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Volumn 102, Issue 6, 2011, Pages 4313-4318

Improvement of catalytic activity of lipase from Candida rugosa via sol-gel encapsulation in the presence of calix(aza)crown

Author keywords

Calix(aza)crowns; Candida rugosa lipase; Enantioselective hydrolysis; Naproxen; Sol gel encapsulation

Indexed keywords

CALIX(AZA)CROWNS; CANDIDA RUGOSA LIPASE; ENANTIOSELECTIVE HYDROLYSIS; NAPROXENS; SOL-GEL ENCAPSULATION;

EID: 79551689143     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2010.12.105     Document Type: Article
Times cited : (54)

References (35)
  • 1
    • 37049034075 scopus 로고    scopus 로고
    • The synthesis and metal cation extraction studies of novel polymer-bound calix(aza)crowns
    • Akkus G.U., Memon S., Gurkas D.E., Aslan S., Yilmaz M. The synthesis and metal cation extraction studies of novel polymer-bound calix(aza)crowns. React. Funct. Polym. 2008, 68:125-132.
    • (2008) React. Funct. Polym. , vol.68 , pp. 125-132
    • Akkus, G.U.1    Memon, S.2    Gurkas, D.E.3    Aslan, S.4    Yilmaz, M.5
  • 3
    • 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
    • 78649709520 scopus 로고    scopus 로고
    • Kinetic resolution of (R/S)-propranolol (1-isopropylamino-3-(1-naphtoxy)-2-propanolol) catalyzed by immobilized preparations of Candida antarctica lipase B (CAL-B)
    • Barbosa O., Ariza C., Ortiz C., Torres R. Kinetic resolution of (R/S)-propranolol (1-isopropylamino-3-(1-naphtoxy)-2-propanolol) catalyzed by immobilized preparations of Candida antarctica lipase B (CAL-B). New Biotechnol. 2010, 27:844-850.
    • (2010) New Biotechnol. , vol.27 , pp. 844-850
    • Barbosa, O.1    Ariza, C.2    Ortiz, C.3    Torres, R.4
  • 6
    • 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. 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.A.1
  • 7
    • 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
  • 8
    • 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
  • 9
    • 77950342129 scopus 로고    scopus 로고
    • Evaluation of the catalytic properties of Burkholderia cepacia lipase immobilized on non-commercial matrices to be used in biodiesel synthesis from different feedstocks
    • Da Rós P.C.M., Silva G.A.M., Mendes A.A., Santos J.C., Heizir F., de Castro H.F. Evaluation of the catalytic properties of Burkholderia cepacia lipase immobilized on non-commercial matrices to be used in biodiesel synthesis from different feedstocks. Bioresour. Technol. 2010, 101:5508-5516.
    • (2010) Bioresour. Technol. , vol.101 , pp. 5508-5516
    • Da Rós, P.C.M.1    Silva, G.A.M.2    Mendes, A.A.3    Santos, J.C.4    Heizir, F.5    de Castro, H.F.6
  • 10
    • 63249085444 scopus 로고    scopus 로고
    • Synthesis of calix[n]arene-based silica polymers for lipase immobilization
    • Erdemir S., Yilmaz M. Synthesis of calix[n]arene-based silica polymers for lipase immobilization. J. Mol. Catal. B: Enzym. 2009, 58:29-35.
    • (2009) J. Mol. Catal. B: Enzym. , vol.58 , pp. 29-35
    • Erdemir, S.1    Yilmaz, M.2
  • 11
    • 0035826279 scopus 로고    scopus 로고
    • Modulation of lipase properties in macroaqueous system by controlled enzyme immobilization: enantioselective hydrolysis of a chiral ester by immobilized Pseudomonas lipase
    • Fernandez-Lorente G., Terreni M., Mateo C., Bastida A., Fernandez-Lafuente R., Dalmases P. Modulation of lipase properties in macroaqueous system by controlled enzyme immobilization: enantioselective hydrolysis of a chiral ester by immobilized Pseudomonas lipase. Enzyme Microb. Technol. 2001, 28:389-396.
    • (2001) Enzyme Microb. Technol. , vol.28 , pp. 389-396
    • Fernandez-Lorente, G.1    Terreni, M.2    Mateo, C.3    Bastida, A.4    Fernandez-Lafuente, R.5    Dalmases, P.6
  • 12
    • 60249100095 scopus 로고    scopus 로고
    • Enzyme immobilization: part 1. Modified bentonite as a new and efficient support for immobilization of Candida rugosa lipase
    • Ghiaci M., Aghaei H., Soleimanian S., Sedaghat M.E. Enzyme immobilization: part 1. Modified bentonite as a new and efficient support for immobilization of Candida rugosa lipase. Appl. Clay Sci. 2008, 43:289-295.
    • (2008) Appl. Clay Sci. , vol.43 , pp. 289-295
    • Ghiaci, M.1    Aghaei, H.2    Soleimanian, S.3    Sedaghat, M.E.4
  • 14
    • 0000873890 scopus 로고
    • Calixarenes. 13. The conformational properties of calix[4]arenes, calix[6]arenes, calix[8]arenes, and oxacalixarenes
    • Gutsche C.D., Bauer L.J. Calixarenes. 13. The conformational properties of calix[4]arenes, calix[6]arenes, calix[8]arenes, and oxacalixarenes. J. Am. Chem. Soc. 1985, 107:6052-6059.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 6052-6059
    • Gutsche, C.D.1    Bauer, L.J.2
  • 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
    • 76249122876 scopus 로고    scopus 로고
    • Formation and hydrolysis of amide bonds by lipase A from Candida antarctica; exceptional features
    • Liljeblad A., Kallio P., Vainio M., Niemi J., Kanerva L.T. Formation and hydrolysis of amide bonds by lipase A from Candida antarctica; exceptional features. Org. Biomol. Chem. 2010, 8:886-895.
    • (2010) Org. Biomol. Chem. , vol.8 , pp. 886-895
    • Liljeblad, A.1    Kallio, P.2    Vainio, M.3    Niemi, J.4    Kanerva, L.T.5
  • 19
    • 34247178318 scopus 로고    scopus 로고
    • Enzymatic polymerization of o-phenylendiamine with cytochrome c activated by a calixarene derivative in organic media
    • Oshima T., Sato M., Shikaze Y., Ohto K., Inoue K., Baba Y. Enzymatic polymerization of o-phenylendiamine with cytochrome c activated by a calixarene derivative in organic media. Biochem. Eng. J. 2007, 35:66-70.
    • (2007) Biochem. Eng. J. , vol.35 , pp. 66-70
    • Oshima, T.1    Sato, M.2    Shikaze, Y.3    Ohto, K.4    Inoue, K.5    Baba, Y.6
  • 20
    • 0036843441 scopus 로고    scopus 로고
    • Modulation of the enantioselectivity of lipases via controlled immobilization and medium engineering: hydrolytic resolution of mandelic acid esters
    • Palomo J.M., Fernandez-Lorente G., Mateo C., Ortiz C., Fernandez-Lafuente R., Guisan J.M. Modulation of the enantioselectivity of lipases via controlled immobilization and medium engineering: hydrolytic resolution of mandelic acid esters. Enzyme Microb. Technol. 2002, 31:775-783.
    • (2002) Enzyme Microb. Technol. , vol.31 , pp. 775-783
    • Palomo, J.M.1    Fernandez-Lorente, G.2    Mateo, C.3    Ortiz, C.4    Fernandez-Lafuente, R.5    Guisan, J.M.6
  • 21
    • 33747087752 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of castor oil: process intensification studies
    • Puthli M.S., Rathod V.K., Pandit A.B. Enzymatic hydrolysis of castor oil: process intensification studies. Biochem. Eng. J. 2006, 31:31-41.
    • (2006) Biochem. Eng. J. , vol.31 , pp. 31-41
    • Puthli, M.S.1    Rathod, V.K.2    Pandit, A.B.3
  • 22
    • 0031251298 scopus 로고    scopus 로고
    • Entrapment of biocatalysts in hydrophobic sol-gel materials for use in organic chemistry
    • Reetz Manfred T. Entrapment of biocatalysts in hydrophobic sol-gel materials for use in organic chemistry. Adv. Mater. 1997, 9:943-954.
    • (1997) Adv. Mater. , vol.9 , pp. 943-954
    • Reetz, M.T.1
  • 23
    • 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
  • 25
    • 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 2009, 369:36-41.
    • (2009) Appl. Catal., A , vol.369 , pp. 36-41
    • Sahin, O.1    Erdemir, S.2    Uyanik, A.3    Yilmaz, M.4
  • 26
    • 0035010788 scopus 로고    scopus 로고
    • Selection of stabilizing additive for lipase immobilization on controlled pore silica by factorial design
    • Soares C.M.D., De Castro H.F., Santana M.H.A., Zanin G.M. Selection of stabilizing additive for lipase immobilization on controlled pore silica by factorial design. Appl. Biochem. Biotechnol. 2001, 91-93:703-718.
    • (2001) Appl. Biochem. Biotechnol. , pp. 703-718
    • Soares, C.M.D.1    De Castro, H.F.2    Santana, M.H.A.3    Zanin, G.M.4
  • 28
    • 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
  • 29
    • 77955627031 scopus 로고    scopus 로고
    • Lipase immobilization on smectite nanoclays: characterization and application to the epoxidation of a-pinene
    • Tzialla A.A., Pavlidis I.V., Felicissimo M.P., Rudolf P., Gournis D., Stamatis H. Lipase immobilization on smectite nanoclays: characterization and application to the epoxidation of a-pinene. Bioresour. Technol. 2010, 101:1587-1594.
    • (2010) Bioresour. Technol. , vol.101 , pp. 1587-1594
    • Tzialla, A.A.1    Pavlidis, I.V.2    Felicissimo, M.P.3    Rudolf, P.4    Gournis, D.5    Stamatis, H.6
  • 30
    • 43849086839 scopus 로고    scopus 로고
    • Immobilization of Candida rugosa lipase on poly(allyl glycidyl ether-co-ethylene glycol dimethacrylate) macroporous polymer particles
    • Vaidya B.K., Ingavle G.C., Ponrathnam S., Kulkarni B.D., Nene S.N. Immobilization of Candida rugosa lipase on poly(allyl glycidyl ether-co-ethylene glycol dimethacrylate) macroporous polymer particles. Bioresour. Technol. 2008, 99:3623-3629.
    • (2008) Bioresour. Technol. , vol.99 , pp. 3623-3629
    • Vaidya, B.K.1    Ingavle, G.C.2    Ponrathnam, S.3    Kulkarni, B.D.4    Nene, S.N.5
  • 31
    • 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. Enzyme Microb. Technol. 2000, 26:124-130.
    • (2000) Enzyme Microb. Technol. , vol.26 , pp. 124-130
    • Wu, J.-Y.1    Liu, S.W.2
  • 32
    • 67349253043 scopus 로고    scopus 로고
    • Improvement of catalytic properties of lipase from Arthrobacter sp. by encapsulation in hydrophobic sol-gel materials
    • Yang G., Wu J., Xu G., Yang L. Improvement of catalytic properties of lipase from Arthrobacter sp. by encapsulation in hydrophobic sol-gel materials. Bioresour. Technol. 2009, 100:4311-4316.
    • (2009) Bioresour. Technol. , vol.100 , pp. 4311-4316
    • Yang, G.1    Wu, J.2    Xu, G.3    Yang, L.4
  • 33
    • 34247639977 scopus 로고    scopus 로고
    • Design of polymer appended calixarenes as ion carries
    • Nova Publishers Inc., New York, R.K. Bregg (Ed.)
    • Yilmaz M., Memon S., Tabakci M., Bartsch R.A. Design of polymer appended calixarenes as ion carries. New Frontiers in Polymer Research 2006, 125-171. Nova Publishers Inc., New York. R.K. Bregg (Ed.).
    • (2006) New Frontiers in Polymer Research , pp. 125-171
    • Yilmaz, M.1    Memon, S.2    Tabakci, M.3    Bartsch, R.A.4
  • 34
    • 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
  • 35
    • 78650707084 scopus 로고    scopus 로고
    • Immobilization of Candida rugosa lipase on glass beads for enantioselective hydrolysis of racemic Naproxen methyl ester
    • Yilmaz E., Can K., Sezgin M., Yilmaz M. Immobilization of Candida rugosa lipase on glass beads for enantioselective hydrolysis of racemic Naproxen methyl ester. Bioresour. Technol. 2011, 102:499-506.
    • (2011) Bioresour. Technol. , vol.102 , pp. 499-506
    • Yilmaz, E.1    Can, K.2    Sezgin, M.3    Yilmaz, M.4


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