메뉴 건너뛰기




Volumn 112, Issue , 2016, Pages 136-142

Hydrolysis and oxidation of racemic esters into prochiral ketones catalyzed by a consortium of immobilized enzymes

Author keywords

Alcohol dehydrogenase; Lipase; Multi enzyme systems; Protein stabilization; System biocatalysis

Indexed keywords

BIOCATALYSTS; CATALYSIS; ENZYME IMMOBILIZATION; ESTERS; HYDROLYSIS; KETONES; LIPASES; REUSABILITY;

EID: 84964334545     PISSN: 1369703X     EISSN: 1873295X     Source Type: Journal    
DOI: 10.1016/j.bej.2016.03.015     Document Type: Article
Times cited : (8)

References (32)
  • 1
    • 84860280473 scopus 로고    scopus 로고
    • Biocatalyzed regio- and chemoselective ester cleavage: synthesis of bioactive molecules
    • Barbayianni E., Kokotos G. Biocatalyzed regio- and chemoselective ester cleavage: synthesis of bioactive molecules. ChemCatChem 2012, 4:592-608.
    • (2012) ChemCatChem , vol.4 , pp. 592-608
    • Barbayianni, E.1    Kokotos, G.2
  • 2
    • 84873814343 scopus 로고    scopus 로고
    • A supramolecular approach to combining enzymatic and transition metal catalysis
    • Wang Z.J., Clary K.N., Bergman R.G., Raymond K.N., Toste F.D. A supramolecular approach to combining enzymatic and transition metal catalysis. Nat. Chem. 2013, 5:100-103.
    • (2013) Nat. Chem. , vol.5 , pp. 100-103
    • Wang, Z.J.1    Clary, K.N.2    Bergman, R.G.3    Raymond, K.N.4    Toste, F.D.5
  • 3
    • 78449259734 scopus 로고    scopus 로고
    • Biocatalysis-key to sustainable industrial chemistry
    • Wohlgemuth R. Biocatalysis-key to sustainable industrial chemistry. Curr. Opin. Biotechnol. 2010, 21:713-724.
    • (2010) Curr. Opin. Biotechnol. , vol.21 , pp. 713-724
    • Wohlgemuth, R.1
  • 4
    • 84901483425 scopus 로고    scopus 로고
    • Recent advances in engineering proteins for biocatalysis
    • Li Y., Cirino P.C. Recent advances in engineering proteins for biocatalysis. Biotechnol. Bioeng. 2014, 111:1273-1287.
    • (2014) Biotechnol. Bioeng. , vol.111 , pp. 1273-1287
    • Li, Y.1    Cirino, P.C.2
  • 5
    • 78349313517 scopus 로고    scopus 로고
    • Beyond directed evolution-semi-rational protein engineering and design
    • Lutz S. Beyond directed evolution-semi-rational protein engineering and design. Curr. Opin. Biotechnol. 2010, 21:734-743.
    • (2010) Curr. Opin. Biotechnol. , vol.21 , pp. 734-743
    • Lutz, S.1
  • 8
    • 85027946164 scopus 로고    scopus 로고
    • Immobilizing systems biocatalysis for the selective oxidation of glycerol coupled to in situ cofactor recycling and hydrogen peroxide elimination
    • Rocha-Martin J., Acosta A., Guisan J.M., Lõpez-Gallego F. Immobilizing systems biocatalysis for the selective oxidation of glycerol coupled to in situ cofactor recycling and hydrogen peroxide elimination. ChemCatChem 2015, 7:1939-1947.
    • (2015) ChemCatChem , vol.7 , pp. 1939-1947
    • Rocha-Martin, J.1    Acosta, A.2    Guisan, J.M.3    Lõpez-Gallego, F.4
  • 9
    • 84943348170 scopus 로고    scopus 로고
    • Design of artificial metabolisms in layered nanomaterials for the enzymatic synthesis of phosphorylated sugars
    • Mahdi R., Guérard-Hélaine C., Prévot V., deBerardinis V., Forano C., Lemaire M. Design of artificial metabolisms in layered nanomaterials for the enzymatic synthesis of phosphorylated sugars. ChemCatChem 2015, 7:3110-3115.
    • (2015) ChemCatChem , vol.7 , pp. 3110-3115
    • Mahdi, R.1    Guérard-Hélaine, C.2    Prévot, V.3    deBerardinis, V.4    Forano, C.5    Lemaire, M.6
  • 10
    • 0024029957 scopus 로고
    • Aldehyde-agarose gels as activated supports for immobilization-stabilization of enzymes
    • Guisán J.M. Aldehyde-agarose gels as activated supports for immobilization-stabilization of enzymes. Enzyme Microb. Technol. 1988, 10:375-382.
    • (1988) Enzyme Microb. Technol. , vol.10 , pp. 375-382
    • Guisán, J.M.1
  • 11
    • 82955162467 scopus 로고    scopus 로고
    • Characterization and further stabilization of a new anti-prelog specific alcohol dehydrogenase from Thermus thermophilus HB27 for asymmetric reduction of carbonyl compounds
    • Rocha-Martín J., Vega D., Bolivar J.M., Hidalgo A., Berenguer J., Guisán J.M., López-Gallego F. Characterization and further stabilization of a new anti-prelog specific alcohol dehydrogenase from Thermus thermophilus HB27 for asymmetric reduction of carbonyl compounds. Bioresour. Technol. 2012, 103:343-350.
    • (2012) Bioresour. Technol. , vol.103 , pp. 343-350
    • Rocha-Martín, J.1    Vega, D.2    Bolivar, J.M.3    Hidalgo, A.4    Berenguer, J.5    Guisán, J.M.6    López-Gallego, F.7
  • 17
    • 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
  • 18
    • 84930216176 scopus 로고    scopus 로고
    • Asymmetric reduction of ketones and β-keto esters by (S)-1-phenylethanol dehydrogenase from denitrifying bacterium Aromatoleum aromaticum
    • Dudzik A., Snoch W., Borowiecki P., Opalinska-Piskorz J., Witko M., Heider J., Szaleniec M. Asymmetric reduction of ketones and β-keto esters by (S)-1-phenylethanol dehydrogenase from denitrifying bacterium Aromatoleum aromaticum. Appl. Microbiol. Biotechnol. 2015, 99:5055-5069.
    • (2015) Appl. Microbiol. Biotechnol. , vol.99 , pp. 5055-5069
    • Dudzik, A.1    Snoch, W.2    Borowiecki, P.3    Opalinska-Piskorz, J.4    Witko, M.5    Heider, J.6    Szaleniec, M.7
  • 19
    • 84888083751 scopus 로고    scopus 로고
    • Kinetic characterization of Rhodococcus ruber DSM 44541 alcohol dehydrogenase A
    • Hamnevik E., Blikstad C., Norrehed S., Widersten M. Kinetic characterization of Rhodococcus ruber DSM 44541 alcohol dehydrogenase A. J. Mol. Catal. B: Enzym. 2014, 99:68-78.
    • (2014) J. Mol. Catal. B: Enzym. , vol.99 , pp. 68-78
    • Hamnevik, E.1    Blikstad, C.2    Norrehed, S.3    Widersten, M.4
  • 21
    • 0037415359 scopus 로고    scopus 로고
    • NADH oxidase from Lactobacillus brevis: a new catalyst for the regeneration of NAD
    • Geueke B., Riebel B., Hummel W. NADH oxidase from Lactobacillus brevis: a new catalyst for the regeneration of NAD. Enzyme Microb. Technol. 2003, 32:205-211.
    • (2003) Enzyme Microb. Technol. , vol.32 , pp. 205-211
    • Geueke, B.1    Riebel, B.2    Hummel, W.3
  • 22
    • 0022179287 scopus 로고
    • The active center of catalase
    • Fita I., Rossmann M.G. The active center of catalase. J. Mol. Biol. 1985, 185:21-37.
    • (1985) J. Mol. Biol. , vol.185 , pp. 21-37
    • Fita, I.1    Rossmann, M.G.2
  • 23
    • 84927945903 scopus 로고    scopus 로고
    • Enantioselective cascade biocatalysis via epoxide hydrolysis and alcohol oxidation: one-pot synthesis of (R)-α-hydroxy ketones from meso- or racemic epoxides
    • Zhang J., Wu S., Wu J., Li Z. Enantioselective cascade biocatalysis via epoxide hydrolysis and alcohol oxidation: one-pot synthesis of (R)-α-hydroxy ketones from meso- or racemic epoxides. ACS Catal. 2015, 5:51-58.
    • (2015) ACS Catal. , vol.5 , pp. 51-58
    • Zhang, J.1    Wu, S.2    Wu, J.3    Li, Z.4
  • 24
    • 1842583994 scopus 로고    scopus 로고
    • Recent advances in the biocatalytic reduction of ketones and oxidation of sec-alcohols
    • Kroutil W., Mang H., Edegger K., Faber K. Recent advances in the biocatalytic reduction of ketones and oxidation of sec-alcohols. Curr. Opin. Chem. Biol. 2004, 8:120-126.
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 120-126
    • Kroutil, W.1    Mang, H.2    Edegger, K.3    Faber, K.4
  • 28
    • 0037095620 scopus 로고    scopus 로고
    • Diversity of properties among catalases
    • Switala J., Loewen P.C. Diversity of properties among catalases. Arch. Biochem. Biophys. 2002, 401:145-154.
    • (2002) Arch. Biochem. Biophys. , vol.401 , pp. 145-154
    • Switala, J.1    Loewen, P.C.2
  • 31
    • 84889780415 scopus 로고    scopus 로고
    • Escherichia coli/ADH-A: an all-inclusive catalyst for the selective biooxidation and deracemisation of secondary alcohols
    • Paul C.E., Lavandera I., Gotor-Fernández V., Kroutil W., Gotor V. Escherichia coli/ADH-A: an all-inclusive catalyst for the selective biooxidation and deracemisation of secondary alcohols. ChemCatChem 2013, 5:3875-3881.
    • (2013) ChemCatChem , vol.5 , pp. 3875-3881
    • Paul, C.E.1    Lavandera, I.2    Gotor-Fernández, V.3    Kroutil, W.4    Gotor, V.5
  • 32
    • 31044449586 scopus 로고    scopus 로고
    • Edible catalysts for clean chemical reactions: bioreduction of aromatic ketones and biooxidation of secondary alcohols using plants
    • Andrade L.H., Utsunomiya R.S., Omori A.T., Porto A.L.M., Comasseto J.V. Edible catalysts for clean chemical reactions: bioreduction of aromatic ketones and biooxidation of secondary alcohols using plants. J. Mol. Catal. B: Enzym. 2006, 38:84-90.
    • (2006) J. Mol. Catal. B: Enzym. , vol.38 , pp. 84-90
    • Andrade, L.H.1    Utsunomiya, R.S.2    Omori, A.T.3    Porto, A.L.M.4    Comasseto, J.V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.