메뉴 건너뛰기




Volumn 19, Issue 4, 2009, Pages 362-367

Production, purification, and characterization of soluble NADH-flavin oxidoreductase (StyB) from Pseudomonas putida SN1

Author keywords

BL21(DE3)pLysS; FAD; NADH; Pseudomonas putida SN1; StyB; Styrene monooxygenase

Indexed keywords

BACTERIAL ENZYME; FLAVINE MONONUCLEOTIDE REDUCTASE; OXIDOREDUCTASE;

EID: 67649321851     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.0806.382     Document Type: Article
Times cited : (9)

References (28)
  • 1
    • 33846051873 scopus 로고    scopus 로고
    • Development of recombinant Pseudomonas putida containing homologous styrene monooxygenase genes for the production of (S)-styrene oxide
    • Bae, J. W., J. H. Han, M. S. Park, S. G. Lee, E. Y. Lee, Y. J. Jeong, and S. H. Park. 2006. Development of recombinant Pseudomonas putida containing homologous styrene monooxygenase genes for the production of (S)-styrene oxide. Biotechnol. Bioprocess Eng. 11: 530-537.
    • (2006) Biotechnol. Bioprocess Eng , vol.11 , pp. 530-537
    • Bae, J.W.1    Han, J.H.2    Park, M.S.3    Lee, S.G.4    Lee, E.Y.5    Jeong, Y.J.6    Park, S.H.7
  • 2
    • 40549106156 scopus 로고    scopus 로고
    • Construction and characterization of a recombinant whole-cell biocatalyst of Escherichia coli expressing styrene monooxygenase under the control of arabinose promoter
    • Bae, J. W., S. H. Shin, M. Raj, S. E. Lee, S. G. Lee, Y. J. Jeong, and S. H. Park. 2008. Construction and characterization of a recombinant whole-cell biocatalyst of Escherichia coli expressing styrene monooxygenase under the control of arabinose promoter. Biotechnol. Bioprocess Eng. 13: 69-76.
    • (2008) Biotechnol. Bioprocess Eng , vol.13 , pp. 69-76
    • Bae, J.W.1    Shin, S.H.2    Raj, M.3    Lee, S.E.4    Lee, S.G.5    Jeong, Y.J.6    Park, S.H.7
  • 4
    • 7044228084 scopus 로고    scopus 로고
    • Protein expression and refolding - A practical guide to getting the most out of inclusion bodies
    • Cabrita, L. D. and S. P. Bottomley. 2004. Protein expression and refolding - A practical guide to getting the most out of inclusion bodies. Biotechnol. Annu. Rev. 10: 31-50.
    • (2004) Biotechnol. Annu. Rev , vol.10 , pp. 31-50
    • Cabrita, L.D.1    Bottomley, S.P.2
  • 5
    • 21644437031 scopus 로고    scopus 로고
    • Production of chiral epoxides: Epoxide hydrolase-catalyzed enantioselective hydrolysis
    • Choi, W. J. and C. Y. Choi. 2005. Production of chiral epoxides: Epoxide hydrolase-catalyzed enantioselective hydrolysis. Biotechnol. Bioprocess Eng. 10: 167-179.
    • (2005) Biotechnol. Bioprocess Eng , vol.10 , pp. 167-179
    • Choi, W.J.1    Choi, C.Y.2
  • 6
    • 0033017776 scopus 로고    scopus 로고
    • A new biocatalyst for production of optically pure aryl epoxides by styrene monooxygenase from Pseudomonas fluorescens ST
    • Di Gennaro, P., A. Colmegna, E. Galli, G. Sello, F. Pelizzoni, and G. Bestetti. 1999. A new biocatalyst for production of optically pure aryl epoxides by styrene monooxygenase from Pseudomonas fluorescens ST. Appl. Environ. Microbiol. 65: 2794-2797.
    • (1999) Appl. Environ. Microbiol , vol.65 , pp. 2794-2797
    • Di Gennaro, P.1    Colmegna, A.2    Galli, E.3    Sello, G.4    Pelizzoni, F.5    Bestetti, G.6
  • 7
    • 0000265909 scopus 로고
    • Biological routes to optically active epoxides
    • A. N. Collins, G. N. Sheldrake, and J. Crosby eds, John Wiley & Sons Ltd, Chichester, United Kingdom
    • Furuhashi, K. 1992. Biological routes to optically active epoxides, pp. 167-186. In A. N. Collins, G. N. Sheldrake, and J. Crosby (eds.). Chirality in Industry. John Wiley & Sons Ltd., Chichester, United Kingdom.
    • (1992) Chirality in Industry , pp. 167-186
    • Furuhashi, K.1
  • 8
    • 0343553240 scopus 로고
    • Microbial degradation of styrene
    • V. P. Singh ed, Elsevier Science, Amsterdam, The Netherlands
    • Hartmans, S. 1995. Microbial degradation of styrene, pp. 227-239. In V. P. Singh (ed.), Biotransformations: Microbial Degradation of Health Risk Compounds. Elsevier Science, Amsterdam, The Netherlands.
    • (1995) Biotransformations: Microbial Degradation of Health Risk Compounds , pp. 227-239
    • Hartmans, S.1
  • 9
    • 0025253582 scopus 로고
    • Bacterial degradation of styrene involving a novel flavin adenine dinucleotide-dependent styrene monooxygenase
    • Hartmans, S., M. J. van der Werft, and J. A. M. de Bont. 1990. Bacterial degradation of styrene involving a novel flavin adenine dinucleotide-dependent styrene monooxygenase. Appl. Environ. Microbiol. 56: 1347-1351.
    • (1990) Appl. Environ. Microbiol , vol.56 , pp. 1347-1351
    • Hartmans, S.1    van der Werft, M.J.2    de Bont, J.A.M.3
  • 10
    • 0038344024 scopus 로고    scopus 로고
    • Stereospecific biocatalytic epoxidation: The first example of direct regeneration of a FAD-dependent monooxygenase for catalysis
    • Hollmann, F., P.-C. Lin, B. Witholt, and A. Schmid. 2003. Stereospecific biocatalytic epoxidation: The first example of direct regeneration of a FAD-dependent monooxygenase for catalysis. J. Am. Chem. Soc. 125: 8209-8217.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 8209-8217
    • Hollmann, F.1    Lin, P.-C.2    Witholt, B.3    Schmid, A.4
  • 11
    • 24944534515 scopus 로고    scopus 로고
    • Mechanism of flavin transfer and oxygen activation by the two-component flavoenzyme styrene monooxygenase
    • Kantz, A., F. Chin, N. Nallamothu, T. Nguyen, and G. T. Gassner. 2005. Mechanism of flavin transfer and oxygen activation by the two-component flavoenzyme styrene monooxygenase. Arch. Biochem. Biophys. 442: 102-116.
    • (2005) Arch. Biochem. Biophys , vol.442 , pp. 102-116
    • Kantz, A.1    Chin, F.2    Nallamothu, N.3    Nguyen, T.4    Gassner, G.T.5
  • 12
    • 3943060045 scopus 로고    scopus 로고
    • Biocatalytic preparation of chiral epichlorohydrins using recombinant Pichia pastoris expressing epoxide hydrolase of Rhodotorula glutinis
    • Kim, H. S., J. H. Lee, S. Park, and E. Y. Lee. 2004. Biocatalytic preparation of chiral epichlorohydrins using recombinant Pichia pastoris expressing epoxide hydrolase of Rhodotorula glutinis. Biotechnol. Bioprocess Eng. 9: 62-64.
    • (2004) Biotechnol. Bioprocess Eng , vol.9 , pp. 62-64
    • Kim, H.S.1    Lee, J.H.2    Park, S.3    Lee, E.Y.4
  • 13
    • 0031786128 scopus 로고    scopus 로고
    • Effect of pLysS on the production of bioadhesive precursor protein by fed-batch cultivation of recombinant Escherichia coli
    • Kim, Y. C., S. Kwon, S. Y. Lee, and H. N. Chang. 1998. Effect of pLysS on the production of bioadhesive precursor protein by fed-batch cultivation of recombinant Escherichia coli. Biotechnol. Lett. 20: 799-803.
    • (1998) Biotechnol. Lett , vol.20 , pp. 799-803
    • Kim, Y.C.1    Kwon, S.2    Lee, S.Y.3    Chang, H.N.4
  • 14
    • 0025509404 scopus 로고
    • Expression of mammalian liver glycolytic/gluconeogenic enzymes in Escherichia coli: Recovery of active enzyme is strain and temperature dependent
    • Lin, K., I. Kurland, L. Z. Xu, A. J. Lange, J. Pilkis, M. R. El-Maghrabi, and S. J. Pilkis. 1990. Expression of mammalian liver glycolytic/gluconeogenic enzymes in Escherichia coli: Recovery of active enzyme is strain and temperature dependent. Protein Express. Purif. 1: 169-176.
    • (1990) Protein Express. Purif , vol.1 , pp. 169-176
    • Lin, K.1    Kurland, I.2    Xu, L.Z.3    Lange, A.J.4    Pilkis, J.5    El-Maghrabi, M.R.6    Pilkis, S.J.7
  • 15
    • 0035047240 scopus 로고    scopus 로고
    • Transcriptional regulation of styrene degradation in Pseudomonas putida CA-3
    • O'Leary, N. D., K. E. O'Connor, W. Duetz, and A. D. W. Dobson. 2001. Transcriptional regulation of styrene degradation in Pseudomonas putida CA-3. Microbiology 147: 973-979.
    • (2001) Microbiology , vol.147 , pp. 973-979
    • O'Leary, N.D.1    O'Connor, K.E.2    Duetz, W.3    Dobson, A.D.W.4
  • 16
    • 3843128465 scopus 로고    scopus 로고
    • Biochemical characterization of StyAB from Pseudomonas sp. strain VLB120 as a two-component flavin-diffusible monooxygenase
    • Otto, K., K. Hofstetter, M. Rothlisberger, B. Witholt, and A. Schmid. 2004. Biochemical characterization of StyAB from Pseudomonas sp. strain VLB120 as a two-component flavin-diffusible monooxygenase. J. Bacteriol. 186: 5292-5302.
    • (2004) J. Bacteriol , vol.186 , pp. 5292-5302
    • Otto, K.1    Hofstetter, K.2    Rothlisberger, M.3    Witholt, B.4    Schmid, A.5
  • 17
    • 0037026952 scopus 로고    scopus 로고
    • Pilot-scale production of (S)-styrene oxide from styrene by recombinant Escherichia coli synthesizing styrene monooxygenase
    • Panke, S., M. Held, M. G. Wubbolts, B. Witholt, and A. Schmid. 2002. Pilot-scale production of (S)-styrene oxide from styrene by recombinant Escherichia coli synthesizing styrene monooxygenase. Biotechnol. Bioeng. 80: 33-41.
    • (2002) Biotechnol. Bioeng , vol.80 , pp. 33-41
    • Panke, S.1    Held, M.2    Wubbolts, M.G.3    Witholt, B.4    Schmid, A.5
  • 18
    • 0032728414 scopus 로고    scopus 로고
    • Engineering of a stable whole-cell biocatalyst capable of (S)-styrene oxide formation for continuous two-liquid-phase application
    • Panke, S., V. Lorezo, A. Kaiser, B. Witholt, and M. G. Wubbolts. 1999. Engineering of a stable whole-cell biocatalyst capable of (S)-styrene oxide formation for continuous two-liquid-phase application. Appl. Environ. Microbiol. 65: 5619-5623.
    • (1999) Appl. Environ. Microbiol , vol.65 , pp. 5619-5623
    • Panke, S.1    Lorezo, V.2    Kaiser, A.3    Witholt, B.4    Wubbolts, M.G.5
  • 19
    • 0031745849 scopus 로고    scopus 로고
    • Towards a biocatalyst for (S)-styrene oxide production: Characterization of the styrene degradation pathway of Pseudomonas sp. strain VBL120
    • Panke, S., B. Witholt, A. Schmid, and M. G. Wubbolts. 1998. Towards a biocatalyst for (S)-styrene oxide production: Characterization of the styrene degradation pathway of Pseudomonas sp. strain VBL120. Appl. Environ. Microbiol. 64: 2032-2043.
    • (1998) Appl. Environ. Microbiol , vol.64 , pp. 2032-2043
    • Panke, S.1    Witholt, B.2    Schmid, A.3    Wubbolts, M.G.4
  • 20
    • 0034609021 scopus 로고    scopus 로고
    • Production of enantiopure styrene oxide by recombinant Escherichia coli synthesizing a two-component styrene monooxygenase
    • Panke, S., M. G. Wubbolts, A. Schmid, and B. Witholt. 2000. Production of enantiopure styrene oxide by recombinant Escherichia coli synthesizing a two-component styrene monooxygenase. Biotechnol. Bioeng. 69: 91-100.
    • (2000) Biotechnol. Bioeng , vol.69 , pp. 91-100
    • Panke, S.1    Wubbolts, M.G.2    Schmid, A.3    Witholt, B.4
  • 21
    • 33746867443 scopus 로고    scopus 로고
    • Characterization of styrene catabolic genes of Pseudomonas putida SN1 and construction of a recombinant Escherichia coli containing styrene monooxygenase gene for the production of (S)-styrene oxide
    • Park, M. S., J. W. Bae, J. H. Han, E. Y. Lee, S. G. Lee, and S. H. Park. 2006. Characterization of styrene catabolic genes of Pseudomonas putida SN1 and construction of a recombinant Escherichia coli containing styrene monooxygenase gene for the production of (S)-styrene oxide. J. Microbiol. Biotechnol. 16: 1032-1040.
    • (2006) J. Microbiol. Biotechnol , vol.16 , pp. 1032-1040
    • Park, M.S.1    Bae, J.W.2    Han, J.H.3    Lee, E.Y.4    Lee, S.G.5    Park, S.H.6
  • 23
    • 33751414738 scopus 로고    scopus 로고
    • Improved conditions for production of recombinant plant sesquiterpene synthases in Escherichia coli
    • Picaud, S., M. E. Olsson, and P. E. Brodelius. 2007. Improved conditions for production of recombinant plant sesquiterpene synthases in Escherichia coli. Protein Express. Purif. 51: 71-79.
    • (2007) Protein Express. Purif , vol.51 , pp. 71-79
    • Picaud, S.1    Olsson, M.E.2    Brodelius, P.E.3
  • 24
    • 67649365740 scopus 로고    scopus 로고
    • Optimization of the expression of single-chain antibodies using different Escherichia coli systems
    • Riedstra, S., G. Leite, C. Ferreira, F. B. Gomes, P. M. P. Costa, and J. P. M. Ferreira. 2007. Optimization of the expression of single-chain antibodies using different Escherichia coli systems. J. Biotech. 131: S251-S252.
    • (2007) J. Biotech , vol.131
    • Riedstra, S.1    Leite, G.2    Ferreira, C.3    Gomes, F.B.4    Costa, P.M.P.5    Ferreira, J.P.M.6
  • 25
    • 0023892436 scopus 로고
    • Formation of soluble recombinant proteins in E. coli is favored by lower growth temperature
    • Schein, C. H. and N. H. M. Noteborn. 1988. Formation of soluble recombinant proteins in E. coli is favored by lower growth temperature. Biotechnology 6: 291-294.
    • (1988) Biotechnology , vol.6 , pp. 291-294
    • Schein, C.H.1    Noteborn, N.H.M.2
  • 26
    • 0023774934 scopus 로고
    • Control of folding of proteins secreted by a high expression sensitive vector, p 1N-111-ompA: 16-fold increase in production of active subtilisin in E. coli
    • Takagi, H., Y. Morinaga, M. Tsuchiya, H. Ikemura, and M. Inauyi. 1988. Control of folding of proteins secreted by a high expression sensitive vector, p 1N-111-ompA: 16-fold increase in production of active subtilisin in E. coli. Biotechnology 6: 948-950.
    • (1988) Biotechnology , vol.6 , pp. 948-950
    • Takagi, H.1    Morinaga, Y.2    Tsuchiya, M.3    Ikemura, H.4    Inauyi, M.5
  • 27
    • 0031910876 scopus 로고    scopus 로고
    • Genetic and functional analysis of the styrene catabolic cluster of Pseudomonas sp. strain Y2
    • Velasco, A., S. Alonso, J. L. Garcia, J. Perera, and E. Diaz. 1998. Genetic and functional analysis of the styrene catabolic cluster of Pseudomonas sp. strain Y2. J. Bacteriol. 180: 1063-1071.
    • (1998) J. Bacteriol , vol.180 , pp. 1063-1071
    • Velasco, A.1    Alonso, S.2    Garcia, J.L.3    Perera, J.4    Diaz, E.5
  • 28
    • 0027096402 scopus 로고
    • Expression, purification, and characterization of the functional dimeric cytoplasmic domain of human erythrocyte band 3 in Escherichia coli
    • Wang, C. C., J. A. Badylak, S. E. Lux, R. Moriyama, J. E. Dixon, and P. S. Low. 1992. Expression, purification, and characterization of the functional dimeric cytoplasmic domain of human erythrocyte band 3 in Escherichia coli. Protein Sci. 1: 1206-1214.
    • (1992) Protein Sci , vol.1 , pp. 1206-1214
    • Wang, C.C.1    Badylak, J.A.2    Lux, S.E.3    Moriyama, R.4    Dixon, J.E.5    Low, P.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.