메뉴 건너뛰기




Volumn 179, Issue 1, 2014, Pages 50-55

Supported liquid membrane as a novel tool for driving the equilibrium of ω-transaminase catalyzed asymmetric synthesis

Author keywords

Asymmetric synthesis; Chiral amines; In situ product removal; Supported liquid membrane; Transaminase

Indexed keywords

AMINES; ESCHERICHIA COLI; EXTRACTION; LIQUID MEMBRANE ELECTRODES; PACKED BEDS;

EID: 84897408319     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2014.03.022     Document Type: Article
Times cited : (49)

References (31)
  • 2
    • 77954791339 scopus 로고    scopus 로고
    • Transaminations with isopropyl amine: equilibrium displacement with yeast alcohol dehydrogenase coupled to in situ cofactor regeneration
    • Cassimjee K.E., Branneby C., Abedi V., Wells A., Berglund P. Transaminations with isopropyl amine: equilibrium displacement with yeast alcohol dehydrogenase coupled to in situ cofactor regeneration. Chem. Commun. 2010, 46:5569-5571.
    • (2010) Chem. Commun. , vol.46 , pp. 5569-5571
    • Cassimjee, K.E.1    Branneby, C.2    Abedi, V.3    Wells, A.4    Berglund, P.5
  • 3
    • 0033237245 scopus 로고    scopus 로고
    • A supported polymeric liquid membrane process for removal of carboxylic acids from a waste stream
    • Ho S.V. A supported polymeric liquid membrane process for removal of carboxylic acids from a waste stream. Environ. Prog. 1999, 18:273-279.
    • (1999) Environ. Prog. , vol.18 , pp. 273-279
    • Ho, S.V.1
  • 4
    • 70349631202 scopus 로고    scopus 로고
    • Biocatalytic routes to optically active amines
    • Höhne M., Bornscheuer U.T. Biocatalytic routes to optically active amines. Chemcatchem 2009, 1:42-51.
    • (2009) Chemcatchem , vol.1 , pp. 42-51
    • Höhne, M.1    Bornscheuer, U.T.2
  • 5
    • 48849087284 scopus 로고    scopus 로고
    • Efficient asymmetric synthesis of chiral amines by combining transaminase and pyruvate decarboxylase
    • Höhne M., Kühl S., Robins K., Bornscheuer U.T. Efficient asymmetric synthesis of chiral amines by combining transaminase and pyruvate decarboxylase. ChemBioChem 2008, 9:363-365.
    • (2008) ChemBioChem , vol.9 , pp. 363-365
    • Höhne, M.1    Kühl, S.2    Robins, K.3    Bornscheuer, U.T.4
  • 6
    • 0034842958 scopus 로고    scopus 로고
    • Membrane extraction in analytical chemistry
    • Jönsson J.A., Mathiasson L. Membrane extraction in analytical chemistry. J. Sep. Sci. 2001, 24:495-507.
    • (2001) J. Sep. Sci. , vol.24 , pp. 495-507
    • Jönsson, J.A.1    Mathiasson, L.2
  • 8
    • 33846192862 scopus 로고    scopus 로고
    • Recent advances in supported liquid membrane technology
    • Kocherginsky N.M., Yang Q., Seelam L. Recent advances in supported liquid membrane technology. Sep. Purif. Technol. 2007, 53:171-177.
    • (2007) Sep. Purif. Technol. , vol.53 , pp. 171-177
    • Kocherginsky, N.M.1    Yang, Q.2    Seelam, L.3
  • 9
    • 56749102605 scopus 로고    scopus 로고
    • Asymmetric synthesis of optically pure pharmacologically relevant amines employing omega-transaminases
    • Koszelewski D., Lavandera I.n.Clay D., Rozzell D., Kroutil W. Asymmetric synthesis of optically pure pharmacologically relevant amines employing omega-transaminases. Adv. Synth. Catal. 2008, 350:2761-2766.
    • (2008) Adv. Synth. Catal. , vol.350 , pp. 2761-2766
    • Koszelewski, D.1    Lavandera I.n.Clay, D.2    Rozzell, D.3    Kroutil, W.4
  • 10
    • 77953120732 scopus 로고    scopus 로고
    • Omega-Transaminases for the synthesis of non-racemic alpha-chiral primary amines
    • Koszelewski D., Tauber K., Faber K., Kroutil W. omega-Transaminases for the synthesis of non-racemic alpha-chiral primary amines. Trends Biotechnol. 2010, 28:324-332.
    • (2010) Trends Biotechnol. , vol.28 , pp. 324-332
    • Koszelewski, D.1    Tauber, K.2    Faber, K.3    Kroutil, W.4
  • 12
    • 34548314434 scopus 로고    scopus 로고
    • Characterization of free and immobilized (S)-aminotransferase for acetophenone production
    • Martin A.R., Shonnard D., Pannuri S., Kamat S. Characterization of free and immobilized (S)-aminotransferase for acetophenone production. Appl. Microbiol. Biotechnol. 2007, 76:843-851.
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 843-851
    • Martin, A.R.1    Shonnard, D.2    Pannuri, S.3    Kamat, S.4
  • 13
    • 84861837623 scopus 로고    scopus 로고
    • Omega-Transaminases for the production of optically pure amines and unnatural amino acids
    • Mathew S., Yun H. omega-Transaminases for the production of optically pure amines and unnatural amino acids. ACS Catal. 2012, 2:993-1001.
    • (2012) ACS Catal. , vol.2 , pp. 993-1001
    • Mathew, S.1    Yun, H.2
  • 15
    • 84872658954 scopus 로고    scopus 로고
    • State-of-the-art review on hollow fibre contactor technology and membrane-based extraction processes
    • Pabby A.K., Sastre A.M. State-of-the-art review on hollow fibre contactor technology and membrane-based extraction processes. J. Membr. Sci. 2013, 430:263-303.
    • (2013) J. Membr. Sci. , vol.430 , pp. 263-303
    • Pabby, A.K.1    Sastre, A.M.2
  • 16
    • 84870174513 scopus 로고    scopus 로고
    • Supported liquid membrane principle and its practices: a short review
    • Parhi P.K. Supported liquid membrane principle and its practices: a short review. J. Chem. 2013, 2013:11.
    • (2013) J. Chem. , vol.2013 , pp. 11
    • Parhi, P.K.1
  • 17
    • 33846197938 scopus 로고    scopus 로고
    • Biocatalysis for pharmaceutical intermediates: the future is now
    • Pollard D.J., Woodley J.M. Biocatalysis for pharmaceutical intermediates: the future is now. Trends Biotechnol. 2007, 25:66-73.
    • (2007) Trends Biotechnol. , vol.25 , pp. 66-73
    • Pollard, D.J.1    Woodley, J.M.2
  • 18
    • 84876725866 scopus 로고    scopus 로고
    • Chitosan flocculation: an effective method for immobilization of E. coli for biocatalytic processes
    • Rehn G., Grey C., Adlercreutz P. Chitosan flocculation: an effective method for immobilization of E. coli for biocatalytic processes. J. Biotechnol. 2013, 165:138-144.
    • (2013) J. Biotechnol. , vol.165 , pp. 138-144
    • Rehn, G.1    Grey, C.2    Adlercreutz, P.3
  • 19
    • 84861330688 scopus 로고    scopus 로고
    • Activity and stability of different immobilized preparations of recombinant E. coli cells containing ω-transaminase
    • Rehn G., Grey C., Branneby C., Lindberg L., Adlercreutz P. Activity and stability of different immobilized preparations of recombinant E. coli cells containing ω-transaminase. Process Biochem. 2012, 47:1129-1134.
    • (2012) Process Biochem. , vol.47 , pp. 1129-1134
    • Rehn, G.1    Grey, C.2    Branneby, C.3    Lindberg, L.4    Adlercreutz, P.5
  • 21
    • 80052815301 scopus 로고    scopus 로고
    • Enzymatic asymmetric synthesis of enantiomerically pure aliphatic, aromatic and arylaliphatic amines with (R)-selective amine transaminases
    • Schätzle S., Steffen-Munsberg F., Thontowi A., Höhne M., Robins K., Bornscheuer U.T. Enzymatic asymmetric synthesis of enantiomerically pure aliphatic, aromatic and arylaliphatic amines with (R)-selective amine transaminases. Adv. Synth. Catal. 2011, 353:2439-2445.
    • (2011) Adv. Synth. Catal. , vol.353 , pp. 2439-2445
    • Schätzle, S.1    Steffen-Munsberg, F.2    Thontowi, A.3    Höhne, M.4    Robins, K.5    Bornscheuer, U.T.6
  • 22
    • 0033589366 scopus 로고    scopus 로고
    • Asymmetric synthesis of chiral amines with omega-transaminase
    • Shin J.-S., Kim B.-G. Asymmetric synthesis of chiral amines with omega-transaminase. Biotechnol. Bioeng. 1999, 65:206-211.
    • (1999) Biotechnol. Bioeng. , vol.65 , pp. 206-211
    • Shin, J.-S.1    Kim, B.-G.2
  • 23
    • 0035810702 scopus 로고    scopus 로고
    • Kinetic resolution of chiral amines with omega-transaminase using an enzyme-membrane reactor
    • Shin J.-S., Kim B.-G., Liese A., Wandrey C. Kinetic resolution of chiral amines with omega-transaminase using an enzyme-membrane reactor. Biotechnol. Bioeng. 2001, 73:179-187.
    • (2001) Biotechnol. Bioeng. , vol.73 , pp. 179-187
    • Shin, J.-S.1    Kim, B.-G.2    Liese, A.3    Wandrey, C.4
  • 24
    • 0343907783 scopus 로고    scopus 로고
    • Kinetic resolution of alpha-methylbenzylamine with omega-transaminase screened from soil microorganisms: application of a biphasic system to overcame product inhibition
    • Shin J.S., Kim B.G. Kinetic resolution of alpha-methylbenzylamine with omega-transaminase screened from soil microorganisms: application of a biphasic system to overcame product inhibition. Biotechnol. Bioeng. 1997, 55:348-358.
    • (1997) Biotechnol. Bioeng. , vol.55 , pp. 348-358
    • Shin, J.S.1    Kim, B.G.2
  • 25
    • 0035812420 scopus 로고    scopus 로고
    • Kinetic resolution of chiral amines using packed-bed reactor
    • Shin J.S., Kim B.G., Shin D.H. Kinetic resolution of chiral amines using packed-bed reactor. Enzyme Microb. Technol. 2001, 29:232-239.
    • (2001) Enzyme Microb. Technol. , vol.29 , pp. 232-239
    • Shin, J.S.1    Kim, B.G.2    Shin, D.H.3
  • 26
    • 77149171446 scopus 로고    scopus 로고
    • Efficient production of enantiomerically pure chiral amines at concentrations of 50g/L using transaminases
    • Truppo M.D., Rozzell J.D., Turner N.J. Efficient production of enantiomerically pure chiral amines at concentrations of 50g/L using transaminases. Org. Process Res. Dev. 2010, 14:234-237.
    • (2010) Org. Process Res. Dev. , vol.14 , pp. 234-237
    • Truppo, M.D.1    Rozzell, J.D.2    Turner, N.J.3
  • 28
    • 33751185588 scopus 로고    scopus 로고
    • Copper recovery and spent ammoniacal etchant regeneration based on hollow fiber supported liquid membrane technology: From bench-scale to pilot-scale tests
    • Yang Q., Kocherginsky N.M. Copper recovery and spent ammoniacal etchant regeneration based on hollow fiber supported liquid membrane technology: From bench-scale to pilot-scale tests. J. Membr. Sci. 2006, 286:301-309.
    • (2006) J. Membr. Sci. , vol.286 , pp. 301-309
    • Yang, Q.1    Kocherginsky, N.M.2
  • 29
    • 34047159317 scopus 로고    scopus 로고
    • Covalent immobilization of ω-transaminase from Vibrio fluvialis JS17 on chitosan beads
    • Yi S.S., Lee C.W., Kim J., Kyung D., Kim B.G., Lee Y.S. Covalent immobilization of ω-transaminase from Vibrio fluvialis JS17 on chitosan beads. Process Biochem. 2007, 42:895-898.
    • (2007) Process Biochem. , vol.42 , pp. 895-898
    • Yi, S.S.1    Lee, C.W.2    Kim, J.3    Kyung, D.4    Kim, B.G.5    Lee, Y.S.6
  • 30
    • 4644286944 scopus 로고    scopus 로고
    • Kinetic resolution of (R,S)-sec-butylamine using omega-transaminase from Vibrio fluvialis JS17 under reduced pressure
    • Yun H., Cho B.-K., Kim B.-G. Kinetic resolution of (R,S)-sec-butylamine using omega-transaminase from Vibrio fluvialis JS17 under reduced pressure. Biotechnol. Bioeng. 2004, 87:772-778.
    • (2004) Biotechnol. Bioeng. , vol.87 , pp. 772-778
    • Yun, H.1    Cho, B.-K.2    Kim, B.-G.3
  • 31
    • 56749153559 scopus 로고    scopus 로고
    • Asymmetric synthesis of (S)-alpha-methylbenzylamine by recombinant Escherichia coli co-expressing omega-transaminase and acetolactate synthase
    • Yun H., Kim B.-G. Asymmetric synthesis of (S)-alpha-methylbenzylamine by recombinant Escherichia coli co-expressing omega-transaminase and acetolactate synthase. Biosci. Biotechnol. Biochem. 2008, 72:3030-3033.
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , pp. 3030-3033
    • Yun, H.1    Kim, B.-G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.