메뉴 건너뛰기




Volumn 15, Issue 7, 2015, Pages 721-726

Compartmented microfluidic bioreactor system using magnetic enzyme immobilisates for fast small-scale biotransformation studies

Author keywords

Bioreactor; Immobilized microfluidic enzymatic reactor; Magnetic particles; Microfluidics; Two phase system

Indexed keywords

BIOCONVERSION; BIOREACTORS; ELECTROMAGNETIC FIELDS; ENZYME ACTIVITY; MAGNETITE; SEPARATION;

EID: 84945444868     PISSN: 16180240     EISSN: 16182863     Source Type: Journal    
DOI: 10.1002/elsc.201400171     Document Type: Article
Times cited : (13)

References (17)
  • 1
    • 33746695331 scopus 로고    scopus 로고
    • Cell-free expression systems for eukaryotic protein production
    • Endo, Y., Sawasaki, T., Cell-free expression systems for eukaryotic protein production. Curr. Opin. Biotechnol. 2006, 17, 373-80.
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 373-380
    • Endo, Y.1    Sawasaki, T.2
  • 2
    • 33745035191 scopus 로고    scopus 로고
    • Developing cell-free biology for industrial applications
    • Swartz, J., Developing cell-free biology for industrial applications. J. Industr. Microbiol. Biotechnol. 2006, 33, 476-485.
    • (2006) J. Industr. Microbiol. Biotechnol. , vol.33 , pp. 476-485
    • Swartz, J.1
  • 3
    • 77951152433 scopus 로고    scopus 로고
    • Deracemisation of mandelic acid to optically pure non-natural L-phenylglycine via a redox-neutral biocatalytic cascade
    • Resch, V., Fabian, W. M. F., Kroutil, W., Deracemisation of mandelic acid to optically pure non-natural L-phenylglycine via a redox-neutral biocatalytic cascade. Adv. Synth. Catal. 2010, 352, 993-997.
    • (2010) Adv. Synth. Catal. , vol.352 , pp. 993-997
    • Resch, V.1    Fabian, W.M.F.2    Kroutil, W.3
  • 4
    • 80052812654 scopus 로고    scopus 로고
    • Multi-enzymatic cascade reactions: overview and perspectives
    • Ricca, E., Brucher, B., Schrittwieser, J. H., Multi-enzymatic cascade reactions: overview and perspectives. Adv. Synth. Catal. 2011, 353, 2239-2262.
    • (2011) Adv. Synth. Catal. , vol.353 , pp. 2239-2262
    • Ricca, E.1    Brucher, B.2    Schrittwieser, J.H.3
  • 5
    • 84888840135 scopus 로고    scopus 로고
    • Characterization and multi-step transketolase-ω-transaminase bioconversions in an immobilized enzyme microreactor (IEMR) with packed tube
    • Halim, A. A., Szita, N., Baganz, F., Characterization and multi-step transketolase-ω-transaminase bioconversions in an immobilized enzyme microreactor (IEMR) with packed tube. J. Biotechnol. 2013, 168, 567-575.
    • (2013) J. Biotechnol. , vol.168 , pp. 567-575
    • Halim, A.A.1    Szita, N.2    Baganz, F.3
  • 6
    • 84881077335 scopus 로고    scopus 로고
    • Design of a prototype flow microreactor for synthetic biology in vitro
    • Boehm, C. R., Freemont, P. S., Ces, O., Design of a prototype flow microreactor for synthetic biology in vitro. Lab Chip 2013, 13, 3426-3432.
    • (2013) Lab Chip , vol.13 , pp. 3426-3432
    • Boehm, C.R.1    Freemont, P.S.2    Ces, O.3
  • 7
    • 79751471817 scopus 로고    scopus 로고
    • Fundamentals and applications of immobilized microfluidic enzymatic reactors
    • Matosevic, S., Szita, N., Baganz, F., Fundamentals and applications of immobilized microfluidic enzymatic reactors. J. Chem. Technol. Biotechnol. 2011, 86, 325-334.
    • (2011) J. Chem. Technol. Biotechnol. , vol.86 , pp. 325-334
    • Matosevic, S.1    Szita, N.2    Baganz, F.3
  • 8
    • 34547209337 scopus 로고    scopus 로고
    • Enzyme immobilization: the quest for optimum performance
    • Sheldon, R. A., Enzyme immobilization: the quest for optimum performance. Adv. Synth. Catal. 2007, 349, 1289-1307.
    • (2007) Adv. Synth. Catal. , vol.349 , pp. 1289-1307
    • Sheldon, R.A.1
  • 9
    • 84893589483 scopus 로고    scopus 로고
    • Immobilization of thermostable β-galactosidase on epoxy support and its use for lactose hydrolysis and galactooligosaccharides biosynthesis
    • Marín-Navarro, J., Talens-Perales, D., Oude-Vrielink, A., Cañada, F. J., et al., Immobilization of thermostable β-galactosidase on epoxy support and its use for lactose hydrolysis and galactooligosaccharides biosynthesis. World J. Microbiol. Biotechnol. 2014, 30, 989-998.
    • (2014) World J. Microbiol. Biotechnol. , vol.30 , pp. 989-998
    • Marín-Navarro, J.1    Talens-Perales, D.2    Oude-Vrielink, A.3    Cañada, F.J.4
  • 11
    • 4544333734 scopus 로고    scopus 로고
    • Preparation, characterization, and application of an enzyme-immobilized magnetic microreactor for flow injection analysis
    • Nomura, A., Shin, S., Mehdi, O. O., Kauffmann, J.-M., Preparation, characterization, and application of an enzyme-immobilized magnetic microreactor for flow injection analysis. Anal. Chem. 2004, 76, 5498-5502.
    • (2004) Anal. Chem. , vol.76 , pp. 5498-5502
    • Nomura, A.1    Shin, S.2    Mehdi, O.O.3    Kauffmann, J.-M.4
  • 12
    • 84897045524 scopus 로고    scopus 로고
    • Use of continuous magnetic extraction for removal of feedstock contaminants in flow-through mode
    • Paulus, A., Fischer, I., Hobley, T. J., Franzreb, M., Use of continuous magnetic extraction for removal of feedstock contaminants in flow-through mode. Sep. Purif. Technol. 2014, 127, 174-180.
    • (2014) Sep. Purif. Technol. , vol.127 , pp. 174-180
    • Paulus, A.1    Fischer, I.2    Hobley, T.J.3    Franzreb, M.4
  • 13
    • 7644232647 scopus 로고    scopus 로고
    • Manipulation of self-assembled structures of magnetic beads for microfluidic mixing and assaying
    • Rida, A., Gijs, M. A. M., Manipulation of self-assembled structures of magnetic beads for microfluidic mixing and assaying. Anal. Chem. 2004, 76, 6239-6246.
    • (2004) Anal. Chem. , vol.76 , pp. 6239-6246
    • Rida, A.1    Gijs, M.A.M.2
  • 14
    • 80052628402 scopus 로고    scopus 로고
    • Mathematical modeling and analysis of a magnetic nanoparticle-enhanced mixing in a microfluidic system using time-dependent magnetic field
    • Munir, A., Wang, J., Zhu, Z., Susan Zhou, H., Mathematical modeling and analysis of a magnetic nanoparticle-enhanced mixing in a microfluidic system using time-dependent magnetic field. IEEE Trans. Nanotechnol. 2011, 10, 953-961.
    • (2011) IEEE Trans. Nanotechnol. , vol.10 , pp. 953-961
    • Munir, A.1    Wang, J.2    Zhu, Z.3    Susan Zhou, H.4
  • 15
    • 0001727195 scopus 로고
    • An alternating-gradient magnetometer (invited)
    • Flanders, P. J., An alternating-gradient magnetometer (invited). J. Appl. Phys. 1988, 63, 3940.
    • (1988) J. Appl. Phys. , vol.63 , pp. 3940
    • Flanders, P.J.1
  • 16
    • 0001390198 scopus 로고
    • A new mechanism involving cyclic tautomers for the reaction with nucleophiles of the water-soluble peptide coupling reagent 1-ethyl-3-(3'-(dimethylamino) propyl) carbodiimide (EDC)
    • Williams, A., Ibrahim, I., A new mechanism involving cyclic tautomers for the reaction with nucleophiles of the water-soluble peptide coupling reagent 1-ethyl-3-(3'-(dimethylamino) propyl) carbodiimide (EDC). J. Am. Chem. Soc. 1981, 103, 7090-7095.
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 7090-7095
    • Williams, A.1    Ibrahim, I.2
  • 17
    • 84902688653 scopus 로고    scopus 로고
    • Direct quantification of immobilized enzymes by means of FTIR ATR spectroscopy-a process analytics tool for biotransformations applying non-porous magnetic enzyme carriers
    • Morhardt, C., Ketterer, B., Heißler, S., Franzreb, M., Direct quantification of immobilized enzymes by means of FTIR ATR spectroscopy-a process analytics tool for biotransformations applying non-porous magnetic enzyme carriers. J. Mol. Catal. B Enzym. 2014, 107, 55-63.
    • (2014) J. Mol. Catal. B Enzym. , vol.107 , pp. 55-63
    • Morhardt, C.1    Ketterer, B.2    Heißler, S.3    Franzreb, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.