메뉴 건너뛰기




Volumn 29, Issue 2, 2012, Pages 227-234

Continuous steroid biotransformations in microchannel reactors

Author keywords

[No Author keywords available]

Indexed keywords

AQUEOUS PHASE; BIOPROCESSES; CHOLESTEROL OXIDASE; CONTINUOUS PRODUCTION; CONVERSION YIELD; ENZYMATIC OXIDATIONS; GAINING MOMENTUM; MICRO CHANNEL REACTORS; MODES OF OPERATION; ORGANIC PHASE; PLUG FLOW REACTOR; PROCESS INTENSIFICATION; RESIDENCE TIME; STIRRED TANK; TWO PHASE SYSTEMS;

EID: 84855801679     PISSN: 18716784     EISSN: 18764347     Source Type: Journal    
DOI: 10.1016/j.nbt.2011.10.001     Document Type: Article
Times cited : (21)

References (44)
  • 1
    • 77950900004 scopus 로고    scopus 로고
    • Miniaturization in biocatalysis
    • Fernandes P. Miniaturization in biocatalysis. Int. J. Mol. Sci. 2010, 11:858-879.
    • (2010) Int. J. Mol. Sci. , vol.11 , pp. 858-879
    • Fernandes, P.1
  • 2
    • 20444402256 scopus 로고    scopus 로고
    • Harnessing microreactions
    • Thayer A.M. Harnessing microreactions. Chem. Eng. News 2005, 83:43-52.
    • (2005) Chem. Eng. News , vol.83 , pp. 43-52
    • Thayer, A.M.1
  • 3
    • 79955623916 scopus 로고    scopus 로고
    • Green and sustainable chemical synthesis using flow microreactors
    • Yoshida J-i., et al. Green and sustainable chemical synthesis using flow microreactors. ChemSusChem 2011, 4:331-340.
    • (2011) ChemSusChem , vol.4 , pp. 331-340
    • Yoshida, J.-I.1
  • 4
    • 33846558913 scopus 로고    scopus 로고
    • Recent advances in synthetic micro reaction technology
    • Watts P., Wiles C. Recent advances in synthetic micro reaction technology. Chem. Commun. (Camb.) 2007, 5:443-467.
    • (2007) Chem. Commun. (Camb.) , vol.5 , pp. 443-467
    • Watts, P.1    Wiles, C.2
  • 5
    • 79959316650 scopus 로고    scopus 로고
    • Biotransformations in microstructured reactors: more than flowing with the stream?
    • Bolivar J.M., et al. Biotransformations in microstructured reactors: more than flowing with the stream?. Trends Biotechnol. 2011, 29:333-342.
    • (2011) Trends Biotechnol. , vol.29 , pp. 333-342
    • Bolivar, J.M.1
  • 6
    • 56249091412 scopus 로고    scopus 로고
    • Enzymatic processing in microfluidic reactors
    • Miyazaki M., et al. Enzymatic processing in microfluidic reactors. Biotechnol. Genet. Eng. Rev. 2008, 25:405-428.
    • (2008) Biotechnol. Genet. Eng. Rev. , vol.25 , pp. 405-428
    • Miyazaki, M.1
  • 7
    • 42949124472 scopus 로고    scopus 로고
    • Enzymatic reactions in microfluidic devices: Michaelis-Menten kinetics
    • Ristenpart W.D., et al. Enzymatic reactions in microfluidic devices: Michaelis-Menten kinetics. Anal. Chem. 2008, 80:3270-3276.
    • (2008) Anal. Chem. , vol.80 , pp. 3270-3276
    • Ristenpart, W.D.1
  • 8
    • 39549091529 scopus 로고    scopus 로고
    • Comparison of two-phase lipase-catalyzed esterification on micro and bench scale
    • Swarts J.W., et al. Comparison of two-phase lipase-catalyzed esterification on micro and bench scale. Biotechnol. Bioeng. 2008, 99:855-861.
    • (2008) Biotechnol. Bioeng. , vol.99 , pp. 855-861
    • Swarts, J.W.1
  • 9
    • 1842834071 scopus 로고    scopus 로고
    • Enzymatic degradation of p-chlorophenol in a two-phase flow microchannel system
    • Maruyama T., et al. Enzymatic degradation of p-chlorophenol in a two-phase flow microchannel system. Lab Chip 2003, 3:308-312.
    • (2003) Lab Chip , vol.3 , pp. 308-312
    • Maruyama, T.1
  • 10
    • 69249208514 scopus 로고    scopus 로고
    • Modelling and experimental studies on lipase-catalyzed isoamyl acetate synthesis in a microreactor
    • Žnidaršič-Plazl P., Plazl I. Modelling and experimental studies on lipase-catalyzed isoamyl acetate synthesis in a microreactor. Process Biochem. 2009, 44:1115-1121.
    • (2009) Process Biochem. , vol.44 , pp. 1115-1121
    • Žnidaršič-Plazl, P.1    Plazl, I.2
  • 11
    • 77954818551 scopus 로고    scopus 로고
    • On the feasibility of in situ steroid biotransformation and product recovery in microchannels
    • Marques M.P.C., et al. On the feasibility of in situ steroid biotransformation and product recovery in microchannels. Chem. Eng. J. 2010, 160:708-714.
    • (2010) Chem. Eng. J. , vol.160 , pp. 708-714
    • Marques, M.P.C.1
  • 12
    • 0034175781 scopus 로고    scopus 로고
    • Cholesterol oxidase: sources, physical properties and analytical applications
    • MacLachlan J., et al. Cholesterol oxidase: sources, physical properties and analytical applications. J. Steroid Biochem. Mol. Biol. 2000, 72:169-195.
    • (2000) J. Steroid Biochem. Mol. Biol. , vol.72 , pp. 169-195
    • MacLachlan, J.1
  • 13
    • 84957791072 scopus 로고
    • The microbiological degradation of steroids: 4. Fission of the steroid molecule
    • Turfitt G.E. The microbiological degradation of steroids: 4. Fission of the steroid molecule. Biochem. J. 1948, 42:376-383.
    • (1948) Biochem. J. , vol.42 , pp. 376-383
    • Turfitt, G.E.1
  • 14
    • 47549115628 scopus 로고    scopus 로고
    • Microbial cholesterol oxidases: bioconversion enzymes or signal proteins?
    • Aparicio J.F., Martin J.F. Microbial cholesterol oxidases: bioconversion enzymes or signal proteins?. Mol. BioSyst. 2008, 4:804-809.
    • (2008) Mol. BioSyst. , vol.4 , pp. 804-809
    • Aparicio, J.F.1    Martin, J.F.2
  • 15
    • 0000614673 scopus 로고
    • Enzymic oxidation of cholesterol in reverse micelles
    • Gupte A., et al. Enzymic oxidation of cholesterol in reverse micelles. Ind. Eng. Chem. Res. 1995, 34:2910-2922.
    • (1995) Ind. Eng. Chem. Res. , vol.34 , pp. 2910-2922
    • Gupte, A.1
  • 16
    • 0000886743 scopus 로고
    • Cholesterol oxidase in microemulsion - enzymatic-activity on a substrate of low water solubility and inactivation by hydrogen-peroxide
    • Lee K.M., Biellmann J.F. Cholesterol oxidase in microemulsion - enzymatic-activity on a substrate of low water solubility and inactivation by hydrogen-peroxide. Bioorg. Chem. 1986, 14:262-273.
    • (1986) Bioorg. Chem. , vol.14 , pp. 262-273
    • Lee, K.M.1    Biellmann, J.F.2
  • 17
    • 33746284567 scopus 로고    scopus 로고
    • The Barton reaction using a microreactor and black light. Continuous-flow synthesis of a key steroid intermediate for an endothelin receptor antagonist
    • Sugimoto A., et al. The Barton reaction using a microreactor and black light. Continuous-flow synthesis of a key steroid intermediate for an endothelin receptor antagonist. Tetrahedron Lett. 2006, 47:6197-6200.
    • (2006) Tetrahedron Lett. , vol.47 , pp. 6197-6200
    • Sugimoto, A.1
  • 18
    • 78049272756 scopus 로고    scopus 로고
    • Development of a continuous steroid biotransformation process and product extraction within microchannel system
    • Žnidaršič-Plazl P., Plazl I. Development of a continuous steroid biotransformation process and product extraction within microchannel system. Catal. Today 2010, 157:315-320.
    • (2010) Catal. Today , vol.157 , pp. 315-320
    • Žnidaršič-Plazl, P.1    Plazl, I.2
  • 19
    • 67449116849 scopus 로고    scopus 로고
    • A simple method for biocatalyst immobilization using PVA-based hydrogel particles
    • Fernandes P., et al. A simple method for biocatalyst immobilization using PVA-based hydrogel particles. J. Chem. Technol. Biotechnol. 2009, 84:561-564.
    • (2009) J. Chem. Technol. Biotechnol. , vol.84 , pp. 561-564
    • Fernandes, P.1
  • 20
    • 77954268016 scopus 로고    scopus 로고
    • Scaling-up of complex whole-cell bioconversions in conventional and non-conventional media
    • Marques M.P.C., et al. Scaling-up of complex whole-cell bioconversions in conventional and non-conventional media. Biotechnol. Bioeng. 2010, 106:619-626.
    • (2010) Biotechnol. Bioeng. , vol.106 , pp. 619-626
    • Marques, M.P.C.1
  • 21
    • 0034333437 scopus 로고    scopus 로고
    • Kinetics of thermal deactivation of enzymes: a simple three parameters phenomenological model can describe the decay of enzyme activity, irrespectively of the mechanism
    • Aymard C., Belarbi A. Kinetics of thermal deactivation of enzymes: a simple three parameters phenomenological model can describe the decay of enzyme activity, irrespectively of the mechanism. Enzyme Microb. Technol. 2000, 27:612-618.
    • (2000) Enzyme Microb. Technol. , vol.27 , pp. 612-618
    • Aymard, C.1    Belarbi, A.2
  • 22
    • 36049037827 scopus 로고    scopus 로고
    • Rapid kinetic microassay for catalase activity
    • Li Y., Schellhorn H.E. Rapid kinetic microassay for catalase activity. J. Biomol. Tech. 2007, 18:185-187.
    • (2007) J. Biomol. Tech. , vol.18 , pp. 185-187
    • Li, Y.1    Schellhorn, H.E.2
  • 23
    • 34347258900 scopus 로고    scopus 로고
    • Steroid extraction in a microchannel system - mathematical modelling and experiments
    • Žnidaršič-Plazl P., Plazl I. Steroid extraction in a microchannel system - mathematical modelling and experiments. Lab Chip 2007, 7:883-889.
    • (2007) Lab Chip , vol.7 , pp. 883-889
    • ŽnidarŠič-Plazl, P.1    Plazl, I.2
  • 24
    • 0001807173 scopus 로고
    • Design and operation of immobilized enzyme reactors
    • Springer
    • Pitcher W. Design and operation of immobilized enzyme reactors. Advances in Biochemical Engineering 1978, Vol. 10. Springer, pp. 1-26.
    • (1978) Advances in Biochemical Engineering , vol.10 , pp. 1-26
    • Pitcher, W.1
  • 25
    • 0011955625 scopus 로고
    • Use of titanium species for the immobilization of cells
    • Kennedy J.F., Cabral J.M.S. Use of titanium species for the immobilization of cells. Transit. Met. Chem. (London) 1990, 15:197-207.
    • (1990) Transit. Met. Chem. (London) , vol.15 , pp. 197-207
    • Kennedy, J.F.1    Cabral, J.M.S.2
  • 26
    • 72849126049 scopus 로고    scopus 로고
    • Lipase-catalyzed synthesis of isoamyl acetate in an ionic liquid/n-heptane two-phase system at the microreactor scale
    • Pohar A., et al. Lipase-catalyzed synthesis of isoamyl acetate in an ionic liquid/n-heptane two-phase system at the microreactor scale. Lab Chip 2009, 9:3385-3390.
    • (2009) Lab Chip , vol.9 , pp. 3385-3390
    • Pohar, A.1
  • 27
    • 79955971581 scopus 로고    scopus 로고
    • L-Malic acid production within a microreactor with surface immobilised fumarase
    • Stojkovič G., et al. l-Malic acid production within a microreactor with surface immobilised fumarase. Microfluid. Nanofluid. 2011, 10:627-635.
    • (2011) Microfluid. Nanofluid. , vol.10 , pp. 627-635
    • Stojkovič, G.1
  • 28
    • 33847288821 scopus 로고    scopus 로고
    • Molecular hydrogel-immobilized enzymes exhibit superactivity and high stability in organic solvents
    • (and references therein)
    • Wang Q.G., et al. Molecular hydrogel-immobilized enzymes exhibit superactivity and high stability in organic solvents. Chem. Commun. (Camb.) 2007, 10:1032-1034. (and references therein).
    • (2007) Chem. Commun. (Camb.) , vol.10 , pp. 1032-1034
    • Wang, Q.G.1
  • 29
    • 50849139867 scopus 로고    scopus 로고
    • Enzyme stability and stabilization - aqueous and non-aqueous environment
    • Iyer P.V., Ananthanarayan L. Enzyme stability and stabilization - aqueous and non-aqueous environment. Process Biochem. 2008, 43:1019-1032.
    • (2008) Process Biochem. , vol.43 , pp. 1019-1032
    • Iyer, P.V.1    Ananthanarayan, L.2
  • 30
    • 0028175482 scopus 로고
    • 11 alpha-Hydroxylation of progesterone in biphasic media using alginate-entrapped Aspergillus ochraceus gel beads coated with polyurea
    • Houng J.Y., et al. 11 alpha-Hydroxylation of progesterone in biphasic media using alginate-entrapped Aspergillus ochraceus gel beads coated with polyurea. Enzyme Microb. Technol. 1994, 16:485-491.
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 485-491
    • Houng, J.Y.1
  • 31
    • 77649183889 scopus 로고    scopus 로고
    • Development of a monolith based immobilized lipase micro-reactor for biocatalytic reactions in a biphasic mobile system
    • He P., et al. Development of a monolith based immobilized lipase micro-reactor for biocatalytic reactions in a biphasic mobile system. Process Biochem. 2010, 45:593-597.
    • (2010) Process Biochem. , vol.45 , pp. 593-597
    • He, P.1
  • 32
    • 78049235505 scopus 로고    scopus 로고
    • Lipase immobilized microstructured fiber based flow-through microreactor for facile lipid transformations
    • Mugo S.M., Ayton K. Lipase immobilized microstructured fiber based flow-through microreactor for facile lipid transformations. J. Mol. Catal. B: Enzym. 2010, 67:202-207.
    • (2010) J. Mol. Catal. B: Enzym. , vol.67 , pp. 202-207
    • Mugo, S.M.1    Ayton, K.2
  • 33
    • 0002994075 scopus 로고
    • The viscosity of a fluid containing small drops of another fluid
    • Taylor G.I. The viscosity of a fluid containing small drops of another fluid. Proc. R. Soc. Lond. Ser. A 1932, 138:41-48.
    • (1932) Proc. R. Soc. Lond. Ser. A , vol.138 , pp. 41-48
    • Taylor, G.I.1
  • 34
    • 80052467173 scopus 로고    scopus 로고
    • Biotransformation in a microreactor: new method for production of hexanal
    • Salic A., et al. Biotransformation in a microreactor: new method for production of hexanal. Biotechnol. Bioprocess Eng. 2011, 16:495-504.
    • (2011) Biotechnol. Bioprocess Eng. , vol.16 , pp. 495-504
    • Salic, A.1
  • 35
    • 79959636155 scopus 로고    scopus 로고
    • Gas-liquid and liquid-liquid mass transfer in microstructured reactors
    • Kashid M.N., et al. Gas-liquid and liquid-liquid mass transfer in microstructured reactors. Chem. Eng. Sci. 2011, 66:3876-3897.
    • (2011) Chem. Eng. Sci. , vol.66 , pp. 3876-3897
    • Kashid, M.N.1
  • 36
    • 80052804710 scopus 로고    scopus 로고
    • Miniaturizing biocatalysis: enzyme-catalyzed reactions in an aqueous/organic segmented flow capillary microreactor
    • Karande R., et al. Miniaturizing biocatalysis: enzyme-catalyzed reactions in an aqueous/organic segmented flow capillary microreactor. Adv. Synth. Catal. 2011, 353:2511-2521.
    • (2011) Adv. Synth. Catal. , vol.353 , pp. 2511-2521
    • Karande, R.1
  • 37
    • 75349100918 scopus 로고    scopus 로고
    • Organic solvent-tolerant enzymes
    • (and references therein)
    • Doukyu N., Ogino H. Organic solvent-tolerant enzymes. Biochem. Eng. J. 2010, 48:270-282. (and references therein).
    • (2010) Biochem. Eng. J. , vol.48 , pp. 270-282
    • Doukyu, N.1    Ogino, H.2
  • 38
    • 79951768234 scopus 로고    scopus 로고
    • Effects of shear on proteins in solution
    • (and references therein)
    • Thomas C.R., Geer D. Effects of shear on proteins in solution. Biotechnol. Lett. 2011, 33:443-456. (and references therein).
    • (2011) Biotechnol. Lett. , vol.33 , pp. 443-456
    • Thomas, C.R.1    Geer, D.2
  • 39
    • 63249123191 scopus 로고    scopus 로고
    • Characterization and properties of catalase immobilized onto controlled pore glass and its application in batch and plug-flow type reactors
    • Alptekin Ö., et al. Characterization and properties of catalase immobilized onto controlled pore glass and its application in batch and plug-flow type reactors. J. Mol. Catal. B: Enzym. 2009, 58:124-131.
    • (2009) J. Mol. Catal. B: Enzym. , vol.58 , pp. 124-131
    • Alptekin, Ö.1
  • 40
    • 77951978040 scopus 로고    scopus 로고
    • Immobilization of catalase onto Eupergit C and its characterization
    • Alptekin Ö., et al. Immobilization of catalase onto Eupergit C and its characterization. J. Mol. Catal. B: Enzym. 2010, 64:177-183.
    • (2010) J. Mol. Catal. B: Enzym. , vol.64 , pp. 177-183
    • Alptekin, Ö.1
  • 42
    • 59649111091 scopus 로고    scopus 로고
    • Preparation of Cu(II) adsorbed chitosan beads for catalase immobilization
    • Çetinus S.A., et al. Preparation of Cu(II) adsorbed chitosan beads for catalase immobilization. Food Chem. 2009, 114:962-969.
    • (2009) Food Chem. , vol.114 , pp. 962-969
    • Çetinus, S.A.1
  • 43
    • 58149092996 scopus 로고    scopus 로고
    • Enhancing the thermal stability of lipases through mutagenesis and immobilization on zeolites
    • Costa L., et al. Enhancing the thermal stability of lipases through mutagenesis and immobilization on zeolites. Bioprocess Biosyst. Eng. 2009, 32:53-61.
    • (2009) Bioprocess Biosyst. Eng. , vol.32 , pp. 53-61
    • Costa, L.1
  • 44
    • 77955488553 scopus 로고    scopus 로고
    • A facile method for improving the covalent crosslinking adsorption process of catalase immobilization
    • Ran J., et al. A facile method for improving the covalent crosslinking adsorption process of catalase immobilization. Bioresour. Technol. 2010, 101:6285-6290.
    • (2010) Bioresour. Technol. , vol.101 , pp. 6285-6290
    • Ran, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.