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Volumn 36, Issue 4, 2016, Pages 652-664

Expression of recombinant protein using Corynebacterium Glutamicum: progress, challenges and applications

Author keywords

Corynebacterium glutamicum; genetic alteration of strain; heterologous genes; plasmids; promoters; protein secretion pathways

Indexed keywords

ESCHERICHIA COLI; GENE EXPRESSION; GENE EXPRESSION REGULATION; GENES; PHYSIOLOGY; PROTEINS;

EID: 84975122998     PISSN: 07388551     EISSN: 15497801     Source Type: Journal    
DOI: 10.3109/07388551.2015.1004519     Document Type: Review
Times cited : (62)

References (116)
  • 1
    • 84876976144 scopus 로고    scopus 로고
    • Development of a secretion system for the production of heterologous proteins in Corynebacterium glutamicum using the Porin B signal peptide
    • S.J.An, S.S.Yim, K.J.Jeong. (2013). Development of a secretion system for the production of heterologous proteins in Corynebacterium glutamicum using the Porin B signal peptide. Protein Expr Purif, 89, 251–7
    • (2013) Protein Expr Purif , vol.89 , pp. 251-257
    • An, S.J.1    Yim, S.S.2    Jeong, K.J.3
  • 2
    • 57349106051 scopus 로고    scopus 로고
    • Dictyostelium discoideum – a promising expression system for the production of eukaryotic proteins
    • R.Arya, A.Bhattacharya, K.S.Saini. (2008). Dictyostelium discoideum – a promising expression system for the production of eukaryotic proteins. FASEB J, 22, 4055–66
    • (2008) FASEB J , vol.22 , pp. 4055-4066
    • Arya, R.1    Bhattacharya, A.2    Saini, K.S.3
  • 3
    • 33847207787 scopus 로고    scopus 로고
    • Altered metabolic flux due to deletion of odhA causes L-glutamate overproduction in Corynebacterium glutamicum
    • Y.Asakura, E.Kimura, Y.Usuda,. (2007). Altered metabolic flux due to deletion of odhA causes L-glutamate overproduction in Corynebacterium glutamicum. Appl Environ Microbiol, 73, 1308–19
    • (2007) Appl Environ Microbiol , vol.73 , pp. 1308-1319
    • Asakura, Y.1    Kimura, E.2    Usuda, Y.3
  • 4
    • 68849123047 scopus 로고    scopus 로고
    • Methods for analyzing deep sequencing expression data: constructing the human and mouse promoterome with deep CAGE data
    • P.J.Balwierz, P.Carninci, C.O.Daub,. (2009). Methods for analyzing deep sequencing expression data: constructing the human and mouse promoterome with deep CAGE data. Genome Biol, 10, R79
    • (2009) Genome Biol , vol.10 , pp. 79
    • Balwierz, P.J.1    Carninci, P.2    Daub, C.O.3
  • 5
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • F.Baneyx. (1999). Recombinant protein expression in Escherichia coli. Curr Opin Biotechnol, 10, 411–21
    • (1999) Curr Opin Biotechnol , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 6
    • 84884188636 scopus 로고    scopus 로고
    • Construction of a prophage-free variant of Corynebacterium glutamicum ATCC 13032 for use as a platform strain for basic research and industrial biotechnology
    • M.Baumgart, S.Unthan, C.Rückert,. (2013). Construction of a prophage-free variant of Corynebacterium glutamicum ATCC 13032 for use as a platform strain for basic research and industrial biotechnology. Appl Environ Microbiol, 79, 6006–15
    • (2013) Appl Environ Microbiol , vol.79 , pp. 6006-6015
    • Baumgart, M.1    Unthan, S.2    Rückert, C.3
  • 7
    • 0032901622 scopus 로고    scopus 로고
    • Positively regulated expression of the Escherichia coli araBAD promoter in Corynebacterium glutamicum
    • K.Ben-Samoun, G.Leblon, O.Reyes. (1999). Positively regulated expression of the Escherichia coli araBAD promoter in Corynebacterium glutamicum. FEMS Microbiol Lett, 174, 125–30
    • (1999) FEMS Microbiol Lett , vol.174 , pp. 125-130
    • Ben-Samoun, K.1    Leblon, G.2    Reyes, O.3
  • 9
    • 84876286207 scopus 로고    scopus 로고
    • Current state and recent advances in biopharmaceutical production in Escherichia coli, yeasts and mammalian cells
    • A.Berlec, B.Strukelj. (2013). Current state and recent advances in biopharmaceutical production in Escherichia coli, yeasts and mammalian cells. J Ind Microbiol Biotechnol, 40, 257–74
    • (2013) J Ind Microbiol Biotechnol , vol.40 , pp. 257-274
    • Berlec, A.1    Strukelj, B.2
  • 10
    • 0028942897 scopus 로고
    • Expression and secretion of heterologous proteases by Corynebacterium glutamicum
    • H.Billman-Jacobe, L.Wang, A.Kortt,. (1995). Expression and secretion of heterologous proteases by Corynebacterium glutamicum. Appl Environ Microbiol, 61, 1610–13
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1610-1613
    • Billman-Jacobe, H.1    Wang, L.2    Kortt, A.3
  • 11
    • 0028197267 scopus 로고
    • Expression of ovine gamma interferon in Escherichia coli and Corynebacterium glutamicum
    • H.Billman-Jacobe, A.L.M.Hodgson, M.Lightowlers,. (1994). Expression of ovine gamma interferon in Escherichia coli and Corynebacterium glutamicum. Appl Environ Microbiol, 60, 1641–5
    • (1994) Appl Environ Microbiol , vol.60 , pp. 1641-1645
    • Billman-Jacobe, H.1    Hodgson, A.L.M.2    Lightowlers, M.3
  • 12
    • 80053636591 scopus 로고    scopus 로고
    • High throughput construction and small scale expression screening of multi-tag vectors in Escherichia coli
    • L.E.Bird. (2011). High throughput construction and small scale expression screening of multi-tag vectors in Escherichia coli. Methods, 55, 29–37
    • (2011) Methods , vol.55 , pp. 29-37
    • Bird, L.E.1
  • 13
    • 0025726498 scopus 로고
    • Studies on the utilization of lactose by Corynebacterium glutamicum, bearing the lactose operon of Escherichia coli
    • W.Brabetz, W.Liebl, K.H.Schleifer. (1991). Studies on the utilization of lactose by Corynebacterium glutamicum, bearing the lactose operon of Escherichia coli. Arch Microbiol, 155, 607–12
    • (1991) Arch Microbiol , vol.155 , pp. 607-612
    • Brabetz, W.1    Liebl, W.2    Schleifer, K.H.3
  • 14
    • 84865594326 scopus 로고    scopus 로고
    • Transcriptional regulation of the operon encoding stress-responsive ECF sigma factor SigH and its anti-sigma factor RshA, and control of its regulatory network in Corynebacterium glutamicum
    • T.Busche, R.Šilar, M.Picˇmanová,. (2012). Transcriptional regulation of the operon encoding stress-responsive ECF sigma factor SigH and its anti-sigma factor RshA, and control of its regulatory network in Corynebacterium glutamicum. BMC Genomics, 13, 445
    • (2012) BMC Genomics , vol.13 , pp. 445
    • Busche, T.1    Šilar, R.2    Picˇmanová, M.3
  • 15
    • 79957987053 scopus 로고    scopus 로고
    • Proteomic screening of anaerobically regulated promoters from Salmonella and its antitumor applications
    • J.Chen, D.Wei, H.Zhuang,. (2011). Proteomic screening of anaerobically regulated promoters from Salmonella and its antitumor applications. Mol Cell Proteomics, 10, M111.009399
    • (2011) Mol Cell Proteomics , vol.10
    • Chen, J.1    Wei, D.2    Zhuang, H.3
  • 16
    • 84897604263 scopus 로고    scopus 로고
    • Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system
    • S.Costa, A.Almeida, A.Castro, L.Domingues. (2014). Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system. Front Microbiol, 5, 63
    • (2014) Front Microbiol , vol.5 , pp. 63
    • Costa, S.1    Almeida, A.2    Castro, A.3    Domingues, L.4
  • 17
    • 84857455818 scopus 로고    scopus 로고
    • Recombinant protein vaccines produced in insect cells
    • M.M.Cox. (2012). Recombinant protein vaccines produced in insect cells. Vaccine, 30, 1759–66
    • (2012) Vaccine , vol.30 , pp. 1759-1766
    • Cox, M.M.1
  • 18
    • 84975145264 scopus 로고    scopus 로고
    • Prediction of soluble heterologous protein expression levels in Escherichia coli from sequence-based features and its potential in biopharmaceutical process development
    • X.Dai, G.Wenwen, Q.Long,. (2014). Prediction of soluble heterologous protein expression levels in Escherichia coli from sequence-based features and its potential in biopharmaceutical process development. Pharm Bioprocess, 2, 253–66
    • (2014) Pharm Bioprocess , vol.2 , pp. 253-266
    • Dai, X.1    Wenwen, G.2    Long, Q.3
  • 19
    • 0026453267 scopus 로고
    • Signal peptidases in prokaryotes and eukaryotes – a new protease family
    • R.E.Dalbey, G.Von Heijne. (1992). Signal peptidases in prokaryotes and eukaryotes – a new protease family. Trends Biochem Sci, 17, 474–8
    • (1992) Trends Biochem Sci , vol.17 , pp. 474-478
    • Dalbey, R.E.1    Von Heijne, G.2
  • 20
    • 0030998468 scopus 로고    scopus 로고
    • The chemistry and enzymology of the type I signal peptidases
    • R.E.Dalbey, M.O.Lively, S.Bron, J.M.van Dijl. (1997). The chemistry and enzymology of the type I signal peptidases. Protein Sci, 6, 1129–38
    • (1997) Protein Sci , vol.6 , pp. 1129-1138
    • Dalbey, R.E.1    Lively, M.O.2    Bron, S.3    van Dijl, J.M.4
  • 21
    • 0032432109 scopus 로고    scopus 로고
    • Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli
    • P.N.Danese, T.J.Silhavy. (1998). Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli. Annu Rev Genet, 32, 59–94
    • (1998) Annu Rev Genet , vol.32 , pp. 59-94
    • Danese, P.N.1    Silhavy, T.J.2
  • 22
    • 33645229632 scopus 로고    scopus 로고
    • Secretion of human epidermal growth factor by Corynebacterium glutamicum
    • M.Date, H.Itaya, H.Matsui, Y.Kikuchi. (2006). Secretion of human epidermal growth factor by Corynebacterium glutamicum. Lett Appl Microbiol, 42, 66–70
    • (2006) Lett Appl Microbiol , vol.42 , pp. 66-70
    • Date, M.1    Itaya, H.2    Matsui, H.3    Kikuchi, Y.4
  • 23
    • 0038219967 scopus 로고    scopus 로고
    • Production of Native-Type Streptoverticillium mobaraense Transglutaminase in Corynebacterium glutamicum
    • M.Date, K.Yokoyama, K.Umezawa,. (2003). Production of Native-Type Streptoverticillium mobaraense Transglutaminase in Corynebacterium glutamicum. Appl Environ Microbiol, 69, 3011–14
    • (2003) Appl Environ Microbiol , vol.69 , pp. 3011-3014
    • Date, M.1    Yokoyama, K.2    Umezawa, K.3
  • 24
    • 0025912270 scopus 로고
    • A family of Corynebacterium glutamicum/Escherichia coli shuttle vectors for cloning, controlled gene expression, and promoter probing
    • B.J.Eikmanns, E.Kleinertz, W.Liebl, H.Sahm. (1991). A family of Corynebacterium glutamicum/Escherichia coli shuttle vectors for cloning, controlled gene expression, and promoter probing. Gene, 102, 93–8
    • (1991) Gene , vol.102 , pp. 93-98
    • Eikmanns, B.J.1    Kleinertz, E.2    Liebl, W.3    Sahm, H.4
  • 25
    • 84917732539 scopus 로고    scopus 로고
    • Quality by design for biopharmaceuticals: a historical review and guide for implementation
    • P.Elliott, S.Billingham, J.Bi, H.Zhang. (2013). Quality by design for biopharmaceuticals: a historical review and guide for implementation. Pharm Bioprocess, 1, 105–22
    • (2013) Pharm Bioprocess , vol.1 , pp. 105-122
    • Elliott, P.1    Billingham, S.2    Bi, J.3    Zhang, H.4
  • 26
    • 0033008601 scopus 로고    scopus 로고
    • Protein targeting to the bacterial cytoplasmic membrane
    • P.Fekkes, A.J.M.Driessen. (1999). Protein targeting to the bacterial cytoplasmic membrane. Microbiol Mol Biol Rev, 63, 161–73
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 161-173
    • Fekkes, P.1    Driessen, A.J.M.2
  • 27
    • 33845946823 scopus 로고    scopus 로고
    • Protein secretion pathways in Bacillus subtilis: implication for optimization of heterologous protein secretion
    • L.L.Fu, Z.R.Xu, W.F.Li,. (2007). Protein secretion pathways in Bacillus subtilis: implication for optimization of heterologous protein secretion. Biotechnol Adv, 25, 1–12
    • (2007) Biotechnol Adv , vol.25 , pp. 1-12
    • Fu, L.L.1    Xu, Z.R.2    Li, W.F.3
  • 28
    • 0037173615 scopus 로고    scopus 로고
    • Functional profiling of the Saccharomyces cerevisiae genome
    • G.Giaever, A.M.Chu, L.Ni,. (2002). Functional profiling of the Saccharomyces cerevisiae genome. Nature, 418, 387–91
    • (2002) Nature , vol.418 , pp. 387-391
    • Giaever, G.1    Chu, A.M.2    Ni, L.3
  • 29
    • 84884587189 scopus 로고    scopus 로고
    • Strategies for the production of recombinant protein in Escherichia coli
    • G.J.Gopal, A.Kumar. (2013). Strategies for the production of recombinant protein in Escherichia coli. Protein J, 32, 419–25
    • (2013) Protein J , vol.32 , pp. 419-425
    • Gopal, G.J.1    Kumar, A.2
  • 30
    • 0242692671 scopus 로고    scopus 로고
    • Multiple sigma subunits and the partitioning of bacterial transcription space
    • T.M.Gruber, C.A.Gross. (2003). Multiple sigma subunits and the partitioning of bacterial transcription space. Annu Rev Microbiol, 57, 441–66
    • (2003) Annu Rev Microbiol , vol.57 , pp. 441-466
    • Gruber, T.M.1    Gross, C.A.2
  • 31
    • 0033014686 scopus 로고    scopus 로고
    • Expression of the Escherichia coli catabolic threonine dehydratase in Corynebacterium glutamicum and its effect on isoleucine production
    • S.Guillouet, A.A.Rodal, G.An,. (1999). Expression of the Escherichia coli catabolic threonine dehydratase in Corynebacterium glutamicum and its effect on isoleucine production. Appl Environ Microbiol, 65, 3100–7
    • (1999) Appl Environ Microbiol , vol.65 , pp. 3100-3107
    • Guillouet, S.1    Rodal, A.A.2    An, G.3
  • 32
    • 67349144044 scopus 로고    scopus 로고
    • A game with many players: control of gdh transcription in Corynebacterium glutamicum
    • E.Hänssler, T.Müller, K.Palumbo,. (2009). A game with many players: control of gdh transcription in Corynebacterium glutamicum. J Biotechnol, 142, 114–22
    • (2009) J Biotechnol , vol.142 , pp. 114-122
    • Hänssler, E.1    Müller, T.2    Palumbo, K.3
  • 33
    • 84975103758 scopus 로고    scopus 로고
    • Heo A, Park W. (2014). Expression of the mexA gene requires the DNA helicase RecG in Pseudomonas aeruginosa PAO1. J Microbiol Biotechnol. 24(7)
  • 34
    • 0041429540 scopus 로고    scopus 로고
    • Industrial production of amino acids by coryneform bacteria
    • T.Hermann. (2003). Industrial production of amino acids by coryneform bacteria. J Biotechnol, 104, 155–72
    • (2003) J Biotechnol , vol.104 , pp. 155-172
    • Hermann, T.1
  • 35
    • 77957370151 scopus 로고    scopus 로고
    • The E2 domain of OdhA of Corynebacterium glutamicum has succinyl transferase activity dependent on lipoyl residues of the acetyl transferase AceF
    • M.Hoffelder, K.Raasch, J.van Ooyen, L.Eggeling. (2010). The E2 domain of OdhA of Corynebacterium glutamicum has succinyl transferase activity dependent on lipoyl residues of the acetyl transferase AceF. J Bacteriol, 192, 5203–11
    • (2010) J Bacteriol , vol.192 , pp. 5203-5211
    • Hoffelder, M.1    Raasch, K.2    van Ooyen, J.3    Eggeling, L.4
  • 36
    • 58849131897 scopus 로고    scopus 로고
    • Metabolic engineering of the L-valine biosynthesis pathway in Corynebacterium glutamicum using promoter activity modulation
    • J.Holátko, V.Elišáková, M.Prouza,. (2009). Metabolic engineering of the L-valine biosynthesis pathway in Corynebacterium glutamicum using promoter activity modulation. J Biotechnol, 139, 203–10
    • (2009) J Biotechnol , vol.139 , pp. 203-210
    • Holátko, J.1    Elišáková, V.2    Prouza, M.3
  • 37
    • 77950601340 scopus 로고    scopus 로고
    • Replication methods and tools in high throughput cultivation processes – recognizing potential variations of growth and product formation by on-line monitoring
    • R.Huber, T.G.Palmen, N.Ryk,. (2010). Replication methods and tools in high throughput cultivation processes – recognizing potential variations of growth and product formation by on-line monitoring. BMC Biotechnology, 10, 22
    • (2010) BMC Biotechnology , vol.10 , pp. 22
    • Huber, R.1    Palmen, T.G.2    Ryk, N.3
  • 38
    • 0032774281 scopus 로고    scopus 로고
    • Construction and application of new Corynebacterium glutamicum vectors
    • M.Jakoby, C.E.Ngouoto-Nkili, A.Burkovski. (1999). Construction and application of new Corynebacterium glutamicum vectors. Biotechnol Tech, 13, 437–41
    • (1999) Biotechnol Tech , vol.13 , pp. 437-441
    • Jakoby, M.1    Ngouoto-Nkili, C.E.2    Burkovski, A.3
  • 39
    • 38149112546 scopus 로고    scopus 로고
    • Improvement of poly (3-hydroxybutyrate)[P(3HB)] production in Corynebacterium glutamicum by codon optimization, point mutation and gene dosage of P (3HB) biosynthetic genes
    • S.-J.Jo, K.I.Matsumoto, C.R.Leong,. (2007). Improvement of poly (3-hydroxybutyrate)[P(3HB)] production in Corynebacterium glutamicum by codon optimization, point mutation and gene dosage of P (3HB) biosynthetic genes. J Biosci Bioeng, 104, 457–63
    • (2007) J Biosci Bioeng , vol.104 , pp. 457-463
    • Jo, S.-J.1    Matsumoto, K.I.2    Leong, C.R.3
  • 40
    • 84900789966 scopus 로고    scopus 로고
    • High-level expression in Corynebacterium glutamicum of nitrile hydratase from Rhodococcus rhodochrous for acrylamide production
    • M.S.Kang, S.S.Han, M.Y.Kim,. (2014). High-level expression in Corynebacterium glutamicum of nitrile hydratase from Rhodococcus rhodochrous for acrylamide production. Appl Microbiol Biotechnol, 98, 4379–87
    • (2014) Appl Microbiol Biotechnol , vol.98 , pp. 4379-4387
    • Kang, M.S.1    Han, S.S.2    Kim, M.Y.3
  • 41
    • 0037229834 scopus 로고    scopus 로고
    • Secretion of active-form Streptoverticillium mobaraense transglutaminase by Corynebacterium glutamicum: processing of the pro-transglutaminase by a cosecreted subtilisin-like protease from Streptomyces albogriseolus
    • Y.Kikuchi, M.Date, K.Yokoyama,. (2003). Secretion of active-form Streptoverticillium mobaraense transglutaminase by Corynebacterium glutamicum: processing of the pro-transglutaminase by a cosecreted subtilisin-like protease from Streptomyces albogriseolus. Appl Environ Microbiol, 69, 358–66
    • (2003) Appl Environ Microbiol , vol.69 , pp. 358-366
    • Kikuchi, Y.1    Date, M.2    Yokoyama, K.3
  • 42
    • 38349189461 scopus 로고    scopus 로고
    • Production of Chryseobacterium proteolyticum protein-glutaminase using the twin-arginine translocation pathway in Corynebacterium glutamicum
    • Y.Kikuchi, H.Itaya, M.Date,. (2008). Production of Chryseobacterium proteolyticum protein-glutaminase using the twin-arginine translocation pathway in Corynebacterium glutamicum. Appl Microbiol Biotechnol, 78, 67–74
    • (2008) Appl Microbiol Biotechnol , vol.78 , pp. 67-74
    • Kikuchi, Y.1    Itaya, H.2    Date, M.3
  • 43
    • 59649085581 scopus 로고    scopus 로고
    • TatABC overexpression improves Corynebacterium glutamicum Tat-dependent protein secretion
    • Y.Kikuchi, H.Itaya, M.Date,. (2009). TatABC overexpression improves Corynebacterium glutamicum Tat-dependent protein secretion. Appl Environ Microbiol, 75, 603–7
    • (2009) Appl Environ Microbiol , vol.75 , pp. 603-607
    • Kikuchi, Y.1    Itaya, H.2    Date, M.3
  • 44
    • 77953231876 scopus 로고    scopus 로고
    • Systems-wide metabolic pathway engineering in Corynebacterium glutamicum for bio-based production of diaminopentane
    • S.Kind, W.K.Jeong, H.Schröder, C.Wittmann. (2010). Systems-wide metabolic pathway engineering in Corynebacterium glutamicum for bio-based production of diaminopentane. Metab Eng, 12, 341–51
    • (2010) Metab Eng , vol.12 , pp. 341-351
    • Kind, S.1    Jeong, W.K.2    Schröder, H.3    Wittmann, C.4
  • 45
    • 0041429497 scopus 로고    scopus 로고
    • Tools for genetic engineering in the amino acid-producing bacterium Corynebacterium glutamicum
    • O.Kirchner, A.Tauch. (2003). Tools for genetic engineering in the amino acid-producing bacterium Corynebacterium glutamicum. J Biotechnol, 104, 287–99
    • (2003) J Biotechnol , vol.104 , pp. 287-299
    • Kirchner, O.1    Tauch, A.2
  • 47
    • 76149090497 scopus 로고    scopus 로고
    • Increased glucose utilization in Corynebacterium glutamicum by use of maltose, and its application for the improvement of L-valine productivity
    • F.S.Krause, A.Henrich, B.Blombach,. (2010). Increased glucose utilization in Corynebacterium glutamicum by use of maltose, and its application for the improvement of L-valine productivity. Appl Environ Microbiol, 76, 370–4
    • (2010) Appl Environ Microbiol , vol.76 , pp. 370-374
    • Krause, F.S.1    Henrich, A.2    Blombach, B.3
  • 48
    • 0026553915 scopus 로고
    • Expression, secretion, and processing of staphylococcal nuclease by Corynebacterium glutamicum
    • W.Liebl, A.J.Sinskey, K.H.Schleifer. (1992). Expression, secretion, and processing of staphylococcal nuclease by Corynebacterium glutamicum. J Bacteriol, 174, 1854–61
    • (1992) J Bacteriol , vol.174 , pp. 1854-1861
    • Liebl, W.1    Sinskey, A.J.2    Schleifer, K.H.3
  • 49
    • 84879840065 scopus 로고    scopus 로고
    • Developing Bacillus spp. as a cell factory for production of microbial enzymes and industrially important biochemicals in the context of systems and synthetic biology
    • L.Liu, Y.Liu, H.-D.Shin,. (2013a). Developing Bacillus spp. as a cell factory for production of microbial enzymes and industrially important biochemicals in the context of systems and synthetic biology. Appl Microbiol Biotechnol, 97, 6113–27
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 6113-6127
    • Liu, L.1    Liu, Y.2    Shin, H.-D.3
  • 50
    • 84888018033 scopus 로고    scopus 로고
    • Recent advances in recombinant protein expression by Corynebacterium, Brevibacterium, and Streptomyces: from transcription and translation regulation to secretion pathway selection
    • L.Liu, H.Yang, H.-D.Shin,. (2013b). Recent advances in recombinant protein expression by Corynebacterium, Brevibacterium, and Streptomyces: from transcription and translation regulation to secretion pathway selection. Appl Microbiol Biotechnol, 97, 9597–608
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 9597-9608
    • Liu, L.1    Yang, H.2    Shin, H.-D.3
  • 51
    • 35449001633 scopus 로고    scopus 로고
    • The impact of PHB accumulation on L-glutamate production by recombinant Corynebacterium glutamicum
    • Q.Liu, S.P.Ouyang, J.Kim, G.Q.Chen. (2007). The impact of PHB accumulation on L-glutamate production by recombinant Corynebacterium glutamicum. J Biotechnol, 132, 273–9
    • (2007) J Biotechnol , vol.132 , pp. 273-279
    • Liu, Q.1    Ouyang, S.P.2    Kim, J.3    Chen, G.Q.4
  • 52
    • 84861020284 scopus 로고    scopus 로고
    • Construction of recombinant Corynebacterium glutamicum for L-threonine production
    • Y.Lv, Z.Wu, S.Han,. (2012). Construction of recombinant Corynebacterium glutamicum for L-threonine production. Biotechnol Bioprocess Eng, 17, 16–21
    • (2012) Biotechnol Bioprocess Eng , vol.17 , pp. 16-21
    • Lv, Y.1    Wu, Z.2    Han, S.3
  • 53
    • 84902674083 scopus 로고    scopus 로고
    • Development and characterization of a cell culture manufacturing process using quality by design (QbD) principles
    • D.M.Marasco, J.Gao, K.Griffiths,. (2013). Development and characterization of a cell culture manufacturing process using quality by design (QbD) principles. Adv Biochem Eng Biotechnol, 39, 93–121
    • (2013) Adv Biochem Eng Biotechnol , vol.39 , pp. 93-121
    • Marasco, D.M.1    Gao, J.2    Griffiths, K.3
  • 54
    • 84899647641 scopus 로고    scopus 로고
    • Double mutation of cell wall proteins CspB and PBP1a increases secretion of the antibody Fab fragment from Corynebacterium glutamicum
    • Y.Matsuda, H.Itaya, Y.Kitahara,. (2014). Double mutation of cell wall proteins CspB and PBP1a increases secretion of the antibody Fab fragment from Corynebacterium glutamicum. Microb Cell Fact, 13, 56
    • (2014) Microb Cell Fact , vol.13 , pp. 56
    • Matsuda, Y.1    Itaya, H.2    Kitahara, Y.3
  • 55
    • 84855932983 scopus 로고    scopus 로고
    • Recombinant protein production in yeasts. Recombinant gene expression
    • D.Mattanovich, P.Branduardi, L.Dato,. (2012). Recombinant protein production in yeasts. Recombinant gene expression. Methods Mol Biol, 824, 329–58
    • (2012) Methods Mol Biol , vol.824 , pp. 329-358
    • Mattanovich, D.1    Branduardi, P.2    Dato, L.3
  • 56
    • 34548019942 scopus 로고    scopus 로고
    • Comparative analysis of twin-arginine (Tat)-dependent protein secretion of a heterologous model protein (GFP) in three different Gram-positive bacteria
    • D.Meissner, A.Vollstedt, J.M.van Dijl, R.Freudl. (2007). Comparative analysis of twin-arginine (Tat)-dependent protein secretion of a heterologous model protein (GFP) in three different Gram-positive bacteria. Appl Microbiol Biotechnol, 76, 633–42
    • (2007) Appl Microbiol Biotechnol , vol.76 , pp. 633-642
    • Meissner, D.1    Vollstedt, A.2    van Dijl, J.M.3    Freudl, R.4
  • 57
    • 84862565273 scopus 로고    scopus 로고
    • Potentials and limitations of prokaryotic and eukaryotic expression systems for recombinant protein production – a comparative view
    • D.Müller, K.Bayer, D.Mattanovich. (2006). Potentials and limitations of prokaryotic and eukaryotic expression systems for recombinant protein production – a comparative view. Microb Cell Fact, 5, P61
    • (2006) Microb Cell Fact , vol.5 , pp. 61
    • Müller, D.1    Bayer, K.2    Mattanovich, D.3
  • 58
    • 79958149403 scopus 로고    scopus 로고
    • Tools for genetic manipulations in Corynebacterium glutamicum and their applications
    • J.Nešvera, M.Pátek. (2011). Tools for genetic manipulations in Corynebacterium glutamicum and their applications. Appl Microbiol Biotechnol, 90, 1641–54
    • (2011) Appl Microbiol Biotechnol , vol.90 , pp. 1641-1654
    • Nešvera, J.1    Pátek, M.2
  • 59
    • 77955947553 scopus 로고    scopus 로고
    • Recent advances in the production of proteins in insect and mammalian cells for structural biology
    • J.E.Nettleship, R.Assenberg, J.M.Diprose,. (2010). Recent advances in the production of proteins in insect and mammalian cells for structural biology. J Struct Biol, 172, 55–65
    • (2010) J Struct Biol , vol.172 , pp. 55-65
    • Nettleship, J.E.1    Assenberg, R.2    Diprose, J.M.3
  • 60
    • 74049087374 scopus 로고    scopus 로고
    • Isolation, evaluation and use of two strong, carbon source-inducible promoters from Corynebacterium glutamicum
    • N.Okibe, N.Suzuki, M.Inui, H.Yukawa. (2010). Isolation, evaluation and use of two strong, carbon source-inducible promoters from Corynebacterium glutamicum. Lett Appl Microbiol, 50, 173–80
    • (2010) Lett Appl Microbiol , vol.50 , pp. 173-180
    • Okibe, N.1    Suzuki, N.2    Inui, M.3    Yukawa, H.4
  • 61
    • 80053455434 scopus 로고    scopus 로고
    • A screening strategy for heterologous protein expression in Escherichia coli with the highest return of investment
    • B.Pacheco, L.Crombet, P.Loppnau, D.Cossar. (2012). A screening strategy for heterologous protein expression in Escherichia coli with the highest return of investment. Protein Expr Purif, 81, 33–41
    • (2012) Protein Expr Purif , vol.81 , pp. 33-41
    • Pacheco, B.1    Crombet, L.2    Loppnau, P.3    Cossar, D.4
  • 62
    • 48649095463 scopus 로고    scopus 로고
    • Construction of heat-inducible expression vector of Corynebacterium glutamicum and C. ammoniagenes: fusion of lambda operator with promoters isolated from C. ammoniagenes
    • J.U.Park, J.H.Jo, Y.J.Kim,. (2008). Construction of heat-inducible expression vector of Corynebacterium glutamicum and C. ammoniagenes: fusion of lambda operator with promoters isolated from C. ammoniagenes. J Microbiol Biotechnol, 18, 639–47
    • (2008) J Microbiol Biotechnol , vol.18 , pp. 639-647
    • Park, J.U.1    Jo, J.H.2    Kim, Y.J.3
  • 63
    • 84873979435 scopus 로고    scopus 로고
    • Corynebacterium glutamicum promoters: a practical approach
    • M.Pátek, J.Holátko, T.Busche,. (2013). Corynebacterium glutamicum promoters: a practical approach. Microb Biotechnol, 6, 103–17
    • (2013) Microb Biotechnol , vol.6 , pp. 103-117
    • Pátek, M.1    Holátko, J.2    Busche, T.3
  • 64
    • 84891852230 scopus 로고    scopus 로고
    • Promoters and plasmid vectors of Corynebacterium glutamicum
    • Yukawa H., Inui M., (eds), Heidelberg: Springer
    • M.Pátek, J.Nešvera. (2012). Promoters and plasmid vectors of Corynebacterium glutamicum. In: H.Yukawa, M.Inui, eds. Corynebacterium glutamicum: biology and biotechnology. Heidelberg: Springer, 51–88
    • (2012) Corynebacterium glutamicum: biology and biotechnology , pp. 51-88
    • Pátek, M.1    Nešvera, J.2
  • 65
    • 0041429496 scopus 로고    scopus 로고
    • Promoters of Corynebacterium glutamicum
    • M.Pátek, J.Nešvera, A.Guyonvarch,. (2003). Promoters of Corynebacterium glutamicum. J Biotechnol, 104, 311–23
    • (2003) J Biotechnol , vol.104 , pp. 311-323
    • Pátek, M.1    Nešvera, J.2    Guyonvarch, A.3
  • 66
    • 0035079744 scopus 로고    scopus 로고
    • Pyruvate carboxylase is a major bottleneck for glutamate and lysine production by Corynebacterium glutamicum
    • P.G.Peters-Wendisch, B.Schiel, V.F.Wendisch,. (2001). Pyruvate carboxylase is a major bottleneck for glutamate and lysine production by Corynebacterium glutamicum. J Mol Microbiol Biotechnol, 3, 295–300
    • (2001) J Mol Microbiol Biotechnol , vol.3 , pp. 295-300
    • Peters-Wendisch, P.G.1    Schiel, B.2    Wendisch, V.F.3
  • 67
    • 84885566725 scopus 로고    scopus 로고
    • A novel type of N-acetylglutamate synthase is involved in the first step of arginine biosynthesis in Corynebacterium glutamicum
    • K.Petri, F.Walter, M.Persicke,. (2013). A novel type of N-acetylglutamate synthase is involved in the first step of arginine biosynthesis in Corynebacterium glutamicum. BMC Genomics, 14, 713
    • (2013) BMC Genomics , vol.14 , pp. 713
    • Petri, K.1    Walter, F.2    Persicke, M.3
  • 68
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • W.A.Prinz, F.Aslund, A.Holmgren, J.Beckwith. (1997). The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. J Biol Chem, 272, 15661–7
    • (1997) J Biol Chem , vol.272 , pp. 15661-15667
    • Prinz, W.A.1    Aslund, F.2    Holmgren, A.3    Beckwith, J.4
  • 69
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • A.P.Pugsley. (1993). The complete general secretory pathway in gram-negative bacteria. Microbiol Rev, 57, 50–108
    • (1993) Microbiol Rev , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 70
    • 84895131301 scopus 로고    scopus 로고
    • High-throughput screening of a Corynebacterium glutamicum mutant library on genomic and metabolic level
    • L.C.Reimer, J.Spura, K.Schmidt-Hohagen, D.Schomburg. (2014). High-throughput screening of a Corynebacterium glutamicum mutant library on genomic and metabolic level. PLoS One, 9, e86799
    • (2014) PLoS One , vol.9 , pp. 86799
    • Reimer, L.C.1    Spura, J.2    Schmidt-Hohagen, K.3    Schomburg, D.4
  • 71
    • 84868259526 scopus 로고    scopus 로고
    • An automated workflow for enhancing microbial bioprocess optimization on a novel microbioreactor platform
    • P.Rohe, D.Venkanna, B.Kleine,. (2012). An automated workflow for enhancing microbial bioprocess optimization on a novel microbioreactor platform. Microb Cell Fact, 11, 144
    • (2012) Microb Cell Fact , vol.11 , pp. 144
    • Rohe, P.1    Venkanna, D.2    Kleine, B.3
  • 72
    • 68349139714 scopus 로고    scopus 로고
    • Optimization of human D-amino acid oxidase expression in Escherichia coli
    • D.Romano, G.Molla, L.Pollegioni, F.Marinelli. (2009). Optimization of human D-amino acid oxidase expression in Escherichia coli. Protein Expr Purif, 68, 72–8
    • (2009) Protein Expr Purif , vol.68 , pp. 72-78
    • Romano, D.1    Molla, G.2    Pollegioni, L.3    Marinelli, F.4
  • 73
    • 84907820245 scopus 로고    scopus 로고
    • Synthetic promoter libraries for Corynebacterium glutamicum
    • J.V.Rytter, S.Helmark, J.Chen,. (2014). Synthetic promoter libraries for Corynebacterium glutamicum. Appl Microbiol Biotechnol, 98, 2617–23
    • (2014) Appl Microbiol Biotechnol , vol.98 , pp. 2617-2623
    • Rytter, J.V.1    Helmark, S.2    Chen, J.3
  • 74
    • 77955714515 scopus 로고    scopus 로고
    • Protein folding and aggregation in bacteria
    • R.Sabate, N.S.De Groot, S.Ventura. (2010). Protein folding and aggregation in bacteria. Cell Mol Life Sci, 67, 2695–715
    • (2010) Cell Mol Life Sci , vol.67 , pp. 2695-2715
    • Sabate, R.1    De Groot, N.S.2    Ventura, S.3
  • 75
    • 0030658935 scopus 로고    scopus 로고
    • Heterologous expression of the Mycobacterium tuberculosis gene encoding antigen 85A in Corynebacterium glutamicum
    • K.Salim, V.Haedens, J.Content,. (1997). Heterologous expression of the Mycobacterium tuberculosis gene encoding antigen 85A in Corynebacterium glutamicum. Appl Environ Microbiol, 63, 4392–400
    • (1997) Appl Environ Microbiol , vol.63 , pp. 4392-4400
    • Salim, K.1    Haedens, V.2    Content, J.3
  • 76
    • 84872410762 scopus 로고    scopus 로고
    • Analysis of the landscape of biologically-derived pharmaceuticals in Europe: dominant production systems, molecule types on the rise and approval trends
    • K.Sarantos, K.Cleo. (2013). Analysis of the landscape of biologically-derived pharmaceuticals in Europe: dominant production systems, molecule types on the rise and approval trends. Eur J Pharm Sci, 48, 428–41
    • (2013) Eur J Pharm Sci , vol.48 , pp. 428-441
    • Sarantos, K.1    Cleo, K.2
  • 77
    • 48449096521 scopus 로고    scopus 로고
    • Distinct roles of two anaplerotic pathways in glutamate production induced by biotin limitation in Corynebacterium glutamicum
    • H.Sato, K.Orishimo, T.Shirai,. (2008). Distinct roles of two anaplerotic pathways in glutamate production induced by biotin limitation in Corynebacterium glutamicum. J Biosci Bioeng, 106, 51–8
    • (2008) J Biosci Bioeng , vol.106 , pp. 51-58
    • Sato, H.1    Orishimo, K.2    Shirai, T.3
  • 78
    • 70349759364 scopus 로고    scopus 로고
    • Plants as bioreactors: recent developments and emerging opportunities
    • A.K.Sharma, M.K.Sharma. (2009). Plants as bioreactors: recent developments and emerging opportunities. Biotechnol Adv, 27, 811–32
    • (2009) Biotechnol Adv , vol.27 , pp. 811-832
    • Sharma, A.K.1    Sharma, M.K.2
  • 79
    • 0037008113 scopus 로고    scopus 로고
    • Construction of fusion vectors of corynebacteria: expression of glutathione-S-transferase fusion protein in Corynebacterium acetoacidophilum ATCC 21476
    • P.Srivastava, J.K.Deb. (2002). Construction of fusion vectors of corynebacteria: expression of glutathione-S-transferase fusion protein in Corynebacterium acetoacidophilum ATCC 21476. FEMS Microbiol Lett, 212, 209–16
    • (2002) FEMS Microbiol Lett , vol.212 , pp. 209-216
    • Srivastava, P.1    Deb, J.K.2
  • 80
    • 14844336971 scopus 로고    scopus 로고
    • Gene expression systems in corynebacteria
    • P.Srivastava, J.K.Deb. (2005). Gene expression systems in corynebacteria. Protein Expr Purif, 40, 221–9
    • (2005) Protein Expr Purif , vol.40 , pp. 221-229
    • Srivastava, P.1    Deb, J.K.2
  • 81
    • 79251605548 scopus 로고    scopus 로고
    • Transformation of, and heterologous protein expression in, Lactobacillus agilis and Lactobacillus vaginalis isolates from the chicken gastrointestinal tract
    • D.P.Stephenson, R.J.Moore, G.E.Allison. (2011). Transformation of, and heterologous protein expression in, Lactobacillus agilis and Lactobacillus vaginalis isolates from the chicken gastrointestinal tract. Appl Environ Microbiol, 77, 220–8
    • (2011) Appl Environ Microbiol , vol.77 , pp. 220-228
    • Stephenson, D.P.1    Moore, R.J.2    Allison, G.E.3
  • 82
    • 36348932173 scopus 로고    scopus 로고
    • Site-directed integration system using a combination of mutant lox sites for Corynebacterium glutamicum
    • N.Suzuki, M.Inui, H.Yukawa. (2007). Site-directed integration system using a combination of mutant lox sites for Corynebacterium glutamicum. Appl Microbiol Biotechnol, 77, 871–8
    • (2007) Appl Microbiol Biotechnol , vol.77 , pp. 871-878
    • Suzuki, N.1    Inui, M.2    Yukawa, H.3
  • 83
    • 80052934431 scopus 로고    scopus 로고
    • High-throughput transposon mutagenesis of Corynebacterium glutamicum
    • N.Suzuki, M.Inui, H.Yukawa. (2011). High-throughput transposon mutagenesis of Corynebacterium glutamicum. Methods Mol Biol, 765, 409–17
    • (2011) Methods Mol Biol , vol.765 , pp. 409-417
    • Suzuki, N.1    Inui, M.2    Yukawa, H.3
  • 84
    • 29144438996 scopus 로고    scopus 로고
    • New multiple-deletion method for the Corynebacterium glutamicum genome, using a mutant lox sequence
    • N.Suzuki, H.Nonaka, Y.Tsuge,. (2005a). New multiple-deletion method for the Corynebacterium glutamicum genome, using a mutant lox sequence. Appl Environ Microbiol, 71, 8472–80
    • (2005) Appl Environ Microbiol , vol.71 , pp. 8472-8480
    • Suzuki, N.1    Nonaka, H.2    Tsuge, Y.3
  • 85
    • 29144440227 scopus 로고    scopus 로고
    • Multiple large segment deletion method for Corynebacterium glutamicum
    • N.Suzuki, H.Nonaka, Y.Tsuge,. (2005b). Multiple large segment deletion method for Corynebacterium glutamicum. Appl Microbiol Biotechnol, 69, 151–61
    • (2005) Appl Microbiol Biotechnol , vol.69 , pp. 151-161
    • Suzuki, N.1    Nonaka, H.2    Tsuge, Y.3
  • 86
    • 33646594074 scopus 로고    scopus 로고
    • High-throughput transposon mutagenesis of Corynebacterium glutamicum and construction of a single-gene disruptant mutant library
    • N.Suzuki, N.Okai, H.Nonaka,. (2006). High-throughput transposon mutagenesis of Corynebacterium glutamicum and construction of a single-gene disruptant mutant library. Appl Environ Microbiol, 72, 3750–5
    • (2006) Appl Environ Microbiol , vol.72 , pp. 3750-3755
    • Suzuki, N.1    Okai, N.2    Nonaka, H.3
  • 87
    • 17844381074 scopus 로고    scopus 로고
    • Cre/loxP-mediated deletion system for large genome rearrangements in Corynebacterium glutamicum
    • N.Suzuki, Y.Tsuge, M.Inui, H.Yukawa. (2005c). Cre/loxP-mediated deletion system for large genome rearrangements in Corynebacterium glutamicum. Appl Microbiol Biotechnol, 67, 225–33
    • (2005) Appl Microbiol Biotechnol , vol.67 , pp. 225-233
    • Suzuki, N.1    Tsuge, Y.2    Inui, M.3    Yukawa, H.4
  • 88
    • 60549108164 scopus 로고    scopus 로고
    • Identification of new secreted proteins and secretion of heterologous amylase by C. glutamicum
    • N.Suzuki, K.Watanabe, N.Okibe,. (2009). Identification of new secreted proteins and secretion of heterologous amylase by C. glutamicum. Appl Microbiol Biotechnol, 82, 491–500
    • (2009) Appl Microbiol Biotechnol , vol.82 , pp. 491-500
    • Suzuki, N.1    Watanabe, K.2    Okibe, N.3
  • 89
    • 36248965184 scopus 로고    scopus 로고
    • Direct production of L-lysine from raw corn starch by Corynebacterium glutamicum secreting Streptococcus bovis alpha-amylase using cspB promoter and signal sequence
    • T.Tateno, H.Fukuda, A.Kondo. (2007). Direct production of L-lysine from raw corn starch by Corynebacterium glutamicum secreting Streptococcus bovis alpha-amylase using cspB promoter and signal sequence. Appl Microbiol Biotechnol, 77, 533–41
    • (2007) Appl Microbiol Biotechnol , vol.77 , pp. 533-541
    • Tateno, T.1    Fukuda, H.2    Kondo, A.3
  • 90
    • 58549095930 scopus 로고    scopus 로고
    • Direct production of cadaverine from soluble starch using Corynebacterium glutamicum coexpressing alpha-amylase and lysine decarboxylase
    • T.Tateno, Y.Okada, T.Tsuchidate,. (2009). Direct production of cadaverine from soluble starch using Corynebacterium glutamicum coexpressing alpha-amylase and lysine decarboxylase. Appl Microbiol Biotechnol, 82, 115–21
    • (2009) Appl Microbiol Biotechnol , vol.82 , pp. 115-121
    • Tateno, T.1    Okada, Y.2    Tsuchidate, T.3
  • 91
    • 0042932755 scopus 로고    scopus 로고
    • Plasmids in Corynebacterium glutamicum and their molecular classification by comparative genomics
    • A.Tauch, A.Pühler, J.Kalinowski, G.Thierbach. (2003). Plasmids in Corynebacterium glutamicum and their molecular classification by comparative genomics. J Biotechnol, 104, 27–40
    • (2003) J Biotechnol , vol.104 , pp. 27-40
    • Tauch, A.1    Pühler, A.2    Kalinowski, J.3    Thierbach, G.4
  • 92
    • 79960739073 scopus 로고    scopus 로고
    • High yield secretion of heterologous proteins in Corynebacterium glutamicum using its own Tat-type signal sequence
    • H.Teramoto, K.Watanabe, N.Suzuki,. (2011). High yield secretion of heterologous proteins in Corynebacterium glutamicum using its own Tat-type signal sequence. Appl Microbiol Biotechnol, 91, 677–87
    • (2011) Appl Microbiol Biotechnol , vol.91 , pp. 677-687
    • Teramoto, H.1    Watanabe, K.2    Suzuki, N.3
  • 93
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome
    • H.Tjalsma, A.Bolhuis, J.D.Jongbloed,. (2000). Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome. Microbiol Mol Biol Rev, 64, 515–47
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 515-547
    • Tjalsma, H.1    Bolhuis, A.2    Jongbloed, J.D.3
  • 94
    • 33846374339 scopus 로고    scopus 로고
    • Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa
    • S.R.Trevino, J.M.Scholtz, C.N.Pace. (2007). Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa. J Mol Biol, 366, 449–60
    • (2007) J Mol Biol , vol.366 , pp. 449-460
    • Trevino, S.R.1    Scholtz, J.M.2    Pace, C.N.3
  • 95
    • 79954622477 scopus 로고    scopus 로고
    • Glutamate production from beta-glucan using endoglucanase-secreting Corynebacterium glutamicum
    • T.Tsuchidate, T.Tateno, N.Okai,. (2011). Glutamate production from beta-glucan using endoglucanase-secreting Corynebacterium glutamicum. Appl Microbiol Biotechnol, 90, 895–901
    • (2011) Appl Microbiol Biotechnol , vol.90 , pp. 895-901
    • Tsuchidate, T.1    Tateno, T.2    Okai, N.3
  • 96
    • 0023894602 scopus 로고
    • Genetic control systems of Escherichia coli can confer inducible expression of cloned genes in coryneform bacteria
    • M.Tsuchiya, Y.Morinaga. (1988). Genetic control systems of Escherichia coli can confer inducible expression of cloned genes in coryneform bacteria. Nat Biotechnol, 6, 428–30
    • (1988) Nat Biotechnol , vol.6 , pp. 428-430
    • Tsuchiya, M.1    Morinaga, Y.2
  • 97
    • 34247630142 scopus 로고    scopus 로고
    • Random segment deletion based on IS31831 and Cre/loxP excision system in Corynebacterium glutamicum
    • Y.Tsuge, N.Suzuki, M.Inui, H.Yukawa. (2007). Random segment deletion based on IS31831 and Cre/loxP excision system in Corynebacterium glutamicum. Appl Microbiol Biotechnol, 74, 1333–41
    • (2007) Appl Microbiol Biotechnol , vol.74 , pp. 1333-1341
    • Tsuge, Y.1    Suzuki, N.2    Inui, M.3    Yukawa, H.4
  • 98
    • 27244446613 scopus 로고    scopus 로고
    • Type I signal peptidase: an overview
    • R.Tuteja. (2005). Type I signal peptidase: an overview. Arch Biochem Biophys, 441, 107–11
    • (2005) Arch Biochem Biophys , vol.441 , pp. 107-111
    • Tuteja, R.1
  • 99
    • 84862689750 scopus 로고    scopus 로고
    • Improved L-lysine production with Corynebacterium glutamicum and systemic insight into citrate synthase flux and activity
    • J.van Ooyen, S.Noack, M.Bott,. (2012). Improved L-lysine production with Corynebacterium glutamicum and systemic insight into citrate synthase flux and activity. Biotechnol Bioeng, 109, 2070–81
    • (2012) Biotechnol Bioeng , vol.109 , pp. 2070-2081
    • van Ooyen, J.1    Noack, S.2    Bott, M.3
  • 100
    • 0345286863 scopus 로고    scopus 로고
    • Analysis of the Corynebacterium glutamicum dapA promoter
    • P.Vasicová, M.Pátek, J.Nešvera,. (1999). Analysis of the Corynebacterium glutamicum dapA promoter. J Bacteriol, 181, 6188–91
    • (1999) J Bacteriol , vol.181 , pp. 6188-6191
    • Vasicová, P.1    Pátek, M.2    Nešvera, J.3
  • 101
    • 84876985466 scopus 로고    scopus 로고
    • Protein secretion systems of Corynebacterium glutamicum
    • Yukawa H., Inui M., (eds), Heidelberg: Springer
    • A.A.Vertes. (2012). Protein secretion systems of Corynebacterium glutamicum, In: H.Yukawa, M.Inui, eds. Corynebacterium glutamicum: biology and biotechnology. Heidelberg: Springer, 351–89
    • (2012) Corynebacterium glutamicum: biology and biotechnology , pp. 351-389
    • Vertes, A.A.1
  • 102
    • 77951076300 scopus 로고    scopus 로고
    • Production of recombinant cholesterol oxidase containing covalently bound FAD in Escherichia coli
    • F.Volontè, L.Pollegioni, G.Molla,. (2010). Production of recombinant cholesterol oxidase containing covalently bound FAD in Escherichia coli. BMC Biotechnol, 10, 33
    • (2010) BMC Biotechnol , vol.10 , pp. 33
    • Volontè, F.1    Pollegioni, L.2    Molla, G.3
  • 103
    • 77956690413 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks 2010
    • G.Walsh. (2010). Biopharmaceutical benchmarks 2010. Nat Biotechnol, 28, 917–24
    • (2010) Nat Biotechnol , vol.28 , pp. 917-924
    • Walsh, G.1
  • 104
    • 84869106902 scopus 로고    scopus 로고
    • New biopharmaceuticals
    • G.Walsh. (2012). New biopharmaceuticals. Biopharm Int, 25, 34–6
    • (2012) Biopharm Int , vol.25 , pp. 34-36
    • Walsh, G.1
  • 105
    • 84888089154 scopus 로고    scopus 로고
    • Milestones and moderate progress in 2012 drug approvals
    • G.Walsh. (2013). Milestones and moderate progress in 2012 drug approvals. Biopharm Int, 26, 54–6
    • (2013) Biopharm Int , vol.26 , pp. 54-56
    • Walsh, G.1
  • 106
    • 84878011326 scopus 로고    scopus 로고
    • Influence of SigB inactivation on Corynebacterium glutamicum protein secretion
    • K.Watanabe, H.Teramoto, N.Suzuki,. (2013). Influence of SigB inactivation on Corynebacterium glutamicum protein secretion. Appl Microbiol Biotechnol, 97, 4917–26
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 4917-4926
    • Watanabe, K.1    Teramoto, H.2    Suzuki, N.3
  • 107
    • 64049102180 scopus 로고    scopus 로고
    • Scanning the Corynebacterium glutamicum R genome for high-efficiency secretion signal sequences
    • K.Watanabe, Y.Tsuchida, N.Okibe,. (2009). Scanning the Corynebacterium glutamicum R genome for high-efficiency secretion signal sequences. Microbiology, 155, 741–50
    • (2009) Microbiology , vol.155 , pp. 741-750
    • Watanabe, K.1    Tsuchida, Y.2    Okibe, N.3
  • 108
    • 33745143219 scopus 로고    scopus 로고
    • Emerging Corynebacterium glutamicum systems biology
    • V.F.Wendisch, M.Bott, J.Kalinowski,. (2006). Emerging Corynebacterium glutamicum systems biology. J Biotechnol, 123, 74–92
    • (2006) J Biotechnol , vol.123 , pp. 74-92
    • Wendisch, V.F.1    Bott, M.2    Kalinowski, J.3
  • 109
    • 77954143208 scopus 로고    scopus 로고
    • An improved shuttle vector constructed for metabolic engineering research in Corynebacterium glutamicum
    • D.Xu, Y.Tan, F.Shi, X.Wang. (2010). An improved shuttle vector constructed for metabolic engineering research in Corynebacterium glutamicum. Plasmid, 64, 85–91
    • (2010) Plasmid , vol.64 , pp. 85-91
    • Xu, D.1    Tan, Y.2    Shi, F.3    Wang, X.4
  • 110
    • 36348944035 scopus 로고    scopus 로고
    • Analyses of the acetate producing pathways in Corynebacterium glutamicum under oxygen-deprived conditions
    • K.Yasuda, T.Jojima, M.Suda,. (2007). Analyses of the acetate producing pathways in Corynebacterium glutamicum under oxygen-deprived conditions. Appl Microbiol Biotechnol, 77, 853–60
    • (2007) Appl Microbiol Biotechnol , vol.77 , pp. 853-860
    • Yasuda, K.1    Jojima, T.2    Suda, M.3
  • 111
    • 0036276602 scopus 로고    scopus 로고
    • Sequence and phylogenetic analyses of the twin-arginine targeting (Tat) protein export system
    • M.R.Yen, Y.H.Tseng, E.H.Nguyen,. (2002). Sequence and phylogenetic analyses of the twin-arginine targeting (Tat) protein export system. Arch Microbiol, 177, 441–50
    • (2002) Arch Microbiol , vol.177 , pp. 441-450
    • Yen, M.R.1    Tseng, Y.H.2    Nguyen, E.H.3
  • 112
    • 84891853096 scopus 로고    scopus 로고
    • High-level secretory production of recombinant single-chain variable fragment (scFv) in Corynebacterium glutamicum
    • S.S.Yim, S.J.An, J.W.Choi,. (2014). High-level secretory production of recombinant single-chain variable fragment (scFv) in Corynebacterium glutamicum. Appl Microbiol Biotechnol, 98, 273–84
    • (2014) Appl Microbiol Biotechnol , vol.98 , pp. 273-284
    • Yim, S.S.1    An, S.J.2    Choi, J.W.3
  • 113
    • 84884532775 scopus 로고    scopus 로고
    • Isolation of fully synthetic promoters for high-level gene expression in Corynebacterium glutamicum
    • S.S.Yim, S.J.An, M.Kang,. (2013). Isolation of fully synthetic promoters for high-level gene expression in Corynebacterium glutamicum. Biotechnol Bioeng, 110, 2959–69
    • (2013) Biotechnol Bioeng , vol.110 , pp. 2959-2969
    • Yim, S.S.1    An, S.J.2    Kang, M.3
  • 115
    • 84866170092 scopus 로고    scopus 로고
    • Development and application of an arabinose-inducible expression system by facilitating inducer uptake in Corynebacterium glutamicum
    • Y.Zhang, X.Shang, S.Lai,. (2012). Development and application of an arabinose-inducible expression system by facilitating inducer uptake in Corynebacterium glutamicum. Appl Environ Microbiol, 78, 5831–8
    • (2012) Appl Environ Microbiol , vol.78 , pp. 5831-5838
    • Zhang, Y.1    Shang, X.2    Lai, S.3
  • 116
    • 84862541940 scopus 로고    scopus 로고
    • Mammalian cell protein expression for biopharmaceutical production
    • J.Zhu. (2012). Mammalian cell protein expression for biopharmaceutical production. Biotechnol Adv, 30, 1158–70
    • (2012) Biotechnol Adv , vol.30 , pp. 1158-1170
    • Zhu, J.1


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