메뉴 건너뛰기




Volumn 40, Issue 2, 2007, Pages 228-235

Hydroxypropyl-β-cyclodextrin induced complexation for the biocatalytic resolution of a poorly soluble epoxide

Author keywords

Biocatalytic resolution; Co solvents; Cyclodextrin; DMF; DMSO; Solubility; Styrene oxide

Indexed keywords

ACTIVATION ENERGY; BIOCATALYSTS; COMPLEXATION; CONCENTRATION (PROCESS); SOLUBILITY; STYRENE; SUBSTRATES;

EID: 33751193431     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2006.04.005     Document Type: Article
Times cited : (13)

References (37)
  • 1
    • 1242270555 scopus 로고    scopus 로고
    • Fungal epoxide hydrolases: new landmarks in sequence-activity space
    • Smit M.S. Fungal epoxide hydrolases: new landmarks in sequence-activity space. Trends Biotechnol 22 (2004) 123-129
    • (2004) Trends Biotechnol , vol.22 , pp. 123-129
    • Smit, M.S.1
  • 2
    • 0035710814 scopus 로고    scopus 로고
    • Microbial epoxide hydrolases for preparative biotransformations
    • Steinreiber A., and Faber K. Microbial epoxide hydrolases for preparative biotransformations. Curr Opin Biotechnol 12 (2001) 552-558
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 552-558
    • Steinreiber, A.1    Faber, K.2
  • 3
    • 0033545515 scopus 로고    scopus 로고
    • Epoxide hydrolases from yeasts and other sources: versatile tools in biocatalysis
    • Weijers C.A.G.M., and De Bont J.A.M. Epoxide hydrolases from yeasts and other sources: versatile tools in biocatalysis. J Mol Catal B: Enzym 6 (1999) 199-214
    • (1999) J Mol Catal B: Enzym , vol.6 , pp. 199-214
    • Weijers, C.A.G.M.1    De Bont, J.A.M.2
  • 4
    • 0031149795 scopus 로고    scopus 로고
    • Asymmetric hydrolysis of racemic para-nitrostyrene oxide using an epoxide hydrolase preparation from Aspergillus niger
    • Morisseau C., Nellaiah H., Archelas A., Furstoss R., and Baratti J. Asymmetric hydrolysis of racemic para-nitrostyrene oxide using an epoxide hydrolase preparation from Aspergillus niger. Enzyme Microb Technol 20 (1997) 446-452
    • (1997) Enzyme Microb Technol , vol.20 , pp. 446-452
    • Morisseau, C.1    Nellaiah, H.2    Archelas, A.3    Furstoss, R.4    Baratti, J.5
  • 5
    • 0029090931 scopus 로고
    • Isolation of a highly enantioselective epoxide hydrolase from Rhodococcus sp. NCIMB 11216
    • Mischitz M., Faber K., and Willets A. Isolation of a highly enantioselective epoxide hydrolase from Rhodococcus sp. NCIMB 11216. Biotechnol Lett 17 (1995) 893-898
    • (1995) Biotechnol Lett , vol.17 , pp. 893-898
    • Mischitz, M.1    Faber, K.2    Willets, A.3
  • 6
    • 0035906338 scopus 로고    scopus 로고
    • The enantioselective catalytic hydrolysis of racemic 1,2-epoxyoctane in a batch and a continuous process
    • Krieg H.M., Botes A.L., Smit M.S., Breytenbach J.C., and Keizer K. The enantioselective catalytic hydrolysis of racemic 1,2-epoxyoctane in a batch and a continuous process. J Mol Catal B: Enzym 13 (2001) 37-47
    • (2001) J Mol Catal B: Enzym , vol.13 , pp. 37-47
    • Krieg, H.M.1    Botes, A.L.2    Smit, M.S.3    Breytenbach, J.C.4    Keizer, K.5
  • 7
    • 0031104802 scopus 로고    scopus 로고
    • Why are enzymes less active in organic solvents than in water?
    • Klibanov A.M. Why are enzymes less active in organic solvents than in water?. Trends Biotechnol 15 (1997) 97-101
    • (1997) Trends Biotechnol , vol.15 , pp. 97-101
    • Klibanov, A.M.1
  • 8
    • 0036844979 scopus 로고    scopus 로고
    • Developments and trends in enzyme catalysis in nonconventional media
    • Hari Krishna S. Developments and trends in enzyme catalysis in nonconventional media. Biotechnol Adv 20 (2002) 239-267
    • (2002) Biotechnol Adv , vol.20 , pp. 239-267
    • Hari Krishna, S.1
  • 9
    • 0033534486 scopus 로고    scopus 로고
    • Lipophilic compounds in biotechnology-interactions with cells and technological problems
    • Angelova B., and Schmauder H.-P. Lipophilic compounds in biotechnology-interactions with cells and technological problems. J Biotechnol 67 (1999) 13-32
    • (1999) J Biotechnol , vol.67 , pp. 13-32
    • Angelova, B.1    Schmauder, H.-P.2
  • 12
    • 16644368855 scopus 로고    scopus 로고
    • Correlation between the physicochemical properties of organic solvents and their biocompatibility toward epoxide hydrolase activity in whole-cells of a yeast, Rhodotorula sp.
    • Lotter J., Botes A.L., Van Dyk M.S., and Breytenbach J.C. Correlation between the physicochemical properties of organic solvents and their biocompatibility toward epoxide hydrolase activity in whole-cells of a yeast, Rhodotorula sp. Biotechnol Lett 26 (2004) 1191-1195
    • (2004) Biotechnol Lett , vol.26 , pp. 1191-1195
    • Lotter, J.1    Botes, A.L.2    Van Dyk, M.S.3    Breytenbach, J.C.4
  • 13
    • 0036099668 scopus 로고    scopus 로고
    • Compressed gases as alternative enzymatic-reaction solvents: a short review
    • Knez Z., and Habulin M. Compressed gases as alternative enzymatic-reaction solvents: a short review. J Supercrit Fluids 23 (2002) 29-42
    • (2002) J Supercrit Fluids , vol.23 , pp. 29-42
    • Knez, Z.1    Habulin, M.2
  • 14
    • 1242293116 scopus 로고    scopus 로고
    • Biocatalysis in ionic liquids: the stereoconvergent hydrolysis of trans-β-methylstyrene oxide catalyzed by soluble epoxide hydrolase
    • Chiappe C., Leandri E., Lucchesi S., Pieraccini D., Hammock B.D., and Morisseau C. Biocatalysis in ionic liquids: the stereoconvergent hydrolysis of trans-β-methylstyrene oxide catalyzed by soluble epoxide hydrolase. J Mol Catal B: Enzym 27 (2004) 243-248
    • (2004) J Mol Catal B: Enzym , vol.27 , pp. 243-248
    • Chiappe, C.1    Leandri, E.2    Lucchesi, S.3    Pieraccini, D.4    Hammock, B.D.5    Morisseau, C.6
  • 17
    • 0035501590 scopus 로고    scopus 로고
    • Stability of free and immobilised peroxidase in aqueous-organic solvents mixtures
    • Azevedo A.M., Prazeres D.M.F., Cabral J.M.S., and Fonseca L.P. Stability of free and immobilised peroxidase in aqueous-organic solvents mixtures. J Mol Catal B: Enzym 15 (2001) 147-153
    • (2001) J Mol Catal B: Enzym , vol.15 , pp. 147-153
    • Azevedo, A.M.1    Prazeres, D.M.F.2    Cabral, J.M.S.3    Fonseca, L.P.4
  • 18
    • 0030595052 scopus 로고    scopus 로고
    • Solvent hydrophobicity predicts biocatalytic behaviour of lignin peroxidase and cytochrome c in aqueous solution of water-miscible organic solvents
    • Torres E., Tinoco R., and Vazquez-Duhalt R. Solvent hydrophobicity predicts biocatalytic behaviour of lignin peroxidase and cytochrome c in aqueous solution of water-miscible organic solvents. J Biotechnol 69 (1996) 59-67
    • (1996) J Biotechnol , vol.69 , pp. 59-67
    • Torres, E.1    Tinoco, R.2    Vazquez-Duhalt, R.3
  • 20
    • 0030569736 scopus 로고    scopus 로고
    • Enantioselective hydrolysis of p-nitrostyrene by an epoxide hydrolase preparation from Aspergillus niger
    • Nellaiah H., Morisseau C., Archelas A., Furstoss R., and Baratti J.C. Enantioselective hydrolysis of p-nitrostyrene by an epoxide hydrolase preparation from Aspergillus niger. Biotechnol Bioeng 49 (1996) 70-77
    • (1996) Biotechnol Bioeng , vol.49 , pp. 70-77
    • Nellaiah, H.1    Morisseau, C.2    Archelas, A.3    Furstoss, R.4    Baratti, J.C.5
  • 21
    • 0035813510 scopus 로고    scopus 로고
    • Substrate specificity and effects of water-miscible solvents on the activity and stability of extracellular lipase from Streptomyces rimosus
    • Leščić I., Vukelić B., Majerić-Elenkov M., Saenger W., and Abramić M. Substrate specificity and effects of water-miscible solvents on the activity and stability of extracellular lipase from Streptomyces rimosus. Enzyme Microb Technol 29 (2001) 548-553
    • (2001) Enzyme Microb Technol , vol.29 , pp. 548-553
    • Leščić, I.1    Vukelić, B.2    Majerić-Elenkov, M.3    Saenger, W.4    Abramić, M.5
  • 22
    • 0036890313 scopus 로고    scopus 로고
    • Biotechnological applications of cyclodextrins
    • Singh M., Sharma R., and Banerjee U.C. Biotechnological applications of cyclodextrins. Biotechnol Adv 20 (2002) 341-359
    • (2002) Biotechnol Adv , vol.20 , pp. 341-359
    • Singh, M.1    Sharma, R.2    Banerjee, U.C.3
  • 23
    • 0037018896 scopus 로고    scopus 로고
    • Esterification of hydrophobic substrates by lipase in the cyclodextrin induced emulsion reaction system
    • Shin H.D., Kim J.H., Kim T.K., Kim S.H., and Lee Y.H. Esterification of hydrophobic substrates by lipase in the cyclodextrin induced emulsion reaction system. Enzyme Microb Technol 30 (2002) 835-842
    • (2002) Enzyme Microb Technol , vol.30 , pp. 835-842
    • Shin, H.D.1    Kim, J.H.2    Kim, T.K.3    Kim, S.H.4    Lee, Y.H.5
  • 24
    • 54649083951 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of hydrophobic triolein by lipase in a mono-phase reaction system containing cyclodextrin: reaction characteristics
    • Lee Y.H., Kim T.K., Shin H.D., and Park D.C. Enzymatic hydrolysis of hydrophobic triolein by lipase in a mono-phase reaction system containing cyclodextrin: reaction characteristics. Biotechnol Bioprocess Eng 3 (1998) 103-108
    • (1998) Biotechnol Bioprocess Eng , vol.3 , pp. 103-108
    • Lee, Y.H.1    Kim, T.K.2    Shin, H.D.3    Park, D.C.4
  • 25
    • 12444334256 scopus 로고    scopus 로고
    • Enantioselective hydrolysis of insoluble (R,S)-ketoprofen ethyl ester in dispersed aqueous reaction system induced by chiral cyclodextrin
    • Kim S.H., Kim T.K., Shin G.S., Lee K.W., Shin H.D., and Lee Y.D. Enantioselective hydrolysis of insoluble (R,S)-ketoprofen ethyl ester in dispersed aqueous reaction system induced by chiral cyclodextrin. Biotechnol Lett 26 (2004) 965-969
    • (2004) Biotechnol Lett , vol.26 , pp. 965-969
    • Kim, S.H.1    Kim, T.K.2    Shin, G.S.3    Lee, K.W.4    Shin, H.D.5    Lee, Y.D.6
  • 26
    • 0242361229 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of diloxanide furoate in the presence of β-cyclodextrin and its methylated derivatives
    • Monteiro J.B., Chiaradia L.D., Brandão T.A.S., Dal Magro J., and Yunes R.A. Enzymatic hydrolysis of diloxanide furoate in the presence of β-cyclodextrin and its methylated derivatives. Int J Pharm 267 (2003) 93-100
    • (2003) Int J Pharm , vol.267 , pp. 93-100
    • Monteiro, J.B.1    Chiaradia, L.D.2    Brandão, T.A.S.3    Dal Magro, J.4    Yunes, R.A.5
  • 29
    • 0031578077 scopus 로고    scopus 로고
    • Separation of a biocatalyst with ultrafiltration or filtration after bioconversion
    • Meinderma G.W., Augeraud J., and Vergossen F.H.P. Separation of a biocatalyst with ultrafiltration or filtration after bioconversion. J Membr Sci 125 (1997) 333-349
    • (1997) J Membr Sci , vol.125 , pp. 333-349
    • Meinderma, G.W.1    Augeraud, J.2    Vergossen, F.H.P.3
  • 31
    • 0033982060 scopus 로고    scopus 로고
    • Enrichment of chlorthalidone enantiomers by an aqueous bulk liquid membrane containing β-cyclodextrin
    • Krieg H.M., Lotter J., Keizer K., and Breytenbach J.C. Enrichment of chlorthalidone enantiomers by an aqueous bulk liquid membrane containing β-cyclodextrin. J Membr Sci 167 (2000) 33-45
    • (2000) J Membr Sci , vol.167 , pp. 33-45
    • Krieg, H.M.1    Lotter, J.2    Keizer, K.3    Breytenbach, J.C.4
  • 32
    • 0029595443 scopus 로고
    • The role of pH change caused by the addition of water-miscible organic solvents in the destabilization of an enzyme
    • Shubhada S., and Sundaram P.V. The role of pH change caused by the addition of water-miscible organic solvents in the destabilization of an enzyme. Enzyme Microb Technol 17 (1995) 330-335
    • (1995) Enzyme Microb Technol , vol.17 , pp. 330-335
    • Shubhada, S.1    Sundaram, P.V.2
  • 33
    • 0042866215 scopus 로고    scopus 로고
    • Studies on pH and thermal deactivation of pectolytic enzymes from Aspergillus niger
    • Naidu G.S.N., and Panda T. Studies on pH and thermal deactivation of pectolytic enzymes from Aspergillus niger. Biochem Eng J 16 (2003) 57-67
    • (2003) Biochem Eng J , vol.16 , pp. 57-67
    • Naidu, G.S.N.1    Panda, T.2
  • 36
    • 0033551906 scopus 로고    scopus 로고
    • Stereospecific enzymatic hydrolysis of racemic epoxide: a process for making chiral epoxide
    • Goswami A., Totleben M.J., Singh A.K., and Patel R.N. Stereospecific enzymatic hydrolysis of racemic epoxide: a process for making chiral epoxide. Tetrahedr: Asymm 10 (1999) 3167-3175
    • (1999) Tetrahedr: Asymm , vol.10 , pp. 3167-3175
    • Goswami, A.1    Totleben, M.J.2    Singh, A.K.3    Patel, R.N.4
  • 37
    • 0037430889 scopus 로고    scopus 로고
    • Effects of temperature and pressure on Rhizomucor meihei lipase stability
    • Noel M., and Combes D. Effects of temperature and pressure on Rhizomucor meihei lipase stability. J Biotechnol 102 (2003) 23-32
    • (2003) J Biotechnol , vol.102 , pp. 23-32
    • Noel, M.1    Combes, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.