Lipase resolution of new (±)-3-aryloxy-1-halogenopropan-2-ols: Versatile building blocks for β-adrenergic receptor antagonists
    • M. Maciejewski, K. Półtorak, and J.E. Kamińska Lipase resolution of new (±)-3-aryloxy-1-halogenopropan-2-ols: versatile building blocks for β-adrenergic receptor antagonists J Mol Catal B: Enzym 62 2010 248 256
    • (2010) J Mol Catal B: Enzym , vol.62 , pp. 248-256
    • Maciejewski, M.1    Półtorak, K.2    Kamińska, J.E.3
  • 8
    • 84886975315 scopus 로고    scopus 로고
    • Biocatalysis for synthesis for chiral pharmaceutical intermediates
    • R.N. Patel, CRC Press Boca Raton
    • R.N. Patel Biocatalysis for synthesis for chiral pharmaceutical intermediates R.N. Patel, Biocatalysis in the Pharmaceutical and Biotechnology Industries 2006 CRC Press Boca Raton 105 158
    • (2006) Biocatalysis in the Pharmaceutical and Biotechnology Industries , pp. 105-158
    • Patel, R.N.1
  • 10
    • 56049097692 scopus 로고    scopus 로고
    • Lipase-catalyzed chemoselective aminolysis of various aminoalcohols with fatty acids
    • L. Couturier, D. Taupin, and F. Yvergnaux Lipase-catalyzed chemoselective aminolysis of various aminoalcohols with fatty acids J Mol Catal B: Enzym 56 2009 29 33
    • (2009) J Mol Catal B: Enzym , vol.56 , pp. 29-33
    • Couturier, L.1    Taupin, D.2    Yvergnaux, F.3
  • 11
    • 78649904292 scopus 로고    scopus 로고
    • Scale up of a novel tri-substrate fermentation for enhanced production of Aspergillus niger lipase for tallow hydrolysis
    • N.G. Edwinoliver, K. Thirunavukarasu, R.B. Naidu, M.K. Gowthaman, T.N. Kambe, and N.R. Kamini Scale up of a novel tri-substrate fermentation for enhanced production of Aspergillus niger lipase for tallow hydrolysis Bioresour Technol 101 2010 6791 6796
    • (2010) Bioresour Technol , vol.101 , pp. 6791-6796
    • Edwinoliver, N.G.1    Thirunavukarasu, K.2    Naidu, R.B.3    Gowthaman, M.K.4    Kambe, T.N.5    Kamini, N.R.6
  • 12
    • 73749086243 scopus 로고    scopus 로고
    • Stabilization of Candida rugosa lipase during transacetylation with vinyl acetate
    • A.B. Majumder, and M.N. Gupta Stabilization of Candida rugosa lipase during transacetylation with vinyl acetate Bioresour Technol 101 2010 2877 2879
    • (2010) Bioresour Technol , vol.101 , pp. 2877-2879
    • Majumder, A.B.1    Gupta, M.N.2
  • 16
    • 33644673625 scopus 로고    scopus 로고
    • Effects of organic solvents and ionic liquids on the aminolysis of (RS)-methyl mandelate catalyzed by lipases
    • C. Pilissão, and M.G. Nascimento Effects of organic solvents and ionic liquids on the aminolysis of (RS)-methyl mandelate catalyzed by lipases Tetrahedron: Asymmetry 17 2006 428 433
    • (2006) Tetrahedron: Asymmetry , vol.17 , pp. 428-433
    • Pilissão, C.1    Nascimento, M.G.2
  • 17
    • 78650707084 scopus 로고    scopus 로고
    • Immobilization of Candida rugosa lipase on glass beads for enantioselective hydrolysis of racemic Naproxen methyl ester
    • E. Yilmaz, K. Can, M. Sezgin, and M. Yilmaz Immobilization of Candida rugosa lipase on glass beads for enantioselective hydrolysis of racemic Naproxen methyl ester Bioresour Technol 102 2011 499 506
    • (2011) Bioresour Technol , vol.102 , pp. 499-506
    • Yilmaz, E.1    Can, K.2    Sezgin, M.3    Yilmaz, M.4
  • 18
    • 34548444587 scopus 로고    scopus 로고
    • Enantiomeric resolution by lipase-catalysed esterification of a trans-5,6-dihydro-1,10-phenanthroline possessing helical and central chirality
    • C. Sanfilippo, and G. Nicolosi Enantiomeric resolution by lipase-catalysed esterification of a trans-5,6-dihydro-1,10-phenanthroline possessing helical and central chirality Tetrahedron: Asymmetry 18 2007 1828 1832
    • (2007) Tetrahedron: Asymmetry , vol.18 , pp. 1828-1832
    • Sanfilippo, C.1    Nicolosi, G.2
  • 19
    • 33646867639 scopus 로고    scopus 로고
    • Lipases: Useful biocatalysts for the preparation of pharmaceuticals
    • V. Gotor-Fernández, R. Brieva, and V. Gotor Lipases: useful biocatalysts for the preparation of pharmaceuticals J Mol Catal B: Enzym 40 2006 111 120
    • (2006) J Mol Catal B: Enzym , vol.40 , pp. 111-120
    • Gotor-Fernández, V.1    Brieva, R.2    Gotor, V.3
  • 20
    • 63249107465 scopus 로고    scopus 로고
    • Lipase mediated resolution of γ-azidoalcohols in aqueous and organic media: Synthesis of (R)- and (S)-fluoxetine and duloxetine
    • A. Kamal, M.S. Malik, A.A. Shaik, and S. Azeeza Lipase mediated resolution of γ-azidoalcohols in aqueous and organic media: synthesis of (R)- and (S)-fluoxetine and duloxetine J Mol Catal B: Enzym 58 2009 132 137
    • (2009) J Mol Catal B: Enzym , vol.58 , pp. 132-137
    • Kamal, A.1    Malik, M.S.2    Shaik, A.A.3    Azeeza, S.4
  • 22
    • 78650818528 scopus 로고    scopus 로고
    • Control of protein immobilization: Coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance
    • K. Hernandez, and R. Fernandez-Lafuente Control of protein immobilization: coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance Enzyme Microb Technol 48 2011 107 122
    • (2011) Enzyme Microb Technol , vol.48 , pp. 107-122
    • Hernandez, K.1    Fernandez-Lafuente, R.2
  • 24
    • 1842474522 scopus 로고    scopus 로고
    • Enzymatic resolution of (±)-glycidyl butyrate in aqueous media. Strong modulation of the properties of the lipase from Rhizopus oryzae via immobilization techniques
    • J.M. Palomo, R.L. Segura, G. Fernandez-Lorente, J.M. Guisan, and R. Fernandez-Lafuente Enzymatic resolution of (±)-glycidyl butyrate in aqueous media. Strong modulation of the properties of the lipase from Rhizopus oryzae via immobilization techniques Tetrahedron: Asymmetry 15 2004 1157 1161
    • (2004) Tetrahedron: Asymmetry , vol.15 , pp. 1157-1161
    • Palomo, J.M.1    Segura, R.L.2    Fernandez-Lorente, G.3    Guisan, J.M.4    Fernandez-Lafuente, R.5
  • 25
    • 33747799719 scopus 로고    scopus 로고
    • Enantioselectivity modulation through immobilization of Arthrobacter sp. lipase: Kinetic resolution of fluoxetine intermediate
    • A. Chaubey, R. Parshad, S. Koul, S.C. Taneja, and G.N. Qazi Enantioselectivity modulation through immobilization of Arthrobacter sp. lipase: kinetic resolution of fluoxetine intermediate J Mol Catal B: Enzym 42 2006 39 44
    • (2006) J Mol Catal B: Enzym , vol.42 , pp. 39-44
    • Chaubey, A.1    Parshad, R.2    Koul, S.3    Taneja, S.C.4    Qazi, G.N.5
  • 26
    • 33847415451 scopus 로고    scopus 로고
    • Glutaraldehyde modification of lipases adsorbed on aminated supports: A simple way to improve their behaviour as enantioselective biocatalyst
    • J.M. Palomo, R.L. Segura, G. Fernandez-Lorente, R. Fernandez-Lafuente, and J.M. Guisan Glutaraldehyde modification of lipases adsorbed on aminated supports: a simple way to improve their behaviour as enantioselective biocatalyst Enzyme Microb Technol 40 2007 704 707
    • (2007) Enzyme Microb Technol , vol.40 , pp. 704-707
    • Palomo, J.M.1    Segura, R.L.2    Fernandez-Lorente, G.3    Fernandez-Lafuente, R.4    Guisan, J.M.5
  • 28
    • 9644260521 scopus 로고    scopus 로고
    • Enantiomers of adrenaline-type amino alcohols by Burkholderia cepacia lipase-catalyzed asymmetric acylation
    • K. Lundell, E. Katainen, A. Kiviniemi, and L.T. Kanerva Enantiomers of adrenaline-type amino alcohols by Burkholderia cepacia lipase-catalyzed asymmetric acylation Tetrahedron: Asymmetry 15 2004 3723 3729
    • (2004) Tetrahedron: Asymmetry , vol.15 , pp. 3723-3729
    • Lundell, K.1    Katainen, E.2    Kiviniemi, A.3    Kanerva, L.T.4
  • 29
    • 84878689986 scopus 로고    scopus 로고
    • Adrenomimetic drugs
    • C.R. Craig, R.E. Stitzel, Lippincott Williams & Wilkins Philadelphia
    • T.J.F. Lee, and R.E. Stitzel Adrenomimetic drugs C.R. Craig, R.E. Stitzel, Modern pharmacology with clinical applications 2004 Lippincott Williams & Wilkins Philadelphia 109 121
    • (2004) Modern Pharmacology with Clinical Applications , pp. 109-121
    • Lee, T.J.F.1    Stitzel, R.E.2
  • 33
    • 3042728749 scopus 로고    scopus 로고
    • Response surface methodological study on lipase-catalyzed synthesis of amino acid surfactants
    • E.L. Soo, A.B. Salleh, M. Basri, R.N.Z.A. Rahman, and K. Kamaruddin Response surface methodological study on lipase-catalyzed synthesis of amino acid surfactants Process Biochem 39 2004 1511 1518
    • (2004) Process Biochem , vol.39 , pp. 1511-1518
    • Soo, E.L.1    Salleh, A.B.2    Basri, M.3    Rahman, R.N.Z.A.4    Kamaruddin, K.5
  • 34
    • 70249138271 scopus 로고    scopus 로고
    • Synthesis of structured lipid with balanced omega-3:omega-6 ratio by lipase-catalyzed acidolysis reaction: Optimization of reaction using response surface methodology
    • M. Sharma, N.K. Rastogi, and B.R. Lokesh Synthesis of structured lipid with balanced omega-3:omega-6 ratio by lipase-catalyzed acidolysis reaction: optimization of reaction using response surface methodology Process Biochem 44 2009 1284 1288
    • (2009) Process Biochem , vol.44 , pp. 1284-1288
    • Sharma, M.1    Rastogi, N.K.2    Lokesh, B.R.3
  • 35
    • 77955662366 scopus 로고    scopus 로고
    • Optimization of immobilization for selective oxidation of benzyl alcohol by Gluconobacter oxydans using response surface methodology
    • J. Wu, J-L. Wang, M-H. Li, J-P. Lin, and D-Z. Wei Optimization of immobilization for selective oxidation of benzyl alcohol by Gluconobacter oxydans using response surface methodology Bioresour Technol 101 2010 8936 8941
    • (2010) Bioresour Technol , vol.101 , pp. 8936-8941
    • Wu, J.1    Wang, J.-L.2    Li, M.-H.3    Lin, J.-P.4    Wei, D.-Z.5
  • 36
    • 80054978339 scopus 로고    scopus 로고
    • Rapid and high yields of synthesis of butyl acetate catalyzed by Novozym 435: Reaction optimization by response surface methodology
    • A.B. Martins, N.G. Graebin, A.S.G. Lorenzoni, R. Fernandez-Lafuente, M.A.Z. Ayub, and R.C. Rodrigues Rapid and high yields of synthesis of butyl acetate catalyzed by Novozym 435: reaction optimization by response surface methodology Process Biochem 46 2011 2311 2316
    • (2011) Process Biochem , vol.46 , pp. 2311-2316
    • Martins, A.B.1    Graebin, N.G.2    Lorenzoni, A.S.G.3    Fernandez-Lafuente, R.4    Ayub, M.A.Z.5    Rodrigues, R.C.6
  • 37
    • 84856900387 scopus 로고    scopus 로고
    • Optimization of immobilization conditions of Thermomyces lanuginosus lipase on olive pomace powder using response surface methodology
    • Y. Yücel Optimization of immobilization conditions of Thermomyces lanuginosus lipase on olive pomace powder using response surface methodology Biocatal Agric Biotechnol 1 2012 20 24
    • (2012) Biocatal Agric Biotechnol , vol.1 , pp. 20-24
    • Yücel, Y.1
  • 38
    • 64549149728 scopus 로고    scopus 로고
    • Using the Box-Benkhen technique to statistically model phenol photocatalytic degradation by titanium dioxide nanoparticles
    • S. Ray, J.A. Lalman, and N. Biswas Using the Box-Benkhen technique to statistically model phenol photocatalytic degradation by titanium dioxide nanoparticles Chem Eng J 150 2009 15 24
    • (2009) Chem Eng J , vol.150 , pp. 15-24
    • Ray, S.1    Lalman, J.A.2    Biswas, N.3
  • 39
    • 0017267831 scopus 로고
    • Covalent coupling methods for inorganic support materials
    • K. Mosbach, Academic Press London
    • H.H. Weetall Covalent coupling methods for inorganic support materials K. Mosbach, Methods in enzymology 1976 Academic Press London 134 148
    • (1976) Methods in Enzymology , pp. 134-148
    • Weetall, H.H.1
  • 40
    • 82955203394 scopus 로고    scopus 로고
    • Covalent immobilization of catalase onto spacer-arm attached modified Florisil: Characterization and application to batch and plug-flow type reactor systems
    • Ö. Alptekin, S.S. Tükel, D. Yildirim, and D. Alagöz Covalent immobilization of catalase onto spacer-arm attached modified Florisil: characterization and application to batch and plug-flow type reactor systems Enzyme Microb Technol 49 2011 547 554
    • (2011) Enzyme Microb Technol , vol.49 , pp. 547-554
    • Alptekin, Ö.1    Tükel, S.S.2    Yildirim, D.3    Alagöz, D.4
  • 41
    • 0025194036 scopus 로고
    • Colorimetric micromethods for glutaraldehyde determination by means of phenol and sulfuric acid or phenol and perchloric acid
    • J. Boratynski, and T. Zal Colorimetric micromethods for glutaraldehyde determination by means of phenol and sulfuric acid or phenol and perchloric acid Anal Biochem 184 1990 259 262
    • (1990) Anal Biochem , vol.184 , pp. 259-262
    • Boratynski, J.1    Zal, T.2
  • 43
    • 0142258126 scopus 로고    scopus 로고
    • Immobilization of Candida rugosa lipase on chitosan with activation of the hydroxyl groups
    • S.-H. Chiou, and W.-T. Wu Immobilization of Candida rugosa lipase on chitosan with activation of the hydroxyl groups Biomaterials 25 2004 197 204
    • (2004) Biomaterials , vol.25 , pp. 197-204
    • Chiou, S.-H.1    Wu, W.-T.2
  • 45
    • 4344622619 scopus 로고    scopus 로고
    • Immobilization and kinetics of catalase onto magnesium silicate
    • S.S. Tukel, and O. Alptekin Immobilization and kinetics of catalase onto magnesium silicate Process Biochem 39 2004 2149 2150
    • (2004) Process Biochem , vol.39 , pp. 2149-2150
    • Tukel, S.S.1    Alptekin, O.2
  • 46
    • 27644433987 scopus 로고    scopus 로고
    • Activity and storage stability of immobilized glucose oxidase onto magnesium silicate
    • G. Ozyilmaz, S.S. Tukel, and O. Alptekin Activity and storage stability of immobilized glucose oxidase onto magnesium silicate J Mol Catal B: Enzym 35 2005 154 160
    • (2005) J Mol Catal B: Enzym , vol.35 , pp. 154-160
    • Ozyilmaz, G.1    Tukel, S.S.2    Alptekin, O.3
  • 47
    • 84861899828 scopus 로고    scopus 로고
    • Versatility of glutaraldehyde to immobilize lipases: Effect of the immobilization protocol on the properties of lipase B from Candida antarctica
    • O. Barbosa, R. Torres, C. Ortiz, and R. Fernandez-Lafuente Versatility of glutaraldehyde to immobilize lipases: effect of the immobilization protocol on the properties of lipase B from Candida antarctica Process Biochem 47 2012 1220 1227
    • (2012) Process Biochem , vol.47 , pp. 1220-1227
    • Barbosa, O.1    Torres, R.2    Ortiz, C.3    Fernandez-Lafuente, R.4
  • 48
    • 4043071644 scopus 로고
    • Cyanohydridoborate anion as a selective reducing agent
    • R.F. Borch, M.D. Bernstein, and H.D. Durst Cyanohydridoborate anion as a selective reducing agent J Am Chem Soc 93 1971 2897 2904
    • (1971) J Am Chem Soc , vol.93 , pp. 2897-2904
    • Borch, R.F.1    Bernstein, M.D.2    Durst, H.D.3
  • 49
    • 0001086044 scopus 로고
    • Enzyme-immobilization by the glutardialdehyde procedure. An investigation of the effects of reducing the Schiff-bases generated, as based on studying the immobilization of glucose oxidase to silanized controlled pore glass
    • E.H. Hansen, and H.S. Mikkelsen Enzyme-immobilization by the glutardialdehyde procedure. An investigation of the effects of reducing the Schiff-bases generated, as based on studying the immobilization of glucose oxidase to silanized controlled pore glass Anal Lett 24 1991 1419-1430
    • (1991) Anal Lett , vol.24 , pp. 1419-1430
    • Hansen, E.H.1    Mikkelsen, H.S.2
  • 50
    • 0037373781 scopus 로고    scopus 로고
    • Immobilization of glutaryl-7-aminocephalosporanic acid acylase on silica gel and enhancement of its stability
    • S.W. Park, J.W. Lee, S.I. Hong, and S.W. Kim Immobilization of glutaryl-7-aminocephalosporanic acid acylase on silica gel and enhancement of its stability Appl Biochem Biotechnol 104 2003 185 198
    • (2003) Appl Biochem Biotechnol , vol.104 , pp. 185-198
    • Park, S.W.1    Lee, J.W.2    Hong, S.I.3    Kim, S.W.4
  • 52
    • 78649321427 scopus 로고    scopus 로고
    • Immobilization and stabilization of microbial lipases by multipoint covalent attachment on aldehyde-resin affinity: Application of the biocatalysts in biodiesel synthesis
    • A.A. Mendes, R.C. Giordano, R.L.C. Giordano, and H.F. de Castro Immobilization and stabilization of microbial lipases by multipoint covalent attachment on aldehyde-resin affinity: application of the biocatalysts in biodiesel synthesis J Mol Catal B: Enzym 68 2011 109 115
    • (2011) J Mol Catal B: Enzym , vol.68 , pp. 109-115
    • Mendes, A.A.1    Giordano, R.C.2    Giordano, R.L.C.3    De Castro, H.F.4
  • 53
    • 80051704822 scopus 로고    scopus 로고
    • Multipoint covalent immobilization of lipase on chitosan hybrid hydrogels: Influence of the polyelectrolyte complex type and chemical modification on the catalytic properties of the biocatalysts
    • A.A. Mendes, H.F. de Castro, D.S. Rodrigues, W.S. Adriano, P.W. Tardioli, E.J. Mammarella, R.C. Giordano, and R.L.C. Giordano Multipoint covalent immobilization of lipase on chitosan hybrid hydrogels: influence of the polyelectrolyte complex type and chemical modification on the catalytic properties of the biocatalysts J Ind Microbiol Biotechnol 38 2011 1055 1066
    • (2011) J Ind Microbiol Biotechnol , vol.38 , pp. 1055-1066
    • Mendes, A.A.1    De Castro, H.F.2    Rodrigues, D.S.3    Adriano, W.S.4    Tardioli, P.W.5    Mammarella, E.J.6    Giordano, R.C.7    Giordano, R.L.C.8
  • 54
    • 14944385555 scopus 로고    scopus 로고
    • Lipase-catalyzed separation of the enantiomers of 1-substituted-3- arylthio-2-propanols
    • M. Wielechowska, and J. Plenkiewicz Lipase-catalyzed separation of the enantiomers of 1-substituted-3-arylthio-2-propanols Tetrahedron: Asymmetry 16 2005 1199 1205
    • (2005) Tetrahedron: Asymmetry , vol.16 , pp. 1199-1205
    • Wielechowska, M.1    Plenkiewicz, J.2
  • 55
    • 0037079654 scopus 로고    scopus 로고
    • Ethyl oleate synthesis by Porcine pancreatic lipase in organic solvents
    • S. Hazarika, P. Goswami, N.N. Dutta, and A.K. Hazarika Ethyl oleate synthesis by Porcine pancreatic lipase in organic solvents Chem Eng J 85 2002 61 68
    • (2002) Chem Eng J , vol.85 , pp. 61-68
    • Hazarika, S.1    Goswami, P.2    Dutta, N.N.3    Hazarika, A.K.4
  • 56
    • 70350564162 scopus 로고    scopus 로고
    • Enantioselective acylation of (RS)-phenylethylamine catalysed by lipases
    • C. Pilissão, P.O. Carvalho, and M.G. Nascimento Enantioselective acylation of (RS)-phenylethylamine catalysed by lipases Process Biochem 44 2009 1352 1357
    • (2009) Process Biochem , vol.44 , pp. 1352-1357
    • Pilissão, C.1    Carvalho, P.O.2    Nascimento, M.G.3
  • 57
    • 38649112936 scopus 로고    scopus 로고
    • Multipoint covalent immobilization of microbial lipase on chitosan and agarose activated by different methods
    • D.S. Rodrigues, A.A. Mendes, W.S. Adriano, L.R.B. Gonçalves, and R.L.C. Giordano Multipoint covalent immobilization of microbial lipase on chitosan and agarose activated by different methods J Mol Catal B: Enzym 51 2008 100 109
    • (2008) J Mol Catal B: Enzym , vol.51 , pp. 100-109
    • Rodrigues, D.S.1    Mendes, A.A.2    Adriano, W.S.3    Gonçalves, L.R.B.4    Giordano, R.L.C.5
  • 58
    • 38949099381 scopus 로고    scopus 로고
    • Glutaraldehyde activation of polymer Nylon-6 for lipase immobilization: Enzyme characteristics and stability
    • S. Pahujani, S.S. Kanwar, G. Chauhan, and R. Gupta Glutaraldehyde activation of polymer Nylon-6 for lipase immobilization: enzyme characteristics and stability Bioresour Technol 99 2008 2566 2570
    • (2008) Bioresour Technol , vol.99 , pp. 2566-2570
    • Pahujani, S.1    Kanwar, S.S.2    Chauhan, G.3    Gupta, R.4
  • 59
    • 84865532220 scopus 로고    scopus 로고
    • Lipase immobilization on glutaraldehyde-activated nanofibrous membranes for improved enzyme stabilities and activities
    • J. Zhu, and G. Sun Lipase immobilization on glutaraldehyde-activated nanofibrous membranes for improved enzyme stabilities and activities React Funct Polym 72 2012 839 845
    • (2012) React Funct Polym , vol.72 , pp. 839-845
    • Zhu, J.1    Sun, G.2
  • 60
    • 33751499686 scopus 로고
    • A rule to predict which enantiomer of a secondary alcohol reacts faster in reactions catalyzed by cholesterol esterase, lipase from Pseudomonas cepacia, and lipase from Candida rugosa
    • R.J. Kazlauskas, A.N.E. Weissfloch, A.T. Rappaport, and L.A. Cuccia A rule to predict which enantiomer of a secondary alcohol reacts faster in reactions catalyzed by cholesterol esterase, lipase from Pseudomonas cepacia, and lipase from Candida rugosa J Org Chem 56 1991 2656 2665
    • (1991) J Org Chem , vol.56 , pp. 2656-2665
    • Kazlauskas, R.J.1    Weissfloch, A.N.E.2    Rappaport, A.T.3    Cuccia, L.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.