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Volumn 61-62, Issue , 2014, Pages 28-34

Immobilized Candida antarctica lipase B on ZnO nanowires/macroporous silica composites for catalyzing chiral resolution of (R,S)-2-octanol

Author keywords

(R,S) 2 Octanol; Chiral resolution; Immobilized lipase; ZnO nanowires

Indexed keywords

ISOMERS; MESOPOROUS MATERIALS; NANOWIRES; ZINC OXIDE;

EID: 84900789862     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2014.04.014     Document Type: Article
Times cited : (24)

References (55)
  • 2
    • 0032103824 scopus 로고    scopus 로고
    • Rhizomucor miehei lipase as the catalyst in the resolution of chiral compounds: an overview
    • Alcántara A.R., Fuentes I.E., Sinisterra J.V. Rhizomucor miehei lipase as the catalyst in the resolution of chiral compounds: an overview. Chem Phys Lipids 1998, 93:169-184.
    • (1998) Chem Phys Lipids , vol.93 , pp. 169-184
    • Alcántara, A.R.1    Fuentes, I.E.2    Sinisterra, J.V.3
  • 3
    • 0041152088 scopus 로고    scopus 로고
    • Properties and synthetic applications of enzymes in organic solvents
    • Carrea G., Riva S. Properties and synthetic applications of enzymes in organic solvents. Angew Chem Int Ed 2000, 39:2226-2254.
    • (2000) Angew Chem Int Ed , vol.39 , pp. 2226-2254
    • Carrea, G.1    Riva, S.2
  • 5
    • 83655163758 scopus 로고    scopus 로고
    • Application of a Burkholderia cepacia lipase-immobilized silica monolith micro-bioreactor to continuous-flow kinetic resolution for transesterification of (R,S)-1-phenylethanol
    • Kawakami K., Ueno M., Takei T., Oda Y., Takahashi R. Application of a Burkholderia cepacia lipase-immobilized silica monolith micro-bioreactor to continuous-flow kinetic resolution for transesterification of (R,S)-1-phenylethanol. Process Biochem 2012, 47:147-150.
    • (2012) Process Biochem , vol.47 , pp. 147-150
    • Kawakami, K.1    Ueno, M.2    Takei, T.3    Oda, Y.4    Takahashi, R.5
  • 6
    • 84455175338 scopus 로고    scopus 로고
    • Asymmetric transesterification resolution of (R,S)-α-phenylethanol in a non-aqueous medium by microbial lipase
    • Qin L.N., Yu X.W., Xu Y. Asymmetric transesterification resolution of (R,S)-α-phenylethanol in a non-aqueous medium by microbial lipase. Chin J Catal 2011, 32:1639-1644.
    • (2011) Chin J Catal , vol.32 , pp. 1639-1644
    • Qin, L.N.1    Yu, X.W.2    Xu, Y.3
  • 7
    • 84860840735 scopus 로고    scopus 로고
    • Lipase entrapment in protamine-induced bio-zirconia particles: characterization and application to the resolution of (R,S)-1-phenylethanol
    • Wang J.Y., Ma C.L., Bao Y.M., Xu P.S. Lipase entrapment in protamine-induced bio-zirconia particles: characterization and application to the resolution of (R,S)-1-phenylethanol. Enzyme Microb Technol 2012, 51:42-46.
    • (2012) Enzyme Microb Technol , vol.51 , pp. 42-46
    • Wang, J.Y.1    Ma, C.L.2    Bao, Y.M.3    Xu, P.S.4
  • 8
    • 78650092281 scopus 로고    scopus 로고
    • Mutated variant of Candida antarctica lipase B in (S)-selective dynamic kinetic resolution of secondary alcohols
    • Engström K., Vallin M., Syrén P.O., Hult K., Bäckvall J.E. Mutated variant of Candida antarctica lipase B in (S)-selective dynamic kinetic resolution of secondary alcohols. Org Biomol Chem 2011, 9:81-82.
    • (2011) Org Biomol Chem , vol.9 , pp. 81-82
    • Engström, K.1    Vallin, M.2    Syrén, P.O.3    Hult, K.4    Bäckvall, J.E.5
  • 9
    • 21044443212 scopus 로고    scopus 로고
    • Combined ruthenium(II) and lipase catalysis for efficient dynamic kinetic resolution of secondary alcohols. Insight into the racemization mechanism
    • Martín-Matute B., Edin M., Bogár K., Kaynak F.B., Bäckvall J.E. Combined ruthenium(II) and lipase catalysis for efficient dynamic kinetic resolution of secondary alcohols. Insight into the racemization mechanism. J Am Chem Soc 2005, 127:8817-8825.
    • (2005) J Am Chem Soc , vol.127 , pp. 8817-8825
    • Martín-Matute, B.1    Edin, M.2    Bogár, K.3    Kaynak, F.B.4    Bäckvall, J.E.5
  • 10
    • 34547933047 scopus 로고    scopus 로고
    • A chemo-enzymatic process for sequential kinetic resolution of (R,S)-2-octanol under microwave irradiation
    • Yu D.H., Chen P., Wang L., Gu Q., Li Y., Wang Z., Cao S.G. A chemo-enzymatic process for sequential kinetic resolution of (R,S)-2-octanol under microwave irradiation. Process Biochem 2007, 42:1312-1318.
    • (2007) Process Biochem , vol.42 , pp. 1312-1318
    • Yu, D.H.1    Chen, P.2    Wang, L.3    Gu, Q.4    Li, Y.5    Wang, Z.6    Cao, S.G.7
  • 11
    • 33646085798 scopus 로고    scopus 로고
    • Resolution of (R,S)-2-octanol by Penicillium expansum PED-03 lipase immobilized on modified ultrastable-Y molecular sieve in microaqueous media
    • Dai D.Z., Xia L.M. Resolution of (R,S)-2-octanol by Penicillium expansum PED-03 lipase immobilized on modified ultrastable-Y molecular sieve in microaqueous media. Process Biochem 2006, 41:1455-1460.
    • (2006) Process Biochem , vol.41 , pp. 1455-1460
    • Dai, D.Z.1    Xia, L.M.2
  • 12
    • 47049084751 scopus 로고    scopus 로고
    • An immobilized lipase with high enantioselectivity in the resolution of racemic ibuprofen
    • Tang L.H., Xia L.M., Su M., Guo H.Y., Zhang J.P. An immobilized lipase with high enantioselectivity in the resolution of racemic ibuprofen. Chin J Process Eng 2008, 8:567-571.
    • (2008) Chin J Process Eng , vol.8 , pp. 567-571
    • Tang, L.H.1    Xia, L.M.2    Su, M.3    Guo, H.Y.4    Zhang, J.P.5
  • 13
    • 84877817460 scopus 로고    scopus 로고
    • Lipase-immobilized magnetic chitosan nanoparticles for kinetic resolution of (R,S)-ibuprofen
    • Tomasz S., Marta Z.B., Michał P.M. Lipase-immobilized magnetic chitosan nanoparticles for kinetic resolution of (R,S)-ibuprofen. J Mol Catal B Enzym 2013, 94:7-14.
    • (2013) J Mol Catal B Enzym , vol.94 , pp. 7-14
    • Tomasz, S.1    Marta, Z.B.2    Michał, P.M.3
  • 14
    • 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
  • 15
    • 79751532883 scopus 로고    scopus 로고
    • Immobilization of Candida rugosa lipase on magnetic sol-gel composite supports for enzymatic resolution of (R,S)-Naproxen methyl ester
    • Yilmaz E., Sezgin M., Yilmaz M. Immobilization of Candida rugosa lipase on magnetic sol-gel composite supports for enzymatic resolution of (R,S)-Naproxen methyl ester. J Mol Catal B Enzym 2011, 69:35-41.
    • (2011) J Mol Catal B Enzym , vol.69 , pp. 35-41
    • Yilmaz, E.1    Sezgin, M.2    Yilmaz, M.3
  • 16
    • 82255186199 scopus 로고    scopus 로고
    • Enantioselective resolution of racemic Naproxen by a lipase from Penicillium expansum
    • Tang L.H., Cai Z.X., Su M., Zhu L., Zhou Q., Lu B.Y. Enantioselective resolution of racemic Naproxen by a lipase from Penicillium expansum. Chin J Process Eng 2011, 11:828-833.
    • (2011) Chin J Process Eng , vol.11 , pp. 828-833
    • Tang, L.H.1    Cai, Z.X.2    Su, M.3    Zhu, L.4    Zhou, Q.5    Lu, B.Y.6
  • 17
    • 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
  • 18
    • 0034099693 scopus 로고    scopus 로고
    • Entrapment of lipases in hydrophobic sol-gel-materials: efficient heterogeneous biocatalysts in aqueous medium
    • Reetz M.T., Wenkel R., Avnir D. Entrapment of lipases in hydrophobic sol-gel-materials: efficient heterogeneous biocatalysts in aqueous medium. Synthesis 2000, 6:781-783.
    • (2000) Synthesis , vol.6 , pp. 781-783
    • Reetz, M.T.1    Wenkel, R.2    Avnir, D.3
  • 19
    • 20444381371 scopus 로고    scopus 로고
    • Sol-gel materials as efficient enzyme protectors: preserving the activity of phosphatases under extreme pH conditions
    • Frenkel-Mullerad H., Avnir D. Sol-gel materials as efficient enzyme protectors: preserving the activity of phosphatases under extreme pH conditions. J Am Chem Soc 2005, 127:8077-8081.
    • (2005) J Am Chem Soc , vol.127 , pp. 8077-8081
    • Frenkel-Mullerad, H.1    Avnir, D.2
  • 20
    • 34247485012 scopus 로고    scopus 로고
    • Biochemically active sol-gel glasses: the trapping of enzymes
    • Braun S., Rappoport S., Zusman R., Avnir D., Ottolenghi M. Biochemically active sol-gel glasses: the trapping of enzymes. Mater Lett 2007, 61:2843-2846.
    • (2007) Mater Lett , vol.61 , pp. 2843-2846
    • Braun, S.1    Rappoport, S.2    Zusman, R.3    Avnir, D.4    Ottolenghi, M.5
  • 21
    • 0041430560 scopus 로고    scopus 로고
    • Immobilised enzymes: carrier-bound or carrier-free
    • Cao L., Langen L., Sheldon R. Immobilised enzymes: carrier-bound or carrier-free. Curr Opin Biotechnol 2003, 14:387-394.
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 387-394
    • Cao, L.1    Langen, L.2    Sheldon, R.3
  • 22
    • 34548587180 scopus 로고    scopus 로고
    • Functionalization of cubic Ia3d mesoporous silica for immobilization of penicillin G acylase
    • Lv Y.J., Lu G.Z., Wang Y.Q., Guo Y., Zhang Z., Wang Y., et al. Functionalization of cubic Ia3d mesoporous silica for immobilization of penicillin G acylase. Adv Funct Mater 2007, 17:2160-2166.
    • (2007) Adv Funct Mater , vol.17 , pp. 2160-2166
    • Lv, Y.J.1    Lu, G.Z.2    Wang, Y.Q.3    Guo, Y.4    Zhang, Z.5    Wang, Y.6
  • 23
    • 0026931265 scopus 로고
    • Ordered mesoporous molecular sieves: synthesized by a liquid-crystal template mechanism
    • Kresge C.T., Leonowicz M.E., Roth W.J., Vartulli J.C., Beck J.S. Ordered mesoporous molecular sieves: synthesized by a liquid-crystal template mechanism. Nature 1992, 359:710-712.
    • (1992) Nature , vol.359 , pp. 710-712
    • Kresge, C.T.1    Leonowicz, M.E.2    Roth, W.J.3    Vartulli, J.C.4    Beck, J.S.5
  • 24
    • 0033556058 scopus 로고    scopus 로고
    • Synthesis and applications of supramolecular-templated mesoporous materials
    • Ying J.Y., Mehnert C.P., Wong M.S. Synthesis and applications of supramolecular-templated mesoporous materials. Angew Chem Int Ed 1999, 38:56-77.
    • (1999) Angew Chem Int Ed , vol.38 , pp. 56-77
    • Ying, J.Y.1    Mehnert, C.P.2    Wong, M.S.3
  • 25
    • 45849151618 scopus 로고    scopus 로고
    • Candida antarctica lipase B immobilization onto hybrid organic-inorganic mesoporous materials
    • Dragoi B., Dumitriu E. Candida antarctica lipase B immobilization onto hybrid organic-inorganic mesoporous materials. Acta Chim Slov 2008, 55:277-285.
    • (2008) Acta Chim Slov , vol.55 , pp. 277-285
    • Dragoi, B.1    Dumitriu, E.2
  • 27
    • 56949094281 scopus 로고    scopus 로고
    • Epoxy-functionalized mesostructured cellular foams as effective support for covalent immobilization of penicillin G acylase
    • Xue P., Xu F., Xu L.D. Epoxy-functionalized mesostructured cellular foams as effective support for covalent immobilization of penicillin G acylase. Appl Surf Sci 2008, 255:1625-1630.
    • (2008) Appl Surf Sci , vol.255 , pp. 1625-1630
    • Xue, P.1    Xu, F.2    Xu, L.D.3
  • 28
    • 0032559316 scopus 로고    scopus 로고
    • Triblock copolymer syntheses of mesoporous silica with periodic 50-300Å pores
    • Zhao D., Feng J., Huo Q., Melosh N., Fredrickson G.H., Chemlka B.F., et al. Triblock copolymer syntheses of mesoporous silica with periodic 50-300Å pores. Science 1998, 279:548-552.
    • (1998) Science , vol.279 , pp. 548-552
    • Zhao, D.1    Feng, J.2    Huo, Q.3    Melosh, N.4    Fredrickson, G.H.5    Chemlka, B.F.6
  • 29
    • 20744454462 scopus 로고    scopus 로고
    • Physical and chemical adsorption of Mucor javanicus lipase on SBA-15 mesoporous silica. Synthesis, structural characterization, and activity performance
    • Salis A., Meloni D., Ligas S., Casula M.F., Monduzzi M., Solinas V., et al. Physical and chemical adsorption of Mucor javanicus lipase on SBA-15 mesoporous silica. Synthesis, structural characterization, and activity performance. Langmuir 2005, 21:5511-5516.
    • (2005) Langmuir , vol.21 , pp. 5511-5516
    • Salis, A.1    Meloni, D.2    Ligas, S.3    Casula, M.F.4    Monduzzi, M.5    Solinas, V.6
  • 30
    • 67349203634 scopus 로고    scopus 로고
    • Adsorption and catalytic activity of porcine pancreatic lipase on rod-like SBA-15 mesoporous material
    • Li Y.J., Zhou G.W., Li C.J., Qin D.W., Qiao W.T., Chu B. Adsorption and catalytic activity of porcine pancreatic lipase on rod-like SBA-15 mesoporous material. Colloids Surf A 2009, 341:79-85.
    • (2009) Colloids Surf A , vol.341 , pp. 79-85
    • Li, Y.J.1    Zhou, G.W.2    Li, C.J.3    Qin, D.W.4    Qiao, W.T.5    Chu, B.6
  • 31
    • 76749111010 scopus 로고    scopus 로고
    • Effect of pore diameter and cross-linking method on the immobilization efficiency of Candida rugosa lipase in SBA-15
    • Gao S.L., Wang Y.J., Diao X., Luo G.S., Dai Y.Y. Effect of pore diameter and cross-linking method on the immobilization efficiency of Candida rugosa lipase in SBA-15. Bioresour Technol 2010, 101:3830-3837.
    • (2010) Bioresour Technol , vol.101 , pp. 3830-3837
    • Gao, S.L.1    Wang, Y.J.2    Diao, X.3    Luo, G.S.4    Dai, Y.Y.5
  • 32
    • 2342566958 scopus 로고    scopus 로고
    • A novel support of MCM-48 molecular sieve for immobilization of penicillin G acylase
    • Xue P., Lu G.Z., Guo Y.L., Wang Y.S., Guo Y. A novel support of MCM-48 molecular sieve for immobilization of penicillin G acylase. J Mol Catal B Enzym 2004, 30:75-81.
    • (2004) J Mol Catal B Enzym , vol.30 , pp. 75-81
    • Xue, P.1    Lu, G.Z.2    Guo, Y.L.3    Wang, Y.S.4    Guo, Y.5
  • 33
    • 0037441136 scopus 로고    scopus 로고
    • Adsorption properties for urokinase on local diatomite surface
    • Yang Y.X., Zhang J.B., Yang W.M., Wu J.D., Chen R.S. Adsorption properties for urokinase on local diatomite surface. Appl Surf Sci 2003, 206:20-28.
    • (2003) Appl Surf Sci , vol.206 , pp. 20-28
    • Yang, Y.X.1    Zhang, J.B.2    Yang, W.M.3    Wu, J.D.4    Chen, R.S.5
  • 34
    • 79957920510 scopus 로고    scopus 로고
    • Immobilization of lipase on nano- and microporous ceramic foam
    • Huang L., Cheng Z.M. Immobilization of lipase on nano- and microporous ceramic foam. Chin J Catal 2008, 29:57-62.
    • (2008) Chin J Catal , vol.29 , pp. 57-62
    • Huang, L.1    Cheng, Z.M.2
  • 38
    • 84890821031 scopus 로고    scopus 로고
    • 2 ternary composite photo-catalyst
    • 2 ternary composite photo-catalyst. Chin J Mater Res 2013, 27:526-531.
    • (2013) Chin J Mater Res , vol.27 , pp. 526-531
    • Li, X.F.1    Zhang, R.F.2
  • 39
    • 3342986578 scopus 로고    scopus 로고
    • Immobilization of uricase on ZnO nanorods for a reagentless uric acid biosensor
    • Zhang F.F., Wang X.L., Ai S.Y., Sun Z.D., Wan Q., Zhu Z.Q., et al. Immobilization of uricase on ZnO nanorods for a reagentless uric acid biosensor. Anal Chim Acta 2004, 519:155-160.
    • (2004) Anal Chim Acta , vol.519 , pp. 155-160
    • Zhang, F.F.1    Wang, X.L.2    Ai, S.Y.3    Sun, Z.D.4    Wan, Q.5    Zhu, Z.Q.6
  • 40
    • 79952450502 scopus 로고    scopus 로고
    • Selective potentiometric determination of uric acid with uricase immobilized on ZnO nanowires
    • Usman A., Alvi N.H., Ibupoto Z., Nur O., Willander M., Danielsson B. Selective potentiometric determination of uric acid with uricase immobilized on ZnO nanowires. Sensor Actuat B Chem 2011, 152:241-247.
    • (2011) Sensor Actuat B Chem , vol.152 , pp. 241-247
    • Usman, A.1    Alvi, N.H.2    Ibupoto, Z.3    Nur, O.4    Willander, M.5    Danielsson, B.6
  • 41
    • 57649184056 scopus 로고    scopus 로고
    • Enhancement of Rhizopus oryzae lipase activity immobilized on alkyl-functionalized spherical mesocellular foam: influence of alkyl chain length
    • Shakeri M., Kawakami K. Enhancement of Rhizopus oryzae lipase activity immobilized on alkyl-functionalized spherical mesocellular foam: influence of alkyl chain length. Microporous Mesoporous Mater 2009, 118:115-120.
    • (2009) Microporous Mesoporous Mater , vol.118 , pp. 115-120
    • Shakeri, M.1    Kawakami, K.2
  • 42
    • 79955466208 scopus 로고    scopus 로고
    • Improving adsorption and activation of the lipase immobilized in amino-functionalized ordered mesoporous SBA-15
    • Xu Y.Q., Zhou G.W., Wu C.C., Li T.D., Song H.B. Improving adsorption and activation of the lipase immobilized in amino-functionalized ordered mesoporous SBA-15. Solid State Sci 2011, 13:867-874.
    • (2011) Solid State Sci , vol.13 , pp. 867-874
    • Xu, Y.Q.1    Zhou, G.W.2    Wu, C.C.3    Li, T.D.4    Song, H.B.5
  • 43
    • 2342642030 scopus 로고    scopus 로고
    • Functionalization of mesoporous silica for lipase immobilization: characterization of the support and the catalysts
    • Blanco R.M., Terreros P., Mónica F.P., Otero C., Guadalupe D.G. Functionalization of mesoporous silica for lipase immobilization: characterization of the support and the catalysts. J Mol Catal B Enzym 2004, 30:83-93.
    • (2004) J Mol Catal B Enzym , vol.30 , pp. 83-93
    • Blanco, R.M.1    Terreros, P.2    Mónica, F.P.3    Otero, C.4    Guadalupe, D.G.5
  • 44
    • 68149165947 scopus 로고    scopus 로고
    • Laccase immobilized on methylene blue modified mesoporous silica MCM-41/PVA
    • Xu X.H., Lu P., Zhou Y.M., Zhao Z.Z., Guo M.Q. Laccase immobilized on methylene blue modified mesoporous silica MCM-41/PVA. Mater Sci Eng C Mater 2009, 29:2160-2164.
    • (2009) Mater Sci Eng C Mater , vol.29 , pp. 2160-2164
    • Xu, X.H.1    Lu, P.2    Zhou, Y.M.3    Zhao, Z.Z.4    Guo, M.Q.5
  • 45
    • 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
  • 46
    • 3343010596 scopus 로고    scopus 로고
    • Immobilization of lipase in a mesoporous reactor based on MCM-41
    • Ma H., He J., Evans D.G., Duan X. Immobilization of lipase in a mesoporous reactor based on MCM-41. J Mol Catal B Enzym 2004, 30:209-217.
    • (2004) J Mol Catal B Enzym , vol.30 , pp. 209-217
    • Ma, H.1    He, J.2    Evans, D.G.3    Duan, X.4
  • 47
    • 2442630236 scopus 로고    scopus 로고
    • Hydrothermal synthesis of one-dimensional ZnO nanostructures with different aspect ratios
    • Cheng B., Samulski E.T. Hydrothermal synthesis of one-dimensional ZnO nanostructures with different aspect ratios. Chem Commun 2004, 19:986-987.
    • (2004) Chem Commun , vol.19 , pp. 986-987
    • Cheng, B.1    Samulski, E.T.2
  • 48
    • 4544270955 scopus 로고    scopus 로고
    • Seed-mediated synthesis of uniform ZnO nanorods in the presence of polyethylene glycol
    • Liu X.M., Zhou Y.C. Seed-mediated synthesis of uniform ZnO nanorods in the presence of polyethylene glycol. J Cryst Growth 2004, 270:527-534.
    • (2004) J Cryst Growth , vol.270 , pp. 527-534
    • Liu, X.M.1    Zhou, Y.C.2
  • 49
    • 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, 58:24-28.
    • (2009) J Mol Catal B Enzym , vol.58 , pp. 24-28
    • Habulin, M.1    Knez, Ž.2
  • 50
    • 28844488269 scopus 로고    scopus 로고
    • Effect of solvent and initial water content on (R,S)-1-phenylethanol resolution
    • Chua L.S., Sarmidi M.R. Effect of solvent and initial water content on (R,S)-1-phenylethanol resolution. Enzyme Microb Technol 2006, 38:551-556.
    • (2006) Enzyme Microb Technol , vol.38 , pp. 551-556
    • Chua, L.S.1    Sarmidi, M.R.2
  • 51
    • 84888204321 scopus 로고    scopus 로고
    • Conformation studies on Burkholderia cenocepacia lipase via resolution of racemic 1-phenylethanol in non-aqueous medium and its process optimization
    • Li X., Xu L., Wang G.L., Zhang H.J., Yan Y.J. Conformation studies on Burkholderia cenocepacia lipase via resolution of racemic 1-phenylethanol in non-aqueous medium and its process optimization. Process Biochem 2013, 48:1905-1933.
    • (2013) Process Biochem , vol.48 , pp. 1905-1933
    • Li, X.1    Xu, L.2    Wang, G.L.3    Zhang, H.J.4    Yan, Y.J.5
  • 52
    • 34547729864 scopus 로고    scopus 로고
    • Resolution of 2-octanol by SBA-15 immobilized Pseudomonas sp. lipase
    • Yu D.H., Wang Z., Zhao L.F., Cheng Y.M., Cao S.G. Resolution of 2-octanol by SBA-15 immobilized Pseudomonas sp. lipase. J Mol Catal B Enzym 2007, 48:64-69.
    • (2007) J Mol Catal B Enzym , vol.48 , pp. 64-69
    • Yu, D.H.1    Wang, Z.2    Zhao, L.F.3    Cheng, Y.M.4    Cao, S.G.5
  • 53
    • 34547197843 scopus 로고    scopus 로고
    • Microwave-assisted resolution of (R,S)-2-octanol by enzymatic transesterification
    • Yu D.H., Wang Z., Chen P., Jin L., Cheng Y.M., Zhou J.G., et al. Microwave-assisted resolution of (R,S)-2-octanol by enzymatic transesterification. J Mol Catal B Enzym 2007, 48:51-57.
    • (2007) J Mol Catal B Enzym , vol.48 , pp. 51-57
    • Yu, D.H.1    Wang, Z.2    Chen, P.3    Jin, L.4    Cheng, Y.M.5    Zhou, J.G.6
  • 54
    • 84856491001 scopus 로고    scopus 로고
    • Immobilization of lipase on aminopropyl-grafted mesoporous silica nanotubes for the resolution of (R,S)-1-phenylethanol
    • Bai W., Yang Y.J., Tao X., Chen J.F., Tan T.W. Immobilization of lipase on aminopropyl-grafted mesoporous silica nanotubes for the resolution of (R,S)-1-phenylethanol. J Mol Catal B Enzym 2012, 76:82-88.
    • (2012) J Mol Catal B Enzym , vol.76 , pp. 82-88
    • Bai, W.1    Yang, Y.J.2    Tao, X.3    Chen, J.F.4    Tan, T.W.5
  • 55
    • 72049122155 scopus 로고    scopus 로고
    • Enantioselective transesterification catalysis by Candida antarctica lipase immobilized on superparamagnetic nanoparticles
    • Netto C., Andrade L.H., Toma H.E. Enantioselective transesterification catalysis by Candida antarctica lipase immobilized on superparamagnetic nanoparticles. Tetrahedron Asymmetry 2009, 20:2299-2304.
    • (2009) Tetrahedron Asymmetry , vol.20 , pp. 2299-2304
    • Netto, C.1    Andrade, L.H.2    Toma, H.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.