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Volumn 46, Issue 3, 2011, Pages 721-729

Effects of dissolved oxygen availability and culture biomass at induction upon the intracellular expression of monoamine oxidase by recombinant E. coli in fed batch bioprocesses

Author keywords

E. coli; Fermentation; Monoamine oxidase; Oxidative stress

Indexed keywords

AERATED CULTURES; AEROBIC PROCESS; AMINO ACID COMPOSITIONS; BIOMASS LEVELS; BIOPROCESSES; CELL DENSITY; CYTOSOLS; E. COLI; FED BATCHES; FED-BATCH CULTURES; FREE ENZYME; INDUCTION CELL; LOW LEVEL; MONOAMINE OXIDASE; OPTIMAL PROCESS; OXIDATIVE DAMAGE; OXYGEN ENRICHMENT; OXYGEN-ENRICHED AIR; POSITIVE EFFECTS; PROTEIN PRODUCTION; RECOMBINANT E. COLI; SPECIFIC ACTIVITY; SPECIFIC GROWTH RATE;

EID: 79951512037     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2010.11.019     Document Type: Article
Times cited : (10)

References (68)
  • 1
    • 67349273072 scopus 로고    scopus 로고
    • Comparison of two expression platforms in respect to protein yield and quality: Pichia pastoris versus Pichia angusta
    • M. Mack, M. Wannemacher, B. Hobl, P. Pietschmann, and B. Hock Comparison of two expression platforms in respect to protein yield and quality: Pichia pastoris versus Pichia angusta Protein Express Purif 66 2009 165 171
    • (2009) Protein Express Purif , vol.66 , pp. 165-171
    • MacK, M.1    Wannemacher, M.2    Hobl, B.3    Pietschmann, P.4    Hock, B.5
  • 2
    • 67149092188 scopus 로고    scopus 로고
    • Molecular basis of methanol-inducible gene expression and its application in the methylotrophic yeast Candida boidinii
    • H. Yurimoto Molecular basis of methanol-inducible gene expression and its application in the methylotrophic yeast Candida boidinii Biosci Biotechnol Biochem 73 2009 793 800
    • (2009) Biosci Biotechnol Biochem , vol.73 , pp. 793-800
    • Yurimoto, H.1
  • 3
    • 33846702659 scopus 로고    scopus 로고
    • Expression by Streptomyces lividans of the rat a Integrin CD11b A-Domain as a secreted and soluble recombinant protein
    • D.Z. Ayadi, H. Chouayekh, S. Mhiri, K. Zerria, D.M. Fathallah, and S. Bejar Expression by Streptomyces lividans of the rat a Integrin CD11b A-Domain as a secreted and soluble recombinant protein J Biomed Biotechnol 2007 Article ID 54327
    • (2007) J Biomed Biotechnol
    • Ayadi, D.Z.1    Chouayekh, H.2    Mhiri, S.3    Zerria, K.4    Fathallah, D.M.5    Bejar, S.6
  • 5
    • 29844438161 scopus 로고    scopus 로고
    • Expression of Bacillus protease (protease BYA) from Bacillus sp. Y in Bacillus subtilis and enhancement of its specific activity by site-directed mutagenesis - Improvement in productivity of detergent enzyme
    • DOI 10.1248/bpb.29.26
    • S. Tobe, H. Shimogaki, M. Ohdera, Y. Asai, K. Oba, and M. Iwama Expression of Bacillus protease (protease BYA) from Bacillus sp. Y in Bacillus subtilis and enhancement of its specific activity by site-directed mutagenesis-improvement in productivity of detergent enzyme Biol Pharm Bull 29 2006 26 33 (Pubitemid 43036688)
    • (2006) Biological and Pharmaceutical Bulletin , vol.29 , Issue.1 , pp. 26-33
    • Tobe, S.1    Shimogaki, H.2    Ohdera, M.3    Asai, Y.4    Oba, K.5    Iwama, M.6    Irie, M.7
  • 8
    • 21644462706 scopus 로고    scopus 로고
    • Appropriate glycosylation of recombinant proteins for human use
    • S. Brooks Appropriate glycosylation of recombinant proteins for human use Mol Biotechnol 28 2004 241 255
    • (2004) Mol Biotechnol , vol.28 , pp. 241-255
    • Brooks, S.1
  • 9
    • 0028224656 scopus 로고
    • Glycosylation of recombinant proteins: Problems and prospects
    • DOI 10.1016/0141-0229(94)90149-X
    • N. Jenkins, and E.M.A. Curling Glycosylation of recombinant proteins: problems and prospects Enzyme Microb Technol 16 1994 354 364 (Pubitemid 24150345)
    • (1994) Enzyme and Microbial Technology , vol.16 , Issue.5 , pp. 354-364
    • Jenkins, N.1    Curling, E.M.A.2
  • 10
    • 25844514728 scopus 로고    scopus 로고
    • Preparative expression of secreted proteins in bacteria: Status report and future prospects
    • DOI 10.1016/j.copbio.2005.07.008, PII S0958166905001242, Tissue and Cell Engineering/Biochemical Engineering
    • G. Georgiou, and L. Segatori Preparative expression of secreted proteins in bacteria: status report and future prospects Curr Opin Biotechnol 16 2005 538 545 (Pubitemid 41393835)
    • (2005) Current Opinion in Biotechnology , vol.16 , Issue.5 , pp. 538-545
    • Georgiou, G.1    Segatori, L.2
  • 12
    • 0034696662 scopus 로고    scopus 로고
    • Enantioselective deprotonation reactions using a novel homochiral magnesium amide base
    • K.W. Henderson, W.J. Kerr, and J.H. Moir Enantioselective deprotonation reactions using a novel homochiral magnesium amide base Chem Commun 2000 479 480 (Pubitemid 30169632)
    • (2000) Chemical Communications , Issue.6 , pp. 479-480
    • Henderson, K.W.1    Kerr, W.J.2    Moir, J.H.3
  • 13
    • 0035974653 scopus 로고    scopus 로고
    • S(+)-4-(1-phenylethylamino)quinazolines as inhibitors of human immunoglobuline E synthesis: Potency is dictated by stereochemistry and atomic point charges at N-1
    • DOI 10.1021/jm010888h
    • M. Berger, B. Albrecht, A. Berces, P. Ettmayer, W. Neruda, and M. Woisetschlager S(+)-4-(1-Phenylethylamino) quinazolines as inhibitors of human immunoglobuline E synthesis: potency is dictated by stereochemistry and atomic point charges at N-1 J Med Chem 44 2001 3031 3038 (Pubitemid 32879131)
    • (2001) Journal of Medicinal Chemistry , vol.44 , Issue.18 , pp. 3031-3038
    • Berger, M.1    Albrecht, B.2    Berces, A.3    Ettmayer, P.4    Neruda, W.5    Woisetschlager, M.6
  • 15
    • 79951509013 scopus 로고    scopus 로고
    • Biochemistry and physiology of growth and metabolism
    • C. Ratledge Biochemistry and physiology of growth and metabolism C. Ratledge, B. Kristiansen, Basic biotechnology 2001 Cambridge University Press
    • (2001) Basic Biotechnology
    • Ratledge, C.1
  • 16
    • 0034152767 scopus 로고    scopus 로고
    • Oxidative stress in bacteria and protein damage by reactive oxygen species
    • E. Cabiscol, J. Tamarit, and J. Ros Oxidative stress in bacteria and protein damage by reactive oxygen species Int Microbiol 3 2000 3 8
    • (2000) Int Microbiol , vol.3 , pp. 3-8
    • Cabiscol, E.1    Tamarit, J.2    Ros, J.3
  • 17
    • 0030447225 scopus 로고    scopus 로고
    • Cellular and molecular physiology of Escherichia coli in the adaptation to aerobic environments
    • S. Iuchi, and L. Weiner Cellular and molecular physiology of Escherichia coli in the adaptation to aerobic environments J Biochem 120 1996 1055 1063 (Pubitemid 27029140)
    • (1996) Journal of Biochemistry , vol.120 , Issue.6 , pp. 1055-1063
    • Iuchi, S.1    Weiner, L.2
  • 18
    • 0033985228 scopus 로고    scopus 로고
    • Iron and oxidative stress in bacteria
    • DOI 10.1006/abbi.1999.1518
    • D. Touati Iron and oxidative stress in bacteria Arch Biochem Biophys 373 2000 1 6 (Pubitemid 30046483)
    • (2000) Archives of Biochemistry and Biophysics , vol.373 , Issue.1 , pp. 1-6
    • Touati, D.1
  • 19
    • 0025786078 scopus 로고
    • Oxidative stress responses in Escherichia coli and Salmonella typhimurium
    • S.B. Farr, and T. Kogoma Oxidative stress responses in Escherichia coli and Salmonella typhimurium Microbiol Mol Biol Rev 55 1991 561 585 (Pubitemid 21895167)
    • (1991) Microbiological Reviews , vol.55 , Issue.4 , pp. 561-585
    • Farr, S.B.1    Kogoma, T.2
  • 20
    • 0030875880 scopus 로고    scopus 로고
    • The effect of oxidative stress on the production of the recombinant protein, interferon γ, produced by Chinese hamster ovary cells in stirred- batch culture
    • DOI 10.1007/s002530051038
    • C.A. Dunster, K.H. Cheeseman, and S.P. Maddix The effect of oxidative stress on the production of the recombinant protein, interferon γ, produced by Chinese hamster ovary cells in stirred-batch culture Appl Microbiol Biotechnol 48 1997 198 203 (Pubitemid 27394750)
    • (1997) Applied Microbiology and Biotechnology , vol.48 , Issue.2 , pp. 198-203
    • Dunster, C.A.1    Cheeseman, K.H.2    Maddix, S.P.3
  • 21
    • 46849101260 scopus 로고    scopus 로고
    • The effects of elevated process temperature on the protein carbonyls in the filamentous fungus, Aspergillus niger B1-D
    • Q. Li, L.M. Harvey, and B. McNeil The effects of elevated process temperature on the protein carbonyls in the filamentous fungus, Aspergillus niger B1-D Process Biochem 43 2008 877 881
    • (2008) Process Biochem , vol.43 , pp. 877-881
    • Li, Q.1    Harvey, L.M.2    McNeil, B.3
  • 22
    • 0030070186 scopus 로고    scopus 로고
    • Comparison of the effects of ozone on the modification of amino acid residues in glutamine synthetase and bovine serum albumin
    • DOI 10.1074/jbc.271.8.4177
    • B.S. Berlett, R.L. Levine, and E.R. Stadtman Comparison of the effects of ozone on the modification of amino acid residues in glutamine synthetase and bovine serum albumin J Biol Chem 271 1996 4177 4182 (Pubitemid 26070518)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.8 , pp. 4177-4182
    • Berlett, B.S.1    Levine, R.L.2    Stadtman, E.R.3
  • 23
    • 0034938628 scopus 로고    scopus 로고
    • Comparing the effect on protein stability of methionine oxidation versus mutagenesis: Steps toward engineering oxidative resistance in proteins
    • Y.H. Kim, A.H. Berry, D.S. Spencer, and W.E. Stites Comparing the effect on protein stability of methionine oxidation versus mutagenesis: steps toward engineering oxidative resistance in proteins Protein Eng 14 2001 343 347 (Pubitemid 32655950)
    • (2001) Protein Engineering , vol.14 , Issue.5 , pp. 343-347
    • Kim, Y.H.1    Berry, A.H.2    Spencer, D.S.3    Stites, W.E.4
  • 24
    • 0346100345 scopus 로고    scopus 로고
    • Free radical-mediated oxidation of free amino acids and amino acid residues in proteins
    • DOI 10.1007/s00726-003-0011-2
    • E.R. Stadtman, and R.L. Levine Free radical-mediated oxidation of free amino acids and amino acid residues in proteins Amino Acids 25 2003 207 218 (Pubitemid 38043943)
    • (2003) Amino Acids , vol.25 , Issue.3-4 , pp. 207-218
    • Stadtman, E.R.1    Levine, R.L.2
  • 26
    • 0034890121 scopus 로고    scopus 로고
    • Aging and oxidation of reactive protein sulfhydryls
    • DOI 10.1016/S0531-5565(01)00137-1, PII S0531556501001371
    • J.A. Thomas, and R.J. Mallis Aging and oxidation of reactive protein sulfhydryls Exp Gerontol 36 2001 1519 1526 (Pubitemid 32768729)
    • (2001) Experimental Gerontology , vol.36 , Issue.9 , pp. 1519-1526
    • Thomas, J.A.1    Mallis, R.J.2
  • 27
    • 0028852816 scopus 로고
    • Oxidation of methionyl residues in proteins: Tools, targets, and reversal
    • W. Vogt Oxidation of methionyl residues in proteins: tools, targets, and reversal Free Radical Biol Med 18 1995 93 105
    • (1995) Free Radical Biol Med , vol.18 , pp. 93-105
    • Vogt, W.1
  • 28
    • 0037008967 scopus 로고    scopus 로고
    • Deracemization of α-methylbenzylamine using an enzyme obtained by in vitro evolution
    • DOI 10.1002/1521-3773(20020902)41:17<3177::AID-ANIE3177>3.0.CO;2-P
    • M. Alexeeva, A. Enright, M.J. Dawson, M. Mahmoudian, and N.J. Turner Deracemization of α-methylbenzylamine using an enzyme obtained by in vitro evolution Angew Chem Int Ed 41 2002 3177 3180 (Pubitemid 35014378)
    • (2002) Angewandte Chemie - International Edition , vol.41 , Issue.17 , pp. 3177-3180
    • Alexeeva, M.1    Enright, A.2    Dawson, M.J.3    Mahmoudian, M.4    Turner, N.J.5
  • 30
    • 33751086112 scopus 로고    scopus 로고
    • Novel biocatalyst technology for the preparation of chiral amines
    • N. Turner, I. Fotheringham, and R. Speight Novel biocatalyst technology for the preparation of chiral amines ChemInform 36 2005
    • (2005) ChemInform , vol.36
    • Turner, N.1    Fotheringham, I.2    Speight, R.3
  • 31
    • 0345085733 scopus 로고    scopus 로고
    • On-line detection of acetate formation in Escherichia coli cultures using dissolved oxygen responses to feed transients
    • DOI 10.1002/(SICI)1097-0290(19990905)64:5<590::AID-BIT9>3.0.CO;2-T
    • M. kesson, E.N. Karlsson, P. Hagander, J.P. Axelsson, and A. Tocaj On-line detection of acetate formation in Escherichia coli cultures using dissolved oxygen responses to feed transients Biotechnol Bioeng 64 1999 590 598 (Pubitemid 29359809)
    • (1999) Biotechnology and Bioengineering , vol.64 , Issue.5 , pp. 590-598
    • Akesson, M.1    Karlsson, E.N.2    Hagander, P.3    Axelsson, J.P.4    Tocaj, A.5
  • 32
    • 84873790809 scopus 로고
    • Replica plating and indirect selection of bacterial mutants
    • J. Lederberg, and E.M. Lederberg Replica plating and indirect selection of bacterial mutants J Bacteriol 63 1952 399 406
    • (1952) J Bacteriol , vol.63 , pp. 399-406
    • Lederberg, J.1    Lederberg, E.M.2
  • 33
    • 0026832754 scopus 로고
    • Acetic acid formation in Escherichia coli fermentation
    • K. Han, H.C. Lim, and J. Hong Acetic acid formation in Escherichia coli fermentation Biotechnol Bioeng 39 1992 663 671
    • (1992) Biotechnol Bioeng , vol.39 , pp. 663-671
    • Han, K.1    Lim, H.C.2    Hong, J.3
  • 34
    • 0025264582 scopus 로고
    • Comparison of growth, acetate production, and acetate inhibition of Escherichia coli strains in batch and fed-batch fermentations
    • G.W. Luli, and W.R. Strohl Comparison of growth, acetate production, and acetate inhibition of Escherichia coli strains in batch and fed-batch fermentations Appl Environ Microbiol 56 1990 1004 1011 (Pubitemid 20114456)
    • (1990) Applied and Environmental Microbiology , vol.56 , Issue.4 , pp. 1004-1011
    • Luli, G.W.1    Strohl, W.R.2
  • 35
    • 0027087370 scopus 로고
    • Comparison of acetate inhibition on growth of host and recombinant E. coli K12 strains
    • DOI 10.1007/BF01027012
    • B.T. Koh, U. Nakashimada, M. Pfeiffer, and M.G.S. Yap Comparison of acetate inhibition on growth of host and recombinant E. coli K12 strains Biotechnol Lett 14 1992 1115 1118 (Pubitemid 23027099)
    • (1992) Biotechnology Letters , vol.14 , Issue.12 , pp. 1115-1118
    • Koh, B.T.1    Nakashimada, U.2    Pfeiffer, M.3    Yap, M.G.S.4
  • 37
    • 16344391449 scopus 로고    scopus 로고
    • Redistribution of metabolic fluxes in the central aerobic metabolic pathway of E. coli mutant strains with deletion of the ackA-pta and poxB pathways for the synthesis of isoamyl acetate
    • DOI 10.1021/bp049730r
    • C.R. Dittrich, R.V. Vadali, G.N. Bennett, and K-Y. San Redistribution of metabolic fluxes in the central aerobic metabolic pathway of E. coli. Mutant strains with deletion of the acka-pta and poxb pathways for the synthesis of isoamyl acetate Biotechnol Prog 21 2005 627 631 (Pubitemid 40466442)
    • (2005) Biotechnology Progress , vol.21 , Issue.2 , pp. 627-631
    • Dittrich, C.R.1    Vadali, R.V.2    Bennett, G.N.3    San, K.-Y.4
  • 38
    • 0023128447 scopus 로고
    • Effects of dissolved oxygen shock on the stability of recombinant Escherichia coli containing plasmid pKN401
    • DOI 10.1002/bit.260290113
    • D.J. Hopkins, M.J. Betenbaugh, and P. Dhurjati Effects of dissolved oxygen shock on the stability of recombinant Escherichia coli containing plasmid pKN401 Biotechnol Bioeng 29 1987 85 91 (Pubitemid 17059299)
    • (1987) Biotechnology and Bioengineering , vol.29 , Issue.1 , pp. 85-91
    • Hopkins, D.J.1    Betenbaugh, M.J.2    Dhurjati, P.3
  • 39
    • 0026594010 scopus 로고
    • Effect of the levels of dissolved oxygen on the expression of recombinant proteins in four recombinant Escherichia coli strains
    • X. Li, J.W. Robbins, and K.B. Taylor Effect of the levels of dissolved oxygen on the expression of recombinant proteins in four recombinant Escherichia coli strains J Ind Microbiol Biotechnol 9 1992 1 9
    • (1992) J Ind Microbiol Biotechnol , vol.9 , pp. 1-9
    • Li, X.1    Robbins, J.W.2    Taylor, K.B.3
  • 40
    • 0022917004 scopus 로고
    • Factors influencing productivity of fermentations employing recombinant microorganisms
    • DOI 10.1016/0141-0229(86)90157-2
    • D.W. Zabriskie, and E.J. Arcuri Factors influencing productivity of fermentations employing recombinant microorganisms Enzyme Microb Technol 8 1986 706 717 (Pubitemid 17226557)
    • (1986) Enzyme and Microbial Technology , vol.8 , Issue.12 , pp. 706-717
    • Zabriskie, D.W.1    Arcuri, E.J.2
  • 41
    • 42749084214 scopus 로고    scopus 로고
    • Design and characterisation of a miniature stirred bioreactor system for parallel microbial fermentations
    • DOI 10.1016/j.bej.2007.09.001, PII S1369703X07003270
    • N.K. Gill, M. Appleton, F. Baganz, and G.J. Lye Design and characterisation of a miniature stirred bioreactor system for parallel microbial fermentations Biochem Eng J 39 2008 164 176 (Pubitemid 351625648)
    • (2008) Biochemical Engineering Journal , vol.39 , Issue.1 , pp. 164-176
    • Gill, N.K.1    Appleton, M.2    Baganz, F.3    Lye, G.J.4
  • 42
    • 0032841652 scopus 로고    scopus 로고
    • Effect of oxygen enrichment aeration on penicillin G acylase production in high cell density culture of recombinant E. coli
    • Y.C. Liu, W.M. Chang, and C.Y. Lee Effect of oxygen enrichment aeration on penicillin G acylase production in high cell density culture of recombinant E. coli Bioprocess Biosyst Eng 21 1999 227 230
    • (1999) Bioprocess Biosyst Eng , vol.21 , pp. 227-230
    • Liu, Y.C.1    Chang, W.M.2    Lee, C.Y.3
  • 43
    • 0028117314 scopus 로고
    • Molecular chaperones in protein folding: The art of avoiding sticky situations
    • DOI 10.1016/0968-0004(94)90169-4
    • F-U. Hartl, R. Hlodan, and T. Langer Molecular chaperones in protein folding: the art of avoiding sticky situations Trends Biochem Sci 19 1994 20 25 (Pubitemid 24028727)
    • (1994) Trends in Biochemical Sciences , vol.19 , Issue.1 , pp. 20-25
    • Hartl, F.-U.1    Hlodan, R.2    Langer, T.3
  • 45
    • 0030829959 scopus 로고    scopus 로고
    • Influence of acetic acid on the growth of Escherichia coli K12 during high-cell-density cultivation in a dialysis reactor
    • DOI 10.1007/s002530051101
    • K. Nakano, M. Rischke, S. Sato, and H. Märkl Influence of acetic acid on the growth of Escherichia coli K12 during high-cell-density cultivation in a dialysis reactor Appl Microbiol Biotechnol 48 1997 597 601 (Pubitemid 27511582)
    • (1997) Applied Microbiology and Biotechnology , vol.48 , Issue.5 , pp. 597-601
    • Nakano, K.1    Rischke, M.2    Sato, S.3    Markl, H.4
  • 46
    • 0025700668 scopus 로고
    • Production of recombinant human growth hormone in Escherichia coli: Expression of different precursors and physiological effects of glucose, acetate, and salts
    • DOI 10.1002/bit.260360102
    • E.B. Jensen, and S. Carlsen Production of recombinant human growth hormone in Escherichia coli: expression of different precursors and physiological effects of glucose, acetate, and salts Biotechnol Bioeng 36 1990 1 11 (Pubitemid 20210769)
    • (1990) Biotechnology and Bioengineering , vol.36 , Issue.1 , pp. 1-11
    • Jensen, E.B.1    Carlsen, S.2
  • 47
    • 4544253176 scopus 로고    scopus 로고
    • Diversion of carbon flux from central metabolism to product formation
    • E. El-Mansi Diversion of carbon flux from central metabolism to product formation Soc Gen Microbiol Symp 145 1997
    • (1997) Soc Gen Microbiol Symp , vol.145
    • El-Mansi, E.1
  • 48
    • 0034918307 scopus 로고    scopus 로고
    • The physiological effects and metabolic alterations caused by the expression of Rhizobium etli pyruvate carboxylase in Escherichia coli
    • DOI 10.1007/s002530100661
    • R.R. Gokarn, J.D. Evans, J.R. Walker, S.A. Martin, M.A. Eiteman, and E. Altman The physiological effects and metabolic alterations caused by the expression of Rhizobium etli pyruvate carboxylase in Escherichia coli Appl Microbiol Biotechnol 56 2001 188 195 (Pubitemid 32661555)
    • (2001) Applied Microbiology and Biotechnology , vol.56 , Issue.1-2 , pp. 188-195
    • Gokarn, R.R.1    Evans, J.D.2    Walker, J.R.3    Martin, S.A.4    Eiteman, M.A.5    Altman, E.6
  • 49
    • 0029636672 scopus 로고
    • Transport of lactate and acetate through the energized cytoplasmic membrane of Escherichia coli
    • D.D. Axe, and J.E. Bailey Transport of lactate and acetate through the energized cytoplasmic membrane of Escherichia coli Biotechnol Bioeng 47 1995 8 19
    • (1995) Biotechnol Bioeng , vol.47 , pp. 8-19
    • Axe, D.D.1    Bailey, J.E.2
  • 50
    • 0019456997 scopus 로고
    • Change in intracellular pH of Escherichia coli mediates the chemotactic response to certain attractants and repellents
    • D.R. Repaske, and J. Adler Change in intracellular pH of Escherichia coli mediates the chemotactic response to certain attractants and repellents J Bacteriol 145 1981 1196 1208 (Pubitemid 11097336)
    • (1981) Journal of Bacteriology , vol.145 , Issue.3 , pp. 1196-1208
    • Repaske, D.R.1    Adler, J.2
  • 51
    • 0036841201 scopus 로고    scopus 로고
    • Expression of an anaplerotic enzyme, pyruvate carboxylase, improves recombinant protein production in Escherichia coli
    • J.C. March, M.A. Eiteman, and E. Altman Expression of an anaplerotic enzyme, pyruvate carboxylase, improves recombinant protein production in Escherichia coli Appl Environ Microbiol 68 2002 5620 5624 (Pubitemid 35265700)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.11 , pp. 5620-5624
    • March, J.C.1    Eiteman, M.A.2    Altman, E.3
  • 53
    • 0028146781 scopus 로고
    • Stoichiometric flux balance models quantitatively predict growth and metabolic by-product secretion in wild-type Escherichia coli W3110
    • A. Varma, and B.O. Palsson Stoichiometric flux balance models quantitatively predict growth and metabolic by-product secretion in wild-type Escherichia coli W3110 Appl Environ Microbiol 60 1994 3724 3731 (Pubitemid 24298868)
    • (1994) Applied and Environmental Microbiology , vol.60 , Issue.10 , pp. 3724-3731
    • Varma, A.1    Palsson, B.O.2
  • 54
    • 0027209389 scopus 로고
    • Strategies of antioxidant defense
    • H. Sies Strategies of antioxidant defense Eur J Biochem 215 1993 213 219 (Pubitemid 23224303)
    • (1993) European Journal of Biochemistry , vol.215 , Issue.2 , pp. 213-219
    • Sies, H.1
  • 55
    • 2942755215 scopus 로고    scopus 로고
    • Stress induced by recombinant protein production in Escherichia coli
    • F. Hoffmann, and U. Rinas Stress induced by recombinant protein production in Escherichia coli Adv Biochem Eng/Biotechnol 89 2004 73 92
    • (2004) Adv Biochem Eng/Biotechnol , vol.89 , pp. 73-92
    • Hoffmann, F.1    Rinas, U.2
  • 56
    • 0024226522 scopus 로고
    • Escherichia coli heat shock gene mutants are defective in proteolysis
    • D.B. Straus, W.A. Walter, and C.A. Gross Escherichia coli heat shock gene mutants are defective in proteolysis Genes Dev 2 1988 1851 1858
    • (1988) Genes Dev , vol.2 , pp. 1851-1858
    • Straus, D.B.1    Walter, W.A.2    Gross, C.A.3
  • 58
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • E.R. Stadtman Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions Annu Rev Biochem 62 1993 797 821 (Pubitemid 23237888)
    • (1993) Annual Review of Biochemistry , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 59
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • R.T. Dean, S. Fu, R. Stocker, and M.J. Davies Biochemistry and pathology of radical-mediated protein oxidation Biochem J 324 1997 1 18 (Pubitemid 27229359)
    • (1997) Biochemical Journal , vol.324 , Issue.1 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 60
    • 0034545719 scopus 로고    scopus 로고
    • Quantification and significance of protein oxidation in biological samples
    • DOI 10.1081/DMR-100102336
    • E. Shacter Quantification and significance of protein oxidation in biological samples Drug Metab Rev 32 2000 307 326 (Pubitemid 32001909)
    • (2000) Drug Metabolism Reviews , vol.32 , Issue.3-4 , pp. 307-326
    • Shacter, E.1
  • 61
    • 0028999344 scopus 로고
    • Cloning, sequencing and heterologous expression of the monoamine oxidase gene from Aspergillus niger
    • B. Schilling, and K. Lerch Cloning, sequencing and heterologous expression of the monoamine oxidase gene from Aspergillus niger Mol Gen Genet 247 1995 430 438
    • (1995) Mol Gen Genet , vol.247 , pp. 430-438
    • Schilling, B.1    Lerch, K.2
  • 62
    • 0029875931 scopus 로고    scopus 로고
    • The use of t-butyl hydroperoxide as a probe for methionine oxidation in proteins
    • DOI 10.1006/abio.1996.0131
    • R.G. Keck The use of t-butyl hydroperoxide as a probe for methionine oxidation in proteins Anal Biochem 236 1996 56 62 (Pubitemid 26100728)
    • (1996) Analytical Biochemistry , vol.236 , Issue.1 , pp. 56-62
    • Keck, R.G.1
  • 63
    • 0034607619 scopus 로고    scopus 로고
    • Substitution of the critical methionine residues in Trigonopsis variabilis D-amino acid oxidase with leucine enhances its resistance to hydrogen peroxide
    • DOI 10.1016/S0378-1097(00)00151-8, PII S0378109700001518
    • S-S. Ju, L-L. Lin, H.R. Chien, and W-H. Hsu Substitution of the critical methionine residues in Trigonopsis variabilis d-amino acid oxidase with leucine enhances its resistance to hydrogen peroxide FEMS Microbiol Lett 186 2000 215 219 (Pubitemid 30232745)
    • (2000) FEMS Microbiology Letters , vol.186 , Issue.2 , pp. 215-219
    • Ju, S.-S.1    Lin, L.-L.2    Chien, H.R.3    Hsu, W.-H.4
  • 64
    • 29144528214 scopus 로고    scopus 로고
    • Single-site oxidation, cysteine 108 to cysteine sulfinic acid, in D-amino acid oxidase from Trigonopsis variabilis and its structural and functional consequences
    • DOI 10.1128/AEM.71.12.8061-8068.2005
    • A. Slavica, I. Dib, and B. Nidetzky Single-site oxidation, cysteine 108 to cysteine sulfinic acid, in d-amino acid oxidase from Trigonopsis variabilis and its structural and functional consequences Appl Environ Microbiol 71 2005 8061 8068 (Pubitemid 41803929)
    • (2005) Applied and Environmental Microbiology , vol.71 , Issue.12 , pp. 8061-8068
    • Slavica, A.1    Dib, I.2    Nidetzky, B.3
  • 65
    • 0031195153 scopus 로고    scopus 로고
    • Identification of a reactive cysteine in the flavin-binding domain of Rhodotorula gracilis D-amino acid oxidase
    • DOI 10.1006/abbi.1997.0123
    • L. Pollegioni, S. Campaner, A.A. Raibekas, and M.S. Pilone Identification of a reactive cysteine in the flavin-binding domain of Rhodotorula gracilis d-amino acid oxidase Arch Biochem Biophys 343 1997 1 5 (Pubitemid 27274335)
    • (1997) Archives of Biochemistry and Biophysics , vol.343 , Issue.1 , pp. 1-5
    • Pollegioni, L.1    Campaner, S.2    Raibekas, A.A.3    Pilone, M.S.4
  • 66
    • 0034256045 scopus 로고    scopus 로고
    • Effect of hydrogen peroxide on D-amino acid oxidase from Rhodotorula gracilis
    • DOI 10.1016/S0141-0229(00)00222-2, PII S0141022900002222
    • I. de la Mata, F. Ramón, V. Obregón, M.P. Castillón, and C. Acebal Effect of hydrogen peroxide on d-amino acid oxidase from Rhodotorula gracilis Enzyme Microb Technol 27 2000 234 239 (Pubitemid 30427196)
    • (2000) Enzyme and Microbial Technology , vol.27 , Issue.3-5 , pp. 234-239
    • De La Mata, I.1    Ramon, F.2    Obregon, V.3    Castillon, M.P.4    Acebal, C.5
  • 67
    • 0029839452 scopus 로고    scopus 로고
    • Crystal structure of d-amino acid oxidase: A case of active site mirror-image convergent evolution with flavocytochrome b2
    • A. Mattevi, M.A. Vanoni, F. Todone, M. Rizzi, A. Teplyakov, and A. Coda Crystal structure of d-amino acid oxidase: a case of active site mirror-image convergent evolution with flavocytochrome b2 Proc Natl Acad Sci USA 93 1996 7496 7501
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7496-7501
    • Mattevi, A.1    Vanoni, M.A.2    Todone, F.3    Rizzi, M.4    Teplyakov, A.5    Coda, A.6
  • 68
    • 0033054493 scopus 로고    scopus 로고
    • Engineering the D-amino acid oxidase from Trigonopsis variabilis to facilitate its overproduction in Escherichia coli and its downstream processing by tailor-made metal chelate supports
    • DOI 10.1016/S0141-0229(99)00019-8, PII S0141022999000198
    • J. Alonso, J.L. Barredo, P. Armisén, B. Díez, F. Salto, and J.M. Guisán Engineering the d-amino acid oxidase from Trigonopsis variabilis to facilitate its overproduction in Escherichia coli and its downstream processing by tailor-made metal chelate supports Enzyme Microb Technol 25 1999 88 95 (Pubitemid 29299367)
    • (1999) Enzyme and Microbial Technology , vol.25 , Issue.1-2 , pp. 88-95
    • Alonso, J.1    Barredo, J.L.2    Armisen, P.3    Diez, B.4    Salto, F.5    Guisan, J.M.6    Garcia, J.L.7    Cortes, E.8


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