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Volumn 102, Issue 2, 2011, Pages 499-506

Immobilization of Candida rugosa lipase on glass beads for enantioselective hydrolysis of racemic Naproxen methyl ester

Author keywords

Candida rugosa lipase; Enantioselective hydrolysis; Glass beads; Immobilization; S Naproxen

Indexed keywords

CANDIDA RUGOSA LIPASE; ENANTIOSELECTIVE HYDROLYSIS; GLASS BEADS; IMMOBILIZATION; S-NAPROXEN;

EID: 78650707084     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2010.08.083     Document Type: Article
Times cited : (91)

References (35)
  • 1
    • 33847402546 scopus 로고    scopus 로고
    • Characterization of an anion-exchange porous polypropylene hollow fiber membrane for immobilization of ABL lipase
    • Abrol K., Qazi G.N., Ghos A.K. Characterization of an anion-exchange porous polypropylene hollow fiber membrane for immobilization of ABL lipase. J. Biotechnol. 2007, 128:838-848.
    • (2007) J. Biotechnol. , vol.128 , pp. 838-848
    • Abrol, K.1    Qazi, G.N.2    Ghos, A.K.3
  • 2
    • 33751158445 scopus 로고
    • Enzymes and other proteins entrapped in sol-gel materials
    • Avnir D., Braun S., Lev O., Ottolenghi M. Enzymes and other proteins entrapped in sol-gel materials. Chem. Mater. 1994, 6:1605-1614.
    • (1994) Chem. Mater. , vol.6 , pp. 1605-1614
    • Avnir, D.1    Braun, S.2    Lev, O.3    Ottolenghi, M.4
  • 4
    • 40849142018 scopus 로고    scopus 로고
    • Lipase enzyme immobilization on synthetic beaded macroporous copolymers for kinetic resolution of chiral drugs intermediates
    • Bhushan I., Parshad R., Qazi G.N., Ingavle G., Rajan C.R., Ponrathnam S., Gupta V.K. Lipase enzyme immobilization on synthetic beaded macroporous copolymers for kinetic resolution of chiral drugs intermediates. Process. Biochem. 2008, 43:321-330.
    • (2008) Process. Biochem. , vol.43 , pp. 321-330
    • Bhushan, I.1    Parshad, R.2    Qazi, G.N.3    Ingavle, G.4    Rajan, C.R.5    Ponrathnam, S.6    Gupta, V.K.7
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation 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.M.1
  • 7
    • 33747799719 scopus 로고    scopus 로고
    • Enantioselectivity modulation through immobilization of Arthrobacter sp. lipase: kinetic resolution of fluoxetine intermediate
    • Chaubey A., Parshad R., Koul S., Taneja S.C., Qazi G.N. Enantioselectivity modulation through immobilization of Arthrobacter sp. lipase: kinetic resolution of fluoxetine intermediate. J. Mol. Catal.: B Enzym. 2006, 42:39-44.
    • (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
  • 8
    • 20644469267 scopus 로고
    • Quantitative analyses of biochemical kinetic resolutions of enantiomers
    • Chen C.S., Fujimoto Y., Girdaukas G., Sih C.J. Quantitative analyses of biochemical kinetic resolutions of enantiomers. J. Am. Chem. Soc. 1982, 104:7294-7299.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 7294-7299
    • Chen, C.S.1    Fujimoto, Y.2    Girdaukas, G.3    Sih, C.J.4
  • 9
    • 0142258126 scopus 로고    scopus 로고
    • Immobilization of Candida rugosa lipase on chitosan with activation of the hydroxyl groups
    • Chiou S.H., Wu W.T. Immobilization of Candida rugosa lipase on chitosan with activation of the hydroxyl groups. Biomaterials 2004, 25:197-204.
    • (2004) Biomaterials , vol.25 , pp. 197-204
    • Chiou, S.H.1    Wu, W.T.2
  • 10
    • 0027138526 scopus 로고
    • Selectivity-enhancement of hydrolase reactions
    • Faber K., Ottolina G., Riva S. Selectivity-enhancement of hydrolase reactions. Biocatalysis 1993, 8:91-132.
    • (1993) Biocatalysis , vol.8 , pp. 91-132
    • Faber, K.1    Ottolina, G.2    Riva, S.3
  • 13
    • 0038039289 scopus 로고    scopus 로고
    • Direct binding and characterization of lipase onto magnetic nanoparticles
    • Hung S.H., Liao M.H., Chen D.H. Direct binding and characterization of lipase onto magnetic nanoparticles. Biotechnol. Progr. 2003, 19:1095-1100.
    • (2003) Biotechnol. Progr. , vol.19 , pp. 1095-1100
    • Hung, S.H.1    Liao, M.H.2    Chen, D.H.3
  • 15
    • 0035085171 scopus 로고    scopus 로고
    • Purification and characterisation of an ester hydrolase from a strain of Arthrobacter species: its application in asymmetrisation of 2-benzyl-1,3-propanediol acylates
    • Johri S., Verma V., Parshad R., Koul S., Taneja S.C., Qazi G.N. Purification and characterisation of an ester hydrolase from a strain of Arthrobacter species: its application in asymmetrisation of 2-benzyl-1,3-propanediol acylates. Bioorg. Med. Chem. 2001, 9:269-273.
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 269-273
    • Johri, S.1    Verma, V.2    Parshad, R.3    Koul, S.4    Taneja, S.C.5    Qazi, G.N.6
  • 16
    • 34249049259 scopus 로고    scopus 로고
    • α-Amylase immobilization on functionalized glass beads by covalent attachment
    • Kahraman M.V., Bayramoglu G., Kayaman-Apohan N., Gungor A. α-Amylase immobilization on functionalized glass beads by covalent attachment. Food Chem. 2007, 104:1385-1392.
    • (2007) Food Chem. , vol.104 , pp. 1385-1392
    • Kahraman, M.V.1    Bayramoglu, G.2    Kayaman-Apohan, N.3    Gungor, A.4
  • 17
    • 34447102668 scopus 로고    scopus 로고
    • Electrospun polyacrylonitrile nanofibrous membranes for lipase immobilization
    • Li S.F., Chen J.P., Wu W.T. Electrospun polyacrylonitrile nanofibrous membranes for lipase immobilization. J. Mol. Catal.: B Enzym. 2007, 47:117-124.
    • (2007) J. Mol. Catal.: B Enzym. , vol.47 , pp. 117-124
    • Li, S.F.1    Chen, J.P.2    Wu, W.T.3
  • 20
    • 0035988098 scopus 로고    scopus 로고
    • Sepabeads: a novel epoxysupport for stabilization of industrial enzyme via very intense multipoint covalent attachment
    • Mateo C., Abian O., Fernandez-Lorente G., Pedroche J., Fernandez-Lafuente R., Guisan J.M. Sepabeads: a novel epoxysupport for stabilization of industrial enzyme via very intense multipoint covalent attachment. Biotechnol. Progr. 2002, 18:629-634.
    • (2002) Biotechnol. Progr. , vol.18 , pp. 629-634
    • Mateo, C.1    Abian, O.2    Fernandez-Lorente, G.3    Pedroche, J.4    Fernandez-Lafuente, R.5    Guisan, J.M.6
  • 23
    • 8444230519 scopus 로고    scopus 로고
    • Glutaraldehyde: behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking
    • Migneault I. Glutaraldehyde: behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking. Biotechniques 2004, 37:790-802.
    • (2004) Biotechniques , vol.37 , pp. 790-802
    • Migneault, I.1
  • 24
    • 67651022185 scopus 로고    scopus 로고
    • Synthesis and characterization of cyclodextrin-based polymers as a support for immobilization of Candida rugosa lipase
    • Ozmen E.Y., Sezgin M., Yilmaz M. Synthesis and characterization of cyclodextrin-based polymers as a support for immobilization of Candida rugosa lipase. J. Mol. Catal.: B Enzym. 2009, 57:109-114.
    • (2009) J. Mol. Catal.: B Enzym. , vol.57 , pp. 109-114
    • Ozmen, E.Y.1    Sezgin, M.2    Yilmaz, M.3
  • 25
    • 70349251213 scopus 로고    scopus 로고
    • Surface modification of glass beads with glutaraldehyde: characterization and their adsorption property for metal ions
    • Ozmen M., Can K., Akin I., Arslan G., Tor A., Cengeloglu Y., Ersoz M. Surface modification of glass beads with glutaraldehyde: characterization and their adsorption property for metal ions. J. Hazard. Mater. 2009, 171:594-600.
    • (2009) J. Hazard. Mater. , vol.171 , pp. 594-600
    • Ozmen, M.1    Can, K.2    Akin, I.3    Arslan, G.4    Tor, A.5    Cengeloglu, Y.6    Ersoz, M.7
  • 26
    • 0035022098 scopus 로고    scopus 로고
    • Kinetic studies of lipase from Candida rugosa: a comparative study of the free and the immobilized enzyme on porous chitosan beads
    • Pereira E.B., Castro H.F., Moraes F.F., Zanin G.M. Kinetic studies of lipase from Candida rugosa: a comparative study of the free and the immobilized enzyme on porous chitosan beads. Appl. Biochem. Biotechnol. 2001, 91:739-752.
    • (2001) Appl. Biochem. Biotechnol. , vol.91 , pp. 739-752
    • Pereira, E.B.1    Castro, H.F.2    Moraes, F.F.3    Zanin, G.M.4
  • 27
    • 0041687879 scopus 로고    scopus 로고
    • Second generation sol-gel encapsulated lipases: robust heterogeneous biocatalysts
    • Reetz M.T., Tielmann P., Wisenhofer W., Konen W., Zonta A. Second generation sol-gel encapsulated lipases: robust heterogeneous biocatalysts. Adv. Synth. Catal. 2003, 345:717-728.
    • (2003) Adv. Synth. Catal. , vol.345 , pp. 717-728
    • Reetz, M.T.1    Tielmann, P.2    Wisenhofer, W.3    Konen, W.4    Zonta, A.5
  • 28
    • 74249093631 scopus 로고    scopus 로고
    • Enantioselective hydrolysis of (R/S)-Naproxen methyl ester with sol-gel encapsulated lipase in presence of calix[n]arene derivatives
    • Sahin O., Erdemir S., Uyanik A., Yilmaz M. Enantioselective hydrolysis of (R/S)-Naproxen methyl ester with sol-gel encapsulated lipase in presence of calix[n]arene derivatives. Appl. Catal. A-Gen. 2009, 369:36-41.
    • (2009) Appl. Catal. A-Gen. , vol.369 , pp. 36-41
    • Sahin, O.1    Erdemir, S.2    Uyanik, A.3    Yilmaz, M.4
  • 29
    • 34247859134 scopus 로고    scopus 로고
    • Impressive effect of immobilization conditions on the catalytic activity and enantioselectivity of Candida rugosa lipase toward S-Naproxen production
    • Takac S., Bakkal M. Impressive effect of immobilization conditions on the catalytic activity and enantioselectivity of Candida rugosa lipase toward S-Naproxen production. Process. Biochem. 2007, 42:1021-1027.
    • (2007) Process. Biochem. , vol.42 , pp. 1021-1027
    • Takac, S.1    Bakkal, M.2
  • 30
    • 33747757680 scopus 로고    scopus 로고
    • Implication of substrate-assisted catalysis on improving lipase activity or enantioselectivity in organic solvents
    • Tsai S.W., Chen C.C., Yang H.S., Ng I.S., Chen T.L. Implication of substrate-assisted catalysis on improving lipase activity or enantioselectivity in organic solvents. BBA - Proteins Proteom. 2006, 1764:1424-1428.
    • (2006) BBA - Proteins Proteom. , vol.1764 , pp. 1424-1428
    • Tsai, S.W.1    Chen, C.C.2    Yang, H.S.3    Ng, I.S.4    Chen, T.L.5
  • 31
    • 0034697072 scopus 로고    scopus 로고
    • Customizing lipases for biocatalysis: a survey of chemical, physical and molecular biological approaches
    • Villeneuve P., Muderhwa J.M., Graille J.M., Haas M.J. Customizing lipases for biocatalysis: a survey of chemical, physical and molecular biological approaches. J. Mol. Catal. B Enzym. 2000, 9:113-148.
    • (2000) J. Mol. Catal. B Enzym. , vol.9 , pp. 113-148
    • Villeneuve, P.1    Muderhwa, J.M.2    Graille, J.M.3    Haas, M.J.4
  • 32
    • 0014697588 scopus 로고
    • Trypsin and papain covalently coupling to porous glass
    • Weetal H.H. Trypsin and papain covalently coupling to porous glass. Science 1969, 166:615-617.
    • (1969) Science , vol.166 , pp. 615-617
    • Weetal, H.H.1
  • 33
    • 0034135667 scopus 로고    scopus 로고
    • Influence of alcohol concentration on lipase-catalyzed enantioselective esterification of racemic Naproxen in isooctane: under controlled water activity
    • Wu J.Y., Liu S.W. Influence of alcohol concentration on lipase-catalyzed enantioselective esterification of racemic Naproxen in isooctane: under controlled water activity. Enzym. Microbiol. Technol. 2000, 26:124-130.
    • (2000) Enzym. Microbiol. Technol. , vol.26 , pp. 124-130
    • Wu, J.Y.1    Liu, S.W.2
  • 34
    • 70350776734 scopus 로고    scopus 로고
    • Immobilized copper-ion affinity adsorbent based on a cross-linked β-cyclodextrin polymer for adsorption of Candida rugosa lipase
    • Yilmaz E., Sezgin M., Yilmaz M. Immobilized copper-ion affinity adsorbent based on a cross-linked β-cyclodextrin polymer for adsorption of Candida rugosa lipase. Biocatal. Biotransform. 2009, 27:360-366.
    • (2009) Biocatal. Biotransform. , vol.27 , pp. 360-366
    • Yilmaz, E.1    Sezgin, M.2    Yilmaz, M.3
  • 35
    • 71249149228 scopus 로고    scopus 로고
    • Enantioselective hydrolysis of rasemic Naproxen methyl ester with sol-gel encapsulated lipase in the presence of sporopollenin
    • Yilmaz E., Sezgin M., Yilmaz M. Enantioselective hydrolysis of rasemic Naproxen methyl ester with sol-gel encapsulated lipase in the presence of sporopollenin. J. Mol. Catal.: B Enzym. 2010, 62:162-168.
    • (2010) J. Mol. Catal.: B Enzym. , vol.62 , pp. 162-168
    • Yilmaz, E.1    Sezgin, M.2    Yilmaz, M.3


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