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Volumn 48, Issue 10, 2013, Pages 1488-1494

Reusable ω-transaminase sol-gel catalyst for the preparation of amine enantiomers

Author keywords

Transaminase from Arthrobacter sp.; Amine enantiomers; Enzymatic stability enhancement; Enzyme immobilization; Kinetic resolution; Sol gel entrapment

Indexed keywords

AROMATIC PRIMARY AMINES; ARTHROBACTER SP; CATALYTIC BEHAVIOR; ENANTIOSELECTIVE REACTIONS; ENZYMATIC STABILITY; KINETIC RESOLUTION; SOL-GEL ENTRAPMENT; TETRAMETHOXYSILANE;

EID: 84883797768     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2013.07.021     Document Type: Article
Times cited : (28)

References (35)
  • 2
    • 70349631202 scopus 로고    scopus 로고
    • Biocatalytic routes to optically active amines
    • M. Höhne, and U.T. Bornscheuer Biocatalytic routes to optically active amines ChemCatChem 1 2009 42 51
    • (2009) ChemCatChem , vol.1 , pp. 42-51
    • Höhne, M.1    Bornscheuer, U.T.2
  • 3
    • 77953120732 scopus 로고    scopus 로고
    • ω-Transaminase for the synthesis of non-racemic α-chiral primary amines
    • D. Koszelewski, K. Tauber, K. Faber, and K. Kroutil ω-Transaminase for the synthesis of non-racemic α-chiral primary amines Trends in Biotechnology 28 2010 324 332
    • (2010) Trends in Biotechnology , vol.28 , pp. 324-332
    • Koszelewski, D.1    Tauber, K.2    Faber, K.3    Kroutil, K.4
  • 4
    • 77958007981 scopus 로고    scopus 로고
    • High-yield biocatalytic amination reactions in organic synthesis
    • J. Ward, and R. Wohlgemuth High-yield biocatalytic amination reactions in organic synthesis Current Organic Chemistry 14 2010 1914 1927
    • (2010) Current Organic Chemistry , vol.14 , pp. 1914-1927
    • Ward, J.1    Wohlgemuth, R.2
  • 6
    • 84861837623 scopus 로고    scopus 로고
    • ω-Transaminases for the production of optically pure amines and unnatural amino acids
    • S. Mathew, and H. Yun ω-Transaminases for the production of optically pure amines and unnatural amino acids ACS Catalysis 2 2012 993 1001
    • (2012) ACS Catalysis , vol.2 , pp. 993-1001
    • Mathew, S.1    Yun, H.2
  • 8
    • 77954797329 scopus 로고    scopus 로고
    • Biocatalytic asymmetric synthesis of chiral amines from ketones applied to sitagliptin manufacture
    • C.K. Savile, J.M. Janey, E.C. Mundorff, J.C. Moore, S. Tam, and W.R. Jarvis Biocatalytic asymmetric synthesis of chiral amines from ketones applied to sitagliptin manufacture Science 329 2010 305 309
    • (2010) Science , vol.329 , pp. 305-309
    • Savile, C.K.1    Janey, J.M.2    Mundorff, E.C.3    Moore, J.C.4    Tam, S.5    Jarvis, W.R.6
  • 9
    • 79951914183 scopus 로고    scopus 로고
    • Sitagliptin manufacture: A compelling tale of green chemistry, process intensification, and industrial asymmetric catalysis
    • A.A. Deasio Sitagliptin manufacture: a compelling tale of green chemistry, process intensification, and industrial asymmetric catalysis Angewandte Chemie International Edition 50 2011 1974 1976
    • (2011) Angewandte Chemie International Edition , vol.50 , pp. 1974-1976
    • Deasio, A.A.1
  • 12
    • 84857910660 scopus 로고    scopus 로고
    • A novel transaminase (R)-amine:Puryvate aminotransferase, from Arthrobacter sp. KNK168 (FERM BP-5228): Purification, characterization, and gene cloning
    • A. Iwasaki, K. Matsymoto, J. Hasegawa, and Y. Yasohara A novel transaminase (R)-amine:puryvate aminotransferase, from Arthrobacter sp. KNK168 (FERM BP-5228): purification, characterization, and gene cloning Applied Microbiology and Biotechnology 93 2012 1563 1573
    • (2012) Applied Microbiology and Biotechnology , vol.93 , pp. 1563-1573
    • Iwasaki, A.1    Matsymoto, K.2    Hasegawa, J.3    Yasohara, Y.4
  • 14
    • 66149094575 scopus 로고    scopus 로고
    • Deracemization of α-chiral primary amines by a one-pot, two-step cascade reaction catalyzed by ω-transaminases
    • 2
    • D. Koszelewski, D. Clay, J.D. Rozell, and W. Kroutil Deracemization of α-chiral primary amines by a one-pot, two-step cascade reaction catalyzed by ω-transaminases European Journal of Organic Chemistry 228 2009 9 229 2
    • (2009) European Journal of Organic Chemistry , vol.228 , pp. 9-229
    • Koszelewski, D.1    Clay, D.2    Rozell, J.D.3    Kroutil, W.4
  • 18
    • 34548314434 scopus 로고    scopus 로고
    • Characterization of free and immobilized (S)-aminotransferase for acetophenone production
    • A.R. Martin, D. Shonnard, S. Pannuri, and S. Kamat Characterization of free and immobilized (S)-aminotransferase for acetophenone production Applied Microbiology and Biotechnology 76 2007 843 851
    • (2007) Applied Microbiology and Biotechnology , vol.76 , pp. 843-851
    • Martin, A.R.1    Shonnard, D.2    Pannuri, S.3    Kamat, S.4
  • 20
    • 84861330688 scopus 로고    scopus 로고
    • Activity and stability of different immobilized preparations of recombinant E. Coli cells containing ω-transaminase
    • G. Rehn, C. Grey, C. Branneby, L. Lindberg, and P. Adlercreutz Activity and stability of different immobilized preparations of recombinant E. coli cells containing ω-transaminase Process Biochemistry 47 2012 1129 1134
    • (2012) Process Biochemistry , vol.47 , pp. 1129-1134
    • Rehn, G.1    Grey, C.2    Branneby, C.3    Lindberg, L.4    Adlercreutz, P.5
  • 21
    • 34047159317 scopus 로고    scopus 로고
    • Covalent immobilization of ω-transaminase from Vibrio fluvialis JS17 on chitosan beads
    • S-S. Yi, C-W. Lee, J. Kim, D. Kyung, B-G. Kim, and Y-S. Lee Covalent immobilization of ω-transaminase from Vibrio fluvialis JS17 on chitosan beads Process Biochemistry 42 2007 895 898
    • (2007) Process Biochemistry , 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
  • 22
    • 84873169472 scopus 로고    scopus 로고
    • Immobilization of two (R)-amine transaminases on an optimized Chitosan support for the enzymatic synthesis of optically pure amines
    • H. Mallin, U. Menyes, T. Vorhaben, M. Höhne, and U.T. Bornscheuer Immobilization of two (R)-amine transaminases on an optimized Chitosan support for the enzymatic synthesis of optically pure amines ChemCatChem 5 2013 588 593
    • (2013) ChemCatChem , vol.5 , pp. 588-593
    • Mallin, H.1    Menyes, U.2    Vorhaben, T.3    Höhne, M.4    Bornscheuer, U.T.5
  • 25
    • 84864357731 scopus 로고    scopus 로고
    • Development of an immobilized transaminase capable of operating in organic solvent
    • M.D. Truppo, H. Strotman, and G. Hughes Development of an immobilized transaminase capable of operating in organic solvent ChemCatChem 4 2012 1071 1074
    • (2012) ChemCatChem , vol.4 , pp. 1071-1074
    • Truppo, M.D.1    Strotman, H.2    Hughes, G.3
  • 26
    • 84883807716 scopus 로고    scopus 로고
    • Immobilized transaminases and process for making and using immobilized transaminases
    • patent WO 2012/177527
    • Truppo MD, Janey JM, Hyghes G. Immobilized transaminases and process for making and using immobilized transaminases. Merck Sharp & Dohme Corp. patent WO 2012/177527.
    • Merck Sharp & Dohme Corp
    • Truppo, M.D.1    Janey, J.M.2    Hyghes, G.3
  • 27
    • 84871058463 scopus 로고    scopus 로고
    • Asymmetric bio-amination of ketones in organic solvents
    • F.G. Mutti, and W. Kroutil Asymmetric bio-amination of ketones in organic solvents Advanced Synthesis and Catalysis 354 2012 3409 3413
    • (2012) Advanced Synthesis and Catalysis , vol.354 , pp. 3409-3413
    • Mutti, F.G.1    Kroutil, W.2
  • 28
    • 84859442003 scopus 로고    scopus 로고
    • Solvent-free kinetic resolution of primary amines catalyzed by Candida antarctica lipase B: Effect of immobilization and recycling stability
    • M. Päiviö, P. Perkiö, and L.T. Kanerva Solvent-free kinetic resolution of primary amines catalyzed by Candida antarctica lipase B: effect of immobilization and recycling stability Tetrahedron: Asymmetry 23 2012 230 236
    • (2012) Tetrahedron: Asymmetry , vol.23 , pp. 230-236
    • Päiviö, M.1    Perkiö, P.2    Kanerva, L.T.3
  • 29
    • 83655167112 scopus 로고    scopus 로고
    • Immobilization to improve properties of Pseudomonas fluorescens lipase for the kinetic resolution of 3-aryl-3-hydroxyesters
    • J. Brem, M.C. Turcu, C. Paizs, K. Lundell, M-I. Tosa, and E-D. Irimie Immobilization to improve properties of Pseudomonas fluorescens lipase for the kinetic resolution of 3-aryl-3-hydroxyesters Process Biochemistry 47 2012 119 126
    • (2012) Process Biochemistry , vol.47 , pp. 119-126
    • Brem, J.1    Turcu, M.C.2    Paizs, C.3    Lundell, K.4    Tosa, M.-I.5    Irimie, E.-D.6
  • 31
    • 0024289285 scopus 로고
    • Investigation of the bicinchoninic acid protein assay: Identification of the groups responsible for color formation
    • K.J. Wiechelman, R.D. Braun, and J.D. Fitzpatrick Investigation of the bicinchoninic acid protein assay: identification of the groups responsible for color formation Analytical Biochemistry 175 1988 231 237
    • (1988) Analytical Biochemistry , vol.175 , pp. 231-237
    • Wiechelman, K.J.1    Braun, R.D.2    Fitzpatrick, J.D.3
  • 32
    • 0030569931 scopus 로고    scopus 로고
    • Efficient immobilization of lipases by entrapment in hydrophobic sol-gel materials
    • M.T. Reetz, A. Zonta, and J. Simpelkamp Efficient immobilization of lipases by entrapment in hydrophobic sol-gel materials Biotechnology and Bioengineering 49 1996 527 534
    • (1996) Biotechnology and Bioengineering , vol.49 , pp. 527-534
    • Reetz, M.T.1    Zonta, A.2    Simpelkamp, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.