메뉴 건너뛰기




Volumn 27, Issue 6, 2010, Pages 844-850

Kinetic resolution of (R/S)-propranolol (1-isopropylamino-3-(1-naphtoxy)-2-propanolol) catalyzed by immobilized preparations of Candida antarctica lipase B (CAL-B)

Author keywords

[No Author keywords available]

Indexed keywords

ACYL DONORS; CANDIDA ANTARCTICA B; CANDIDA ANTARCTICA LIPASE B; ENANTIOMERIC RATIO; ENZYME PREPARATION; IMMOBILIZED LIPASE; KINETIC RESOLUTION; PROPANOLOL; VINYL ACETATES;

EID: 78649709520     PISSN: 18716784     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nbt.2010.07.015     Document Type: Article
Times cited : (40)

References (64)
  • 1
    • 0036525716 scopus 로고    scopus 로고
    • Lipases as practical biocatalysts
    • Reetz T. Lipases as practical biocatalysts. Biocatal. Biotransform. 2002, 6:145-150.
    • (2002) Biocatal. Biotransform. , vol.6 , pp. 145-150
    • Reetz, T.1
  • 2
    • 0035843122 scopus 로고    scopus 로고
    • Enzymes for chemical synthesis
    • Koeller K.M., Wong C.H. Enzymes for chemical synthesis. Nature 2001, 409:232-240.
    • (2001) Nature , vol.409 , pp. 232-240
    • Koeller, K.M.1    Wong, C.H.2
  • 3
    • 0037206735 scopus 로고    scopus 로고
    • Enantioselective lipase-catalysed kinetic resolution of acyloxymethyl and ethoxycarbonylmethyl esters of 1,4-dihydroisonicotinic acid derivatives
    • Sobolev A., et al. Enantioselective lipase-catalysed kinetic resolution of acyloxymethyl and ethoxycarbonylmethyl esters of 1,4-dihydroisonicotinic acid derivatives. Tetrahedron: Asymmetry 2002, 13:2389-2397.
    • (2002) Tetrahedron: Asymmetry , vol.13 , pp. 2389-2397
    • Sobolev, A.1
  • 4
    • 0037158235 scopus 로고    scopus 로고
    • Pseudomonas sp. lipase immobilized in polymers versus the use of free enzyme in the resolution of (R,S)-methyl mandelate
    • Queiroz N., Nascimento M. Pseudomonas sp. lipase immobilized in polymers versus the use of free enzyme in the resolution of (R,S)-methyl mandelate. Tetrahedron Lett. 2002, 43:5225-5227.
    • (2002) Tetrahedron Lett. , vol.43 , pp. 5225-5227
    • Queiroz, N.1    Nascimento, M.2
  • 5
    • 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
    • Palomo J.M., et al. Enzymatic resolution of (±)-glycidyl butyrate in aqueous media. Strong modulation of the properties of the lipase from Rhizopus oryzae via immobilization techniques. Tetrahedron: Asymmetry 2004, 15:1157-1161.
    • (2004) Tetrahedron: Asymmetry , vol.15 , pp. 1157-1161
    • Palomo, J.M.1
  • 6
    • 0032032060 scopus 로고    scopus 로고
    • Lipase-catalysed enantioselective esterification of ibuprofen in organic solvents under controlled water activity
    • Ducret A., et al. Lipase-catalysed enantioselective esterification of ibuprofen in organic solvents under controlled water activity. Enzyme Microb. Technol. 1998, 22:212-216.
    • (1998) Enzyme Microb. Technol. , vol.22 , pp. 212-216
    • Ducret, A.1
  • 7
    • 0027588112 scopus 로고
    • Enzymes in the synthesis of chiral drugs
    • Margolin A.L. Enzymes in the synthesis of chiral drugs. Enzyme Microb. Technol. 1993, 15:266-280.
    • (1993) Enzyme Microb. Technol. , vol.15 , pp. 266-280
    • Margolin, A.L.1
  • 8
    • 0034804537 scopus 로고    scopus 로고
    • A practical enzymatic method for preparation of (S)-ketoprofen with a crude Candida rugosa lipase
    • Wu H.Y., et al. A practical enzymatic method for preparation of (S)-ketoprofen with a crude Candida rugosa lipase. Synth. Commun. 2001, 31:3491-3496.
    • (2001) Synth. Commun. , vol.31 , pp. 3491-3496
    • Wu, H.Y.1
  • 9
    • 0025057072 scopus 로고
    • A serine protease triad forms the catalytic center of a triacylglycerol lipase
    • Brady L., et al. A serine protease triad forms the catalytic center of a triacylglycerol lipase. Nature 1990, 343:767-770.
    • (1990) Nature , vol.343 , pp. 767-770
    • Brady, L.1
  • 10
    • 0026418174 scopus 로고
    • A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex
    • Brzozowski A.M., et al. A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. Nature 1991, 351:491-494.
    • (1991) Nature , vol.351 , pp. 491-494
    • Brzozowski, A.M.1
  • 11
    • 0026550733 scopus 로고
    • Catalysis at the interface: the anatomy of conformational change in a triglyceride lipase
    • Derewenda U., et al. Catalysis at the interface: the anatomy of conformational change in a triglyceride lipase. Biochemistry 1992, 31:1532-1541.
    • (1992) Biochemistry , vol.31 , pp. 1532-1541
    • Derewenda, U.1
  • 12
    • 0032104742 scopus 로고    scopus 로고
    • Immobilization of lipases by selective adsorption on hydrophobic supports
    • Fernández-Lafuente R., et al. Immobilization of lipases by selective adsorption on hydrophobic supports. Chem. Phys. Lipids 1998, 93:185-197.
    • (1998) Chem. Phys. Lipids , vol.93 , pp. 185-197
    • Fernández-Lafuente, R.1
  • 13
    • 13844256708 scopus 로고    scopus 로고
    • Synthesis of enantiomerically pure glycidol via a fully enantioselective lipase-catalyzed resolution
    • Palomo J.M., et al. Synthesis of enantiomerically pure glycidol via a fully enantioselective lipase-catalyzed resolution. Tetrahedron: Asymmetry 2005, 16:869-874.
    • (2005) Tetrahedron: Asymmetry , vol.16 , pp. 869-874
    • Palomo, J.M.1
  • 14
    • 0037025268 scopus 로고    scopus 로고
    • Modulation of the enantioselectivity of Candida antarctica B lipase via conformational engineering: kinetic resolution of (±)-hydroxy-phenylacetic acid derivatives
    • Palomo J.M., et al. Modulation of the enantioselectivity of Candida antarctica B lipase via conformational engineering: kinetic resolution of (±)-hydroxy-phenylacetic acid derivatives. Tetrahedron: Asymmetry 2002, 13:1337-1345.
    • (2002) Tetrahedron: Asymmetry , vol.13 , pp. 1337-1345
    • Palomo, J.M.1
  • 15
    • 34547162510 scopus 로고    scopus 로고
    • Modulation of immobilized lipase enantioselectivity via chemical amination
    • Palomo J.M., et al. Modulation of immobilized lipase enantioselectivity via chemical amination. Adv. Synth. Catal. 2007, 349:1119-1127.
    • (2007) Adv. Synth. Catal. , vol.349 , pp. 1119-1127
    • Palomo, J.M.1
  • 16
    • 33646502629 scopus 로고    scopus 로고
    • Improvement of the enantioselectivity of lipase (fraction B) from Candida antarctica via adsorption on polyethylenimine-agarose under different experimental conditions
    • Torres R., et al. Improvement of the enantioselectivity of lipase (fraction B) from Candida antarctica via adsorption on polyethylenimine-agarose under different experimental conditions. Enzyme Microb. Technol. 2006, 39:167-171.
    • (2006) Enzyme Microb. Technol. , vol.39 , pp. 167-171
    • Torres, R.1
  • 17
    • 0024029957 scopus 로고
    • Aldehyde gels as activated support for immobilization stabilization of enzymes
    • Guisan J.M. Aldehyde gels as activated support for immobilization stabilization of enzymes. Enzyme Microb. Technol. 1988, 10:375-382.
    • (1988) Enzyme Microb. Technol. , vol.10 , pp. 375-382
    • Guisan, J.M.1
  • 18
    • 0026417558 scopus 로고
    • Immobilization-stabilization of chymotrypsin by covalent attachment to aldehyde agarose gels
    • Guisan J.M., et al. Immobilization-stabilization of chymotrypsin by covalent attachment to aldehyde agarose gels. Biotechnol. Bioeng. 1991, 39:75-84.
    • (1991) Biotechnol. Bioeng. , vol.39 , pp. 75-84
    • Guisan, J.M.1
  • 19
    • 0024675074 scopus 로고
    • Immobilization-stabilization of enzymes. Variables that control the intensity of the trypsin (amine)-agarose (aldehyde) multi-point covalent attachment
    • Blanco R.M., et al. Immobilization-stabilization of enzymes. Variables that control the intensity of the trypsin (amine)-agarose (aldehyde) multi-point covalent attachment. Enzyme Microb. Technol. 1988, 11:353-359.
    • (1988) Enzyme Microb. Technol. , vol.11 , pp. 353-359
    • Blanco, R.M.1
  • 20
    • 1242315536 scopus 로고    scopus 로고
    • Chemoenzymatic dynamic kinetic resolution
    • Pámies O., Backvall J. Chemoenzymatic dynamic kinetic resolution. Trends Biotechnol. 2004, 22:130-135.
    • (2004) Trends Biotechnol. , vol.22 , pp. 130-135
    • Pámies, O.1    Backvall, J.2
  • 21
    • 0037054396 scopus 로고    scopus 로고
    • Enzymatic resolution of the chiral inductor 2-methoxy-2-phenylethanol
    • Monterde M., et al. Enzymatic resolution of the chiral inductor 2-methoxy-2-phenylethanol. Tetrahedron: Asymmetry 2002, 13:1091-1096.
    • (2002) Tetrahedron: Asymmetry , vol.13 , pp. 1091-1096
    • Monterde, M.1
  • 22
    • 27144487754 scopus 로고    scopus 로고
    • Resolution of (±)-menthol by immobilized Candida rugosa lipase on superparamagnetic nanoparticles
    • Bai S., et al. Resolution of (±)-menthol by immobilized Candida rugosa lipase on superparamagnetic nanoparticles. Food Chem. 2005, 96:1-7.
    • (2005) Food Chem. , vol.96 , pp. 1-7
    • Bai, S.1
  • 23
    • 0035831162 scopus 로고    scopus 로고
    • A highly chemo and stereoselective synthesis of B-keto esters via a polymer-supported lipase catalyzed transesterification
    • Córdova A., Janda K.D. A highly chemo and stereoselective synthesis of B-keto esters via a polymer-supported lipase catalyzed transesterification. J. Org. Chem. 2001, 66:1906-1909.
    • (2001) J. Org. Chem. , vol.66 , pp. 1906-1909
    • Córdova, A.1    Janda, K.D.2
  • 24
    • 27744576870 scopus 로고    scopus 로고
    • Increased racemate resolution of propranolol esters by lipase immobilized catalysis
    • Avila R., et al. Increased racemate resolution of propranolol esters by lipase immobilized catalysis. Latin Am. Appl. Res. 2005, 35:307-311.
    • (2005) Latin Am. Appl. Res. , vol.35 , pp. 307-311
    • Avila, R.1
  • 26
    • 0022344552 scopus 로고
    • Cardio beta-adrenoceptor blockade: the guest for selectivity
    • Barret A.M. Cardio beta-adrenoceptor blockade: the guest for selectivity. J. Pharm. 1985, 2:95-108.
    • (1985) J. Pharm. , vol.2 , pp. 95-108
    • Barret, A.M.1
  • 27
    • 78649718698 scopus 로고
    • Additional features of beta-blockers
    • Eber O., et al. Additional features of beta-blockers. Clin. Endocrinol. 1990, 32:363-370.
    • (1990) Clin. Endocrinol. , vol.32 , pp. 363-370
    • Eber, O.1
  • 28
    • 0018651305 scopus 로고
    • Resolution of (±)-propranolol
    • Yost Y., Holtzman J.L. Resolution of (±)-propranolol. J. Pharm. Sci. 1979, 16:1181-1182.
    • (1979) J. Pharm. Sci. , vol.16 , pp. 1181-1182
    • Yost, Y.1    Holtzman, J.L.2
  • 29
    • 0019196959 scopus 로고
    • Stereospecific assay for (-) and (+)-propranolol in human and dog plasma
    • Silber B., Riegelman S. Stereospecific assay for (-) and (+)-propranolol in human and dog plasma. Pharmacol. Exp. Ther. 1980, 215:643-648.
    • (1980) Pharmacol. Exp. Ther. , vol.215 , pp. 643-648
    • Silber, B.1    Riegelman, S.2
  • 30
    • 0022394750 scopus 로고
    • Preparation of optically active 1-acetoxy-2-aryloxypropionitriles and its application to a facile synthesis of (S)-(-)-(+)-propranolol
    • Matsuo N., Ohno H. Preparation of optically active 1-acetoxy-2-aryloxypropionitriles and its application to a facile synthesis of (S)-(-)-(+)-propranolol. Tetrahedron Lett. 1985, 26:5533-5534.
    • (1985) Tetrahedron Lett. , vol.26 , pp. 5533-5534
    • Matsuo, N.1    Ohno, H.2
  • 31
    • 0023716150 scopus 로고
    • Highly efficient lipase-catalyzed asymmetric synthesis of chiral glycerol derivatives leading to practical synthesis of S-propranolol
    • Terao Y., et al. Highly efficient lipase-catalyzed asymmetric synthesis of chiral glycerol derivatives leading to practical synthesis of S-propranolol. Tetrahedron Lett. 1988, 29:5173-5176.
    • (1988) Tetrahedron Lett. , vol.29 , pp. 5173-5176
    • Terao, Y.1
  • 32
    • 33646867639 scopus 로고    scopus 로고
    • Lipases: useful biocatalysts for the preparation of pharmaceuticals
    • Gotor-Fernández V., et al. Lipases: useful biocatalysts for the preparation of pharmaceuticals. J. Mol. Catal. B: Enzym. 2006, 40:111-120.
    • (2006) J. Mol. Catal. B: Enzym. , vol.40 , pp. 111-120
    • Gotor-Fernández, V.1
  • 33
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents
    • Klibanov A.M. Improving enzymes by using them in organic solvents. Nature 2001, 409:241-246.
    • (2001) Nature , vol.409 , pp. 241-246
    • Klibanov, A.M.1
  • 34
    • 63249106284 scopus 로고    scopus 로고
    • Optimization of (R,S)-1-phenylethanol kinetic resolution over Candida antarctica lipase B in ionic liquids
    • Habulin M., Knez Z. Optimization of (R,S)-1-phenylethanol kinetic resolution over Candida antarctica lipase B in ionic liquids. J. Mol. Catal. B: Enzym. 2009, 58:24-28.
    • (2009) J. Mol. Catal. B: Enzym. , vol.58 , pp. 24-28
    • Habulin, M.1    Knez, Z.2
  • 35
    • 14944385555 scopus 로고    scopus 로고
    • Lipase-catalyzed separation of the enantiomers of 1-substituted-3-arylthio-2-propanols
    • Wielechowska M., Plenkiewicz J. Lipase-catalyzed separation of the enantiomers of 1-substituted-3-arylthio-2-propanols. Tetrahedron: Asymmetry 2005, 16:1199-1205.
    • (2005) Tetrahedron: Asymmetry , vol.16 , pp. 1199-1205
    • Wielechowska, M.1    Plenkiewicz, J.2
  • 36
    • 13844265823 scopus 로고    scopus 로고
    • Immobilization does not influence the enantioselectivity of CAL-B catalyzed kinetic resolution of secondary alcohols
    • Jacobsen E., et al. Immobilization does not influence the enantioselectivity of CAL-B catalyzed kinetic resolution of secondary alcohols. Tetrahedron: Asymmetry 2005, 16:847-850.
    • (2005) Tetrahedron: Asymmetry , vol.16 , pp. 847-850
    • Jacobsen, E.1
  • 37
    • 0037116425 scopus 로고    scopus 로고
    • Factors affecting the resolution of dl-menthol by immobilized lipase catalyzed esterification in organic solvent
    • Wang L., et al. Factors affecting the resolution of dl-menthol by immobilized lipase catalyzed esterification in organic solvent. J. Agric. Food Chem. 2002, 50:262-265.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 262-265
    • Wang, L.1
  • 38
    • 0025848460 scopus 로고
    • Practical chemoenzymatic synthesis of both enantiomers of propranolol
    • Bevinakatti H.S., Banerji A.A. Practical chemoenzymatic synthesis of both enantiomers of propranolol. J. Org. Chem. 1991, 56:5372-5375.
    • (1991) J. Org. Chem. , vol.56 , pp. 5372-5375
    • Bevinakatti, H.S.1    Banerji, A.A.2
  • 39
    • 0019276840 scopus 로고
    • Simultaneous determination of d- and l-propranolol in human plasma by high-performance liquid chromatography
    • Hermansson J., Von Bahr C. Simultaneous determination of d- and l-propranolol in human plasma by high-performance liquid chromatography. J. Chromatogr. 1980, 221:109-117.
    • (1980) J. Chromatogr. , vol.221 , pp. 109-117
    • Hermansson, J.1    Von Bahr, C.2
  • 40
    • 0020056110 scopus 로고
    • Separation and quantification of (R)- and (S)-propranolol as their diastereomeric derivatives in human plasma by reversed-phase ion-pair chromatography
    • Hermansson J. Separation and quantification of (R)- and (S)-propranolol as their diastereomeric derivatives in human plasma by reversed-phase ion-pair chromatography. Acta Pharm. Suec. 1982, 19:11-24.
    • (1982) Acta Pharm. Suec. , vol.19 , pp. 11-24
    • Hermansson, J.1
  • 41
    • 0019964117 scopus 로고
    • Procedure for the chiral derivatization and chromatographic resolution of R-(+)- and S-(-)-propranolol
    • Thompson J.A., et al. Procedure for the chiral derivatization and chromatographic resolution of R-(+)- and S-(-)-propranolol. J. Chromatogr. 1982, 238:470-475.
    • (1982) J. Chromatogr. , vol.238 , pp. 470-475
    • Thompson, J.A.1
  • 42
    • 0034575018 scopus 로고    scopus 로고
    • Multifunctional epoxy supports: a new tool to improve the covalent immobilization of proteins. The promotion of physical adsorptions of proteins on the supports before their covalent linkage
    • Mateo C., et al. Multifunctional epoxy supports: a new tool to improve the covalent immobilization of proteins. The promotion of physical adsorptions of proteins on the supports before their covalent linkage. Biomacromolecules 2000, 1:739-745.
    • (2000) Biomacromolecules , vol.1 , pp. 739-745
    • Mateo, C.1
  • 44
    • 0032506270 scopus 로고    scopus 로고
    • Interfacial affinity chromatography of lipases: separation of different fractions by selective adsorption on supports activated with hydrophobics groups
    • Sabuquillo P., et al. Interfacial affinity chromatography of lipases: separation of different fractions by selective adsorption on supports activated with hydrophobics groups. Biochim. Biophys. Acta 1998, 1388:337-348.
    • (1998) Biochim. Biophys. Acta , vol.1388 , pp. 337-348
    • Sabuquillo, P.1
  • 45
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 46
    • 33845282987 scopus 로고
    • Enzymatic resolution coupled with substrate racemization using a thioester substrate
    • Chen C.-S., et al. Enzymatic resolution coupled with substrate racemization using a thioester substrate. J. Am. Chem. Soc. 1987, 109:2812-2817.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 2812-2817
    • Chen, C.-S.1
  • 47
    • 0032486523 scopus 로고    scopus 로고
    • A single step purification, immobilization, and hyperactivation of lipases via interfacial adsorption on strongly hydrophobic supports
    • Bastida A., et al. A single step purification, immobilization, and hyperactivation of lipases via interfacial adsorption on strongly hydrophobic supports. Biotechnol. Bioeng. 1998, 58:486-493.
    • (1998) Biotechnol. Bioeng. , vol.58 , pp. 486-493
    • Bastida, A.1
  • 48
    • 0034607269 scopus 로고    scopus 로고
    • Reversible enzyme immobilization via a very strong and non-distorting adsorption on support-polyethyleneimine composites
    • Mateo C., et al. Reversible enzyme immobilization via a very strong and non-distorting adsorption on support-polyethyleneimine composites. Biotechnol. Bioeng. 2000, 68:98-105.
    • (2000) Biotechnol. Bioeng. , vol.68 , pp. 98-105
    • Mateo, C.1
  • 49
    • 0034647968 scopus 로고    scopus 로고
    • Resolution of racemic 1-azido-3-aryloxy-2-propanols by lipase-catalyzed enantioselective acetylation
    • Pchelka B., et al. Resolution of racemic 1-azido-3-aryloxy-2-propanols by lipase-catalyzed enantioselective acetylation. Tetrahedron: Asymmetry 2000, 11:2719-2732.
    • (2000) Tetrahedron: Asymmetry , vol.11 , pp. 2719-2732
    • Pchelka, B.1
  • 50
    • 0343657238 scopus 로고    scopus 로고
    • 1α,25-Dihydroxyvitamin D3 A-ring precursors: studies on regioselective enzymatic alkoxycarbonylation reactions of their stereoisomers. chemoenzymatic synthesis of A-ring synthon carbamate derivatives, including carbazates and polyamino carbamates
    • Gotor F., et al. 1α,25-Dihydroxyvitamin D3 A-ring precursors: studies on regioselective enzymatic alkoxycarbonylation reactions of their stereoisomers. chemoenzymatic synthesis of A-ring synthon carbamate derivatives, including carbazates and polyamino carbamates. J. Org. Chem. 1999, 64:7504-7510.
    • (1999) J. Org. Chem. , vol.64 , pp. 7504-7510
    • Gotor, F.1
  • 51
    • 0032572886 scopus 로고    scopus 로고
    • Lipase-catalyzed kinetic resolution of large secondary alcohols having tetraphenylporphyrin
    • Ema T., et al. Lipase-catalyzed kinetic resolution of large secondary alcohols having tetraphenylporphyrin. Tetrahedron Lett. 1998, 39:6311-6314.
    • (1998) Tetrahedron Lett. , vol.39 , pp. 6311-6314
    • Ema, T.1
  • 52
    • 34249281639 scopus 로고    scopus 로고
    • A lipase-catalysed resolution of N-(3-cyano-2-hydroxy propan-1-yl)phthalimide: synthesis of (R)-GABOB and (R)-carnitine
    • Kamal A., et al. A lipase-catalysed resolution of N-(3-cyano-2-hydroxy propan-1-yl)phthalimide: synthesis of (R)-GABOB and (R)-carnitine. J. Mol. Catal. B: Enzym. 2007, 47:1.
    • (2007) J. Mol. Catal. B: Enzym. , vol.47 , pp. 1
    • Kamal, A.1
  • 53
    • 34249287914 scopus 로고    scopus 로고
    • Enzymatic kinetic resolution of racemic 4-tetrahydropyranols by Candida rugosa lipase
    • Yadav J., et al. Enzymatic kinetic resolution of racemic 4-tetrahydropyranols by Candida rugosa lipase. Tetrahedron Lett. 2007, 48:4631-4633.
    • (2007) Tetrahedron Lett. , vol.48 , pp. 4631-4633
    • Yadav, J.1
  • 54
    • 34250024347 scopus 로고    scopus 로고
    • Enzymatic resolution of α-tetralols by CALB-catalyzed acetylation
    • Ferraz H., et al. Enzymatic resolution of α-tetralols by CALB-catalyzed acetylation. Tetrahedron: Asymmetry 2007, 18:1070-1076.
    • (2007) Tetrahedron: Asymmetry , vol.18 , pp. 1070-1076
    • Ferraz, H.1
  • 55
    • 0346199337 scopus 로고    scopus 로고
    • Enantioselective acylation of chiral amines catalysed by serine hydrolases
    • Van Rantwijk F., Sheldon R.A. Enantioselective acylation of chiral amines catalysed by serine hydrolases. Tetrahedron 2004, 60:501-519.
    • (2004) Tetrahedron , vol.60 , pp. 501-519
    • Van Rantwijk, F.1    Sheldon, R.A.2
  • 56
    • 33947602594 scopus 로고    scopus 로고
    • Improvement of enzyme activity, stability and selectivity via immobilization techniques
    • Mateo C., et al. Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzyme Microb. Technol. 2007, 40:1451-1463.
    • (2007) Enzyme Microb. Technol. , vol.40 , pp. 1451-1463
    • Mateo, C.1
  • 57
    • 16244405562 scopus 로고    scopus 로고
    • Immobilized enzymes: science or art?
    • Cao L. Immobilized enzymes: science or art?. Curr. Opin. Chem. Biol. 2005, 9:217-226.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 217-226
    • Cao, L.1
  • 58
    • 67349248070 scopus 로고    scopus 로고
    • The co-operative effect of physical and covalent protein adsorption on heterofunctional supports
    • Bolivar J., et al. The co-operative effect of physical and covalent protein adsorption on heterofunctional supports. Process Biochem. 2009, 44:757-763.
    • (2009) Process Biochem. , vol.44 , pp. 757-763
    • Bolivar, J.1
  • 59
    • 4644350558 scopus 로고    scopus 로고
    • Rational strategies for highly enantioselective lipase-catalyzed kinetic resolutions of very bulky chiral compounds: substrate design and high-temperature biocatalysis
    • Ema T. Rational strategies for highly enantioselective lipase-catalyzed kinetic resolutions of very bulky chiral compounds: substrate design and high-temperature biocatalysis. Tetrahedron: Asymmetry 2004, 15:2765-2770.
    • (2004) Tetrahedron: Asymmetry , vol.15 , pp. 2765-2770
    • Ema, T.1
  • 60
    • 0027160452 scopus 로고
    • Insights into interfacial activation from an open structure of Candida rugosa lipase
    • Grochulski P., et al. Insights into interfacial activation from an open structure of Candida rugosa lipase. J. Biol. Chem. 1993, 268:12843-12847.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12843-12847
    • Grochulski, P.1
  • 61
    • 0035496145 scopus 로고    scopus 로고
    • Improved enantioselectivity of a lipase by rational protein engineering
    • Rotticci D., et al. Improved enantioselectivity of a lipase by rational protein engineering. Chembiochem 2001, 2:766-770.
    • (2001) Chembiochem , vol.2 , pp. 766-770
    • Rotticci, D.1
  • 62
    • 0032530607 scopus 로고    scopus 로고
    • Reversed enantiopreference of Candida rugosa lipase supports different modes of binding enantiomers of a chiral acyl donor
    • Berglund P., et al. Reversed enantiopreference of Candida rugosa lipase supports different modes of binding enantiomers of a chiral acyl donor. J. Mol. Catal. B: Enzym. 1998, 5:283-287.
    • (1998) J. Mol. Catal. B: Enzym. , vol.5 , pp. 283-287
    • Berglund, P.1
  • 63
    • 0032826753 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of (R)- and (S)-atenolol and propranolol employing lipase catalyzed enantioselective esterification and hydrolysis
    • Darnle S., et al. Chemoenzymatic synthesis of (R)- and (S)-atenolol and propranolol employing lipase catalyzed enantioselective esterification and hydrolysis. Synth. Commun. 1999, 29:3855-3862.
    • (1999) Synth. Commun. , vol.29 , pp. 3855-3862
    • Darnle, S.1
  • 64
    • 31844447220 scopus 로고    scopus 로고
    • Lipase-catalyzed preparation of S-propranolol in presence of hydroxypropyl β-cyclodextrins
    • Ávila-González R., et al. Lipase-catalyzed preparation of S-propranolol in presence of hydroxypropyl β-cyclodextrins. J. Biosci. Bioeng. 2005, 100:423-428.
    • (2005) J. Biosci. Bioeng. , vol.100 , pp. 423-428
    • Ávila-González, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.