메뉴 건너뛰기




Volumn 28, Issue 3, 2012, Pages 693-698

Immobilization of Escherichia coli containing ω-transaminase activity in LentiKats®

Author keywords

transaminase; Asymmetric synthesis; Cell permeabilization; Chiral amines; Immobilization by entrapment; LentiKats ; Whole cell biocatalysis

Indexed keywords

ASYMMETRIC SYNTHESIS; CELL PERMEABILIZATION; CHIRAL AMINES; LENTIKATS; WHOLE-CELL BIOCATALYSIS;

EID: 84862206197     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.1538     Document Type: Article
Times cited : (38)

References (28)
  • 2
    • 77950345610 scopus 로고    scopus 로고
    • Chiral amine synthesis-recent developments and trends for enamide reduction, reductive amination, and imine reduction
    • Nugent TC, El-Shazly M. Chiral amine synthesis-recent developments and trends for enamide reduction, reductive amination, and imine reduction. Adv Synth Catal. 2010; 352: 753-819.
    • (2010) Adv Synth Catal. , vol.352 , pp. 753-819
    • Nugent, T.C.1    El-Shazly, M.2
  • 3
    • 3543087310 scopus 로고    scopus 로고
    • Trends and innovations in industrial biocatalysis for the production of fine chemicals
    • Panke S, Held M, Wubbolts M. Trends and innovations in industrial biocatalysis for the production of fine chemicals. Curt Opin Biotechnol. 2004; 15: 272-279.
    • (2004) Curt Opin Biotechnol. , vol.15 , pp. 272-279
    • Panke, S.1    Held, M.2    Wubbolts, M.3
  • 4
    • 0037012917 scopus 로고    scopus 로고
    • Exploring the active site of amine:pyruvate aminotransferase on the basis of the substrate structure-reactivity relationship: how the enzyme controls substrate specificity and stereoselectivity
    • Shin JS, Kim BG. Exploring the active site of amine:pyruvate aminotransferase on the basis of the substrate structure-reactivity relationship: how the enzyme controls substrate specificity and stereoselectivity. J Org Chem. 2002; 67: 2848-2853.
    • (2002) J Org Chem. , vol.67 , pp. 2848-2853
    • Shin, J.S.1    Kim, B.G.2
  • 5
    • 77953120732 scopus 로고    scopus 로고
    • ω-Transaminases for the synthesis of non-racemic α-chiral primary amines
    • Koszelewski D, Tauber K, Faber K, Kroutil W. ω-Transaminases for the synthesis of non-racemic α-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
  • 6
    • 0033589366 scopus 로고    scopus 로고
    • Asymmetric synthesis of chiral amines with ω-transaminase
    • Shin JS, Kim BG. Asymmetric synthesis of chiral amines with ω-transaminase. Biotechnol Bioeng. 1999; 65: 206-211.
    • (1999) Biotechnol Bioeng. , vol.65 , pp. 206-211
    • Shin, J.S.1    Kim, B.G.2
  • 7
    • 0035812420 scopus 로고    scopus 로고
    • Kinetic resolution of chiral amines using packed-bed reactor
    • Shin JS, Kim BG, Shin DH. 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
  • 8
    • 0035433593 scopus 로고    scopus 로고
    • Comparison of the ω-transaminase from different microorganisms and application to production of chiral amines
    • Shin JS, Kim BG. Comparison of the ω-transaminase from different microorganisms and application to production of chiral amines. Biosci Biotechnol Biochem. 2001; 65: 1782-1788.
    • (2001) Biosci Biotechnol Biochem. , vol.65 , pp. 1782-1788
    • Shin, J.S.1    Kim, B.G.2
  • 10
    • 79251471098 scopus 로고    scopus 로고
    • Guidelines and cost analysis for catalyst production in biocatalytic processes
    • Tufvesson P, Lima-Ramos J, Nordblad M, Woodley JM. Guidelines and cost analysis for catalyst production in biocatalytic processes. Org Process Res Dev. 2011; 15: 266-274.
    • (2011) Org Process Res Dev. , vol.15 , pp. 266-274
    • Tufvesson, P.1    Lima-Ramos, J.2    Nordblad, M.3    Woodley, J.M.4
  • 11
    • 0021942677 scopus 로고
    • Immobilization of whole cells: the engineering principle
    • Karel SF, Libicki SB, Robertson CR. Immobilization of whole cells: the engineering principle. Chem Eng Sci. 1985; 40: 1321-1354.
    • (1985) Chem Eng Sci. , vol.40 , pp. 1321-1354
    • Karel, S.F.1    Libicki, S.B.2    Robertson, C.R.3
  • 12
    • 33847273107 scopus 로고    scopus 로고
    • Permeability issues in whole-cell bioprocesses and cellular membrane engineering
    • Chen RR. Permeability issues in whole-cell bioprocesses and cellular membrane engineering. Appl Microbiol Biotechnol. 2007; 74: 730-738.
    • (2007) Appl Microbiol Biotechnol. , vol.74 , pp. 730-738
    • Chen, R.R.1
  • 13
  • 15
    • 0033694562 scopus 로고    scopus 로고
    • Continuous malolactic fermentation by Oenococcus Oeni entrapped in LentiKats®
    • Durieux A, Nicolay X, Simon JP. Continuous malolactic fermentation by Oenococcus Oeni entrapped in LentiKats®. Biotechnol Lett. 2000; 22: 1679-1684.
    • (2000) Biotechnol Lett. , vol.22 , pp. 1679-1684
    • Durieux, A.1    Nicolay, X.2    Simon, J.P.3
  • 16
    • 27844457119 scopus 로고    scopus 로고
    • PVA-gel (Lentikats®) as an effective matrix for yeast strain immobilization aimed at heterologous protein production
    • Parascandola P, Branduardi P, Alteriis E. PVA-gel (Lentikats®) as an effective matrix for yeast strain immobilization aimed at heterologous protein production. Enzyme Microb Technol. 2006; 38: 184-189.
    • (2006) Enzyme Microb Technol. , vol.38 , pp. 184-189
    • Parascandola, P.1    Branduardi, P.2    Alteriis, E.3
  • 17
    • 27644480256 scopus 로고    scopus 로고
    • High efficiency ethanol fermentation by entrapment of Zymomonas mobilis into LentiKats
    • Rebros M, Rosenberg M, Stloukal L, Kristofi{dotless}kova L. High efficiency ethanol fermentation by entrapment of Zymomonas mobilis into LentiKats. Lett Appl Microbiol. 2005; 41: 412-416.
    • (2005) Lett Appl Microbiol. , vol.41 , pp. 412-416
    • Rebros, M.1    Rosenberg, M.2    Stloukal, L.3    Kristofikova, L.4
  • 18
    • 77954747863 scopus 로고    scopus 로고
    • Paracoccus denitrificans for the effluent recycling during continuous denitrification of liquid food
    • Tippkötter N, Roikaew W, Ulber R, Hoffmann R, Denzler HJ, Buchholz H. Paracoccus denitrificans for the effluent recycling during continuous denitrification of liquid food. Biotechnol Prog. 2010; 26: 756-762.
    • (2010) Biotechnol Prog. , vol.26 , pp. 756-762
    • Tippkötter, N.1    Roikaew, W.2    Ulber, R.3    Hoffmann, R.4    Denzler, H.J.5    Buchholz, H.6
  • 20
    • 0038236890 scopus 로고    scopus 로고
    • Purification, characterization, and molecular cloning of a novel amine:pyruvate transaminase from Vibrio fluvialis JS17
    • Shin JS, Yun H, Jang JW, Park I, Kim BG. Purification, characterization, and molecular cloning of a novel amine:pyruvate transaminase from Vibrio fluvialis JS17. Appl Microbiol Biotechnol. 2003; 61: 463-471.
    • (2003) Appl Microbiol Biotechnol. , vol.61 , pp. 463-471
    • Shin, J.S.1    Yun, H.2    Jang, J.W.3    Park, I.4    Kim, B.G.5
  • 21
    • 77954791339 scopus 로고    scopus 로고
    • Transaminations with isopropyl amine: equilibrium displacement with yeast alcohol dehydrogenase coupled to in situ cofactor regeneration
    • Cassimjee KJ, Branneby C, Abedi V, Wellsd 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.J.1    Branneby, C.2    Abedi, V.3    Wellsd, A.4    Berglund, P.5
  • 22
    • 48849087284 scopus 로고    scopus 로고
    • Efficient asymmetric synthesis of chiral amines by combining transaminase and pyruvate decarboxylase
    • Hohne M, Kuhl S, Robins K, Bornscheuer UT. Efficient asymmetric synthesis of chiral amines by combining transaminase and pyruvate decarboxylase. Chem Bio Chem. 2008; 9: 363-365.
    • (2008) Chem Bio Chem. , vol.9 , pp. 363-365
    • Hohne, M.1    Kuhl, S.2    Robins, K.3    Bornscheuer, U.T.4
  • 23
    • 56749153559 scopus 로고    scopus 로고
    • Asymmetric synthesis of (S)-α-methylbenzylamine by recombinant Escherichia coli co-expressing omega-transaminase and acetolactate synthase
    • Yun H, Kim BG. Asymmetric synthesis of (S)-α-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
  • 24
    • 77953119870 scopus 로고    scopus 로고
    • Synthesis of optically active amines employing recombinant ω-Transaminases in E. coli cells
    • Koszelewski D, Gçritzer M, Clay D, Seisser B, Kroutil W. Synthesis of optically active amines employing recombinant ω-Transaminases in E. coli cells. Chem Cat Chem. 2010; 2: 73-77.
    • (2010) Chem Cat Chem. , vol.2 , pp. 73-77
    • Koszelewski, D.1    Gçritzer, M.2    Clay, D.3    Seisser, B.4    Kroutil, W.5
  • 25
    • 28444451937 scopus 로고    scopus 로고
    • High temperature lactic acid production by Bacillus coagulans immobilized in LentiKats®
    • Rosenberg M, Rebros M, Kristofi{dotless}kova L, Malatova K. High temperature lactic acid production by Bacillus coagulans immobilized in LentiKats®. Biotechnol Lett. 2005; 27: 1943-1947.
    • (2005) Biotechnol Lett. , vol.27 , pp. 1943-1947
    • Rosenberg, M.1    Rebros, M.2    Kristofikova, L.3    Malatova, K.4
  • 26
    • 34548314434 scopus 로고    scopus 로고
    • Characterization of free and immobilized (S)-aminotransferase for acetophenone production
    • Martin AR, 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
  • 27
    • 34047159317 scopus 로고    scopus 로고
    • Covalent immobilization of ω-transaminase from Vibrio fluvialis JS17 on chitosan beads
    • Yi SS, Lee CW, Kim J, Kyung D, Kim BG, Lee YS. 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
  • 28
    • 33748515939 scopus 로고    scopus 로고
    • Improved immobilized enzyme systems using spherical sol-gel enzyme beads
    • Lee CW, Yi SS, Kim J, Lee YS, Kim BG. Improved immobilized enzyme systems using spherical sol-gel enzyme beads. Biotechnol Bioprocess Eng. 2006; 11: 277-281.
    • (2006) Biotechnol Bioprocess Eng. , vol.11 , pp. 277-281
    • Lee, C.W.1    Yi, S.S.2    Kim, J.3    Lee, Y.S.4    Kim, B.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.