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Volumn 102, Issue 1, 2009, Pages 176-187

Microbial bio-production of a recombinant stimuli-responsive biosurfactant

Author keywords

Bio production; Biosurfactant; E. Coli; Maltose binding protein; Peptide; Precipitation; TEVp

Indexed keywords

BIO-PRODUCTION; BIOSURFACTANT; E. COLI; MALTOSE BINDING PROTEIN; PEPTIDE; PRECIPITATION; TEVP;

EID: 58149265697     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.22037     Document Type: Article
Times cited : (16)

References (50)
  • 2
    • 0034078278 scopus 로고    scopus 로고
    • Potential commercial applications of microbial surfactants
    • Banat IM, Makkar RS, Cameotra SS. 2000. Potential commercial applications of microbial surfactants. Appl Microbiol Biotechnol 53(5):495- 508.
    • (2000) Appl Microbiol Biotechnol , vol.53 , Issue.5 , pp. 495-508
    • Banat, I.M.1    Makkar, R.S.2    Cameotra, S.S.3
  • 3
    • 0020541133 scopus 로고
    • Purification and amino acid sequence of a noncalcitonin secretory peptide derived from prepro- calcitonin
    • Birnbaum RS, Mahoney W, Roos BA. 1983. Purification and amino acid sequence of a noncalcitonin secretory peptide derived from prepro- calcitonin. J Biol Chem 258(9):5463-5466.
    • (1983) J Biol Chem , vol.258 , Issue.9 , pp. 5463-5466
    • Birnbaum, R.S.1    Mahoney, W.2    Roos, B.A.3
  • 5
    • 2942560687 scopus 로고    scopus 로고
    • Recent applications of biosurfactants as biological and immunological molecules
    • Cameotra SS, Makkar RS. 2004. Recent applications of biosurfactants as biological and immunological molecules. Curr Opin Microbiol 7(3):262-266.
    • (2004) Curr Opin Microbiol , vol.7 , Issue.3 , pp. 262-266
    • Cameotra, S.S.1    Makkar, R.S.2
  • 6
    • 0036091817 scopus 로고    scopus 로고
    • Amino acid-based surfactants: Enzymatic synthesis, properties and potential applications
    • Clapes P, Infante MR. 2002. Amino acid-based surfactants: Enzymatic synthesis, properties and potential applications. Biocatal Biotransfor 20(4):215-233.
    • (2002) Biocatal Biotransfor , vol.20 , Issue.4 , pp. 215-233
    • Clapes, P.1    Infante, M.R.2
  • 7
    • 0027729733 scopus 로고
    • The development of stable protein formulations: A close look at protein aggregation, deamidation, and oxidation
    • Cleland JL, Powell MF, Shire SJ. 1993. The development of stable protein formulations: A close look at protein aggregation, deamidation, and oxidation. Crit Rev Ther Drug 10(4):307-377.
    • (1993) Crit Rev Ther Drug , vol.10 , Issue.4 , pp. 307-377
    • Cleland, J.L.1    Powell, M.F.2    Shire, S.J.3
  • 9
    • 34547531123 scopus 로고    scopus 로고
    • Switchable peptide surfactants with designed metal binding capacity
    • Dexter AF, Middelberg APJ. 2007. Switchable peptide surfactants with designed metal binding capacity. J Phys Chem C 111(28):10484-10492.
    • (2007) J Phys Chem C , vol.111 , Issue.28 , pp. 10484-10492
    • Dexter, A.F.1    Middelberg, A.P.J.2
  • 10
    • 33744780455 scopus 로고    scopus 로고
    • Reversible active switching of the mechanical properties of a peptide film at a fluid-fluid interface
    • Dexter AF, Malcolm AS, Middelberg APJ. 2006. Reversible active switching of the mechanical properties of a peptide film at a fluid-fluid interface. Nat Mater 5(6):502-506.
    • (2006) Nat Mater , vol.5 , Issue.6 , pp. 502-506
    • Dexter, A.F.1    Malcolm, A.S.2    Middelberg, A.P.J.3
  • 11
    • 34248202284 scopus 로고    scopus 로고
    • Diao H, Guo C, Lin D, Zhang Y. 2007. Intein- mediated expression is an effective approach in the study of (β-defensins. Biochem Biophys Res Commun 357(4):840-846.
    • Diao H, Guo C, Lin D, Zhang Y. 2007. Intein- mediated expression is an effective approach in the study of (β-defensins. Biochem Biophys Res Commun 357(4):840-846.
  • 12
    • 0024730021 scopus 로고
    • Characterization of the catalytic residues of the tobacco etch virus 49-kDa proteinase
    • Dougherty WG, Parks TD, Cary SM, Bazan JF, Fletterick RJ. 1989. Characterization of the catalytic residues of the tobacco etch virus 49-kDa proteinase. Virology 172(1):302-310.
    • (1989) Virology , vol.172 , Issue.1 , pp. 302-310
    • Dougherty, W.G.1    Parks, T.D.2    Cary, S.M.3    Bazan, J.F.4    Fletterick, R.J.5
  • 14
    • 0028085989 scopus 로고
    • A novel approach for high level production of a recombinant human parathyroid hormone fragment in Escherichia coli
    • Gram H, Ramage P, Memmert K, Gamse R, Kocher HP. 1994. A novel approach for high level production of a recombinant human parathyroid hormone fragment in Escherichia coli. Nat Biotechnol 12(10): 1017-1023.
    • (1994) Nat Biotechnol , vol.12 , Issue.10 , pp. 1017-1023
    • Gram, H.1    Ramage, P.2    Memmert, K.3    Gamse, R.4    Kocher, H.P.5
  • 15
    • 0031085258 scopus 로고    scopus 로고
    • Lipopeptides with improved properties: Structure by NMR, purification by HPLC and structure-activity relationships of new isoleucyl-rich surfactins
    • Grangemard I, Peypoux F, Wallach J, Das BC, Labbe H, Caille A, Genest M, Maget-Dana R, Ptak M, Bonmatin JM. 1997. Lipopeptides with improved properties: Structure by NMR, purification by HPLC and structure-activity relationships of new isoleucyl-rich surfactins. J Pept Sci 3(2):145-154.
    • (1997) J Pept Sci , vol.3 , Issue.2 , pp. 145-154
    • Grangemard, I.1    Peypoux, F.2    Wallach, J.3    Das, B.C.4    Labbe, H.5    Caille, A.6    Genest, M.7    Maget-Dana, R.8    Ptak, M.9    Bonmatin, J.M.10
  • 16
    • 33947379507 scopus 로고    scopus 로고
    • Structural characterization of daptomycin analogues A21978C 1-3 (D-Asn11) produced by a recombinant Streptomyces roseosporus strain
    • Gu JQ, Nguyen KT, Gandhi C, Rajgarhia V, Baltz RH, Brian P, Chu M. 2007. Structural characterization of daptomycin analogues A21978C 1-3 (D-Asn11) produced by a recombinant Streptomyces roseosporus strain. J Nat Prod 70(2):233-240.
    • (2007) J Nat Prod , vol.70 , Issue.2 , pp. 233-240
    • Gu, J.Q.1    Nguyen, K.T.2    Gandhi, C.3    Rajgarhia, V.4    Baltz, R.H.5    Brian, P.6    Chu, M.7
  • 18
    • 34247868094 scopus 로고    scopus 로고
    • Recombinant production of antimicrobial peptides in heterologous microbial systems
    • Ingham AB, Moore RJ. 2007. Recombinant production of antimicrobial peptides in heterologous microbial systems. Biotechnol Appl Biochem 47(1):1-9.
    • (2007) Biotechnol Appl Biochem , vol.47 , Issue.1 , pp. 1-9
    • Ingham, A.B.1    Moore, R.J.2
  • 19
    • 0017697097 scopus 로고
    • Expression in Escherichia coli of a chemically synthesized gene for the hormone somatostatin
    • Itakura K, Hirose T, Crea R. 1977. Expression in Escherichia coli of a chemically synthesized gene for the hormone somatostatin. Science 198(4321):1056-1063.
    • (1977) Science , vol.198 , Issue.4321 , pp. 1056-1063
    • Itakura, K.1    Hirose, T.2    Crea, R.3
  • 20
    • 0037118274 scopus 로고    scopus 로고
    • Direct determination of the mechanical properties of an interfacially adsorbed protein film
    • Jones DB, Middelberg APJ. 2002. Direct determination of the mechanical properties of an interfacially adsorbed protein film. Chem Eng Sci 57(10):1711-1722.
    • (2002) Chem Eng Sci , vol.57 , Issue.10 , pp. 1711-1722
    • Jones, D.B.1    Middelberg, A.P.J.2
  • 21
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • Kapust RB, Waugh DS. 1999. Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci 8(8):1668-1674.
    • (1999) Protein Sci , vol.8 , Issue.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 22
    • 0035711194 scopus 로고    scopus 로고
    • Tobacco etch virus protease: Mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency
    • Kapust RB, Toezser J, Fox JD, Anderson DE, Cherry S, Copeland TD, Waugh DS. 2001. Tobacco etch virus protease: Mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency. Prot Eng 14(12):993-1000.
    • (2001) Prot Eng , vol.14 , Issue.12 , pp. 993-1000
    • Kapust, R.B.1    Toezser, J.2    Fox, J.D.3    Anderson, D.E.4    Cherry, S.5    Copeland, T.D.6    Waugh, D.S.7
  • 24
    • 33645890565 scopus 로고    scopus 로고
    • Cloning and production of a novel Bacteriocin, Lactococcin K, from Lactococcus lactis Subsp. lactis MY23
    • Kim Y, Kim M, Kim P, Kim J. 2006. Cloning and production of a novel Bacteriocin, Lactococcin K, from Lactococcus lactis Subsp. lactis MY23. Biotechnol Lett 28(5):357-362.
    • (2006) Biotechnol Lett , vol.28 , Issue.5 , pp. 357-362
    • Kim, Y.1    Kim, M.2    Kim, P.3    Kim, J.4
  • 25
    • 0028017482 scopus 로고
    • Production, purification, and cleavage of tandem repeats of recombinant peptides
    • Kuliopulos A, Walsh CT. 1994. Production, purification, and cleavage of tandem repeats of recombinant peptides. J Am Chem Soc 116(11): 4599-4607.
    • (1994) J Am Chem Soc , vol.116 , Issue.11 , pp. 4599-4607
    • Kuliopulos, A.1    Walsh, C.T.2
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of Bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of Bacteriophage T4. Nature 227(5259):680-685.
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 23444452903 scopus 로고    scopus 로고
    • Recombinant biocatalytic and cell-free synthesis of HIV fusion inhibitor
    • Lee EJ, Kim HS, Lee EY. 2005. Recombinant biocatalytic and cell-free synthesis of HIV fusion inhibitor. J Ind Eng Chem 11(4):515-521.
    • (2005) J Ind Eng Chem , vol.11 , Issue.4 , pp. 515-521
    • Lee, E.J.1    Kim, H.S.2    Lee, E.Y.3
  • 28
    • 0023589183 scopus 로고
    • High-level expression of α-human atrial natriuretic peptide from multiple joined genes in Escherichia coli
    • Lennick M, Haynes JR, Shen S-H. 1987. High-level expression of α-human atrial natriuretic peptide from multiple joined genes in Escherichia coli. Gene 61(1):103-112.
    • (1987) Gene , vol.61 , Issue.1 , pp. 103-112
    • Lennick, M.1    Haynes, J.R.2    Shen, S.-H.3
  • 29
    • 34447310561 scopus 로고    scopus 로고
    • High-level expression of milk-derived antihypertensive peptide in Escherichia coli and its bioactivity
    • Liu D, Sun H, Zhang L, Li S. 2007. High-level expression of milk-derived antihypertensive peptide in Escherichia coli and its bioactivity. J Agric Food Chem 55(13):5109-5112.
    • (2007) J Agric Food Chem , vol.55 , Issue.13 , pp. 5109-5112
    • Liu, D.1    Sun, H.2    Zhang, L.3    Li, S.4
  • 30
    • 33750983005 scopus 로고    scopus 로고
    • Foaming properties of a peptide designed to form stimuli-responsive interfacial films
    • Malcolm AS, Dexter AF, Middelberg APJ. 2006. Foaming properties of a peptide designed to form stimuli-responsive interfacial films. Soft Matter 2(12):1057-1066.
    • (2006) Soft Matter , vol.2 , Issue.12 , pp. 1057-1066
    • Malcolm, A.S.1    Dexter, A.F.2    Middelberg, A.P.J.3
  • 31
    • 36348987628 scopus 로고    scopus 로고
    • The interfacial structure and Young's modulus of peptide films having switchable mechanical properties
    • Middelberg APJ, He L, Dexter AF, Shen HH, Holt SA, Thomas RK. 2008. The interfacial structure and Young's modulus of peptide films having switchable mechanical properties. J Roy Soc Interf 5(18):47-54.
    • (2008) J Roy Soc Interf , vol.5 , Issue.18 , pp. 47-54
    • Middelberg, A.P.J.1    He, L.2    Dexter, A.F.3    Shen, H.H.4    Holt, S.A.5    Thomas, R.K.6
  • 32
    • 33646787464 scopus 로고    scopus 로고
    • Recombinant expression of indolicidin concatamers in Escherichia coli
    • Morin K, Arcidiacono S, Beckwitt R, Mello C. 2006. Recombinant expression of indolicidin concatamers in Escherichia coli. Appl Microbiol Biotechnol 70(6):698-704.
    • (2006) Appl Microbiol Biotechnol , vol.70 , Issue.6 , pp. 698-704
    • Morin, K.1    Arcidiacono, S.2    Beckwitt, R.3    Mello, C.4
  • 33
    • 4644240798 scopus 로고    scopus 로고
    • Bioprocess-centered molecular design (BMD) for the efficient production of an interfacially active peptide
    • Morreale G, Lee EG, Jones DB, Middelberg APJ. 2004. Bioprocess-centered molecular design (BMD) for the efficient production of an interfacially active peptide. Biotechnol Bioeng 87(7):912-923.
    • (2004) Biotechnol Bioeng , vol.87 , Issue.7 , pp. 912-923
    • Morreale, G.1    Lee, E.G.2    Jones, D.B.3    Middelberg, A.P.J.4
  • 34
    • 0030798111 scopus 로고    scopus 로고
    • Isolation of new variants of surfactin by a recombinant Bacillus subtilis
    • Nakayama S, Takahashi S, Hirai M, Shoda M. 1997. Isolation of new variants of surfactin by a recombinant Bacillus subtilis. Appl Microbiol Biotechnol 48(1):80-82.
    • (1997) Appl Microbiol Biotechnol , vol.48 , Issue.1 , pp. 80-82
    • Nakayama, S.1    Takahashi, S.2    Hirai, M.3    Shoda, M.4
  • 35
    • 5344232818 scopus 로고    scopus 로고
    • Efficient site-specific processing of fusion proteins by tobacco vein mottling virus protease in vivo and in vitro
    • Nallamsetty S, Kapust RB, Tözséer J, Cherry S, Tropea JE, Copeland TD, Waugh DS. 2004. Efficient site-specific processing of fusion proteins by tobacco vein mottling virus protease in vivo and in vitro. Prot Expr Purif 38(1):108-115.
    • (2004) Prot Expr Purif , vol.38 , Issue.1 , pp. 108-115
    • Nallamsetty, S.1    Kapust, R.B.2    Tözséer, J.3    Cherry, S.4    Tropea, J.E.5    Copeland, T.D.6    Waugh, D.S.7
  • 36
    • 0029329111 scopus 로고
    • Production of a lipopeptide antibiotic, surfactin, by recombinant Bacillus subtilis in solid state fermentation
    • Ohno A, Ano T, Shoda M. 1995. Production of a lipopeptide antibiotic, surfactin, by recombinant Bacillus subtilis in solid state fermentation. Biotechnol Bioeng 47(2):209-214.
    • (1995) Biotechnol Bioeng , vol.47 , Issue.2 , pp. 209-214
    • Ohno, A.1    Ano, T.2    Shoda, M.3
  • 40
    • 33845196016 scopus 로고    scopus 로고
    • Biosurfactants: An overview
    • Sekhon BS. 2006. Biosurfactants: An overview. Natl Acad Sci Lett 29(9-10): 317-332.
    • (2006) Natl Acad Sci Lett , vol.29 , Issue.9-10 , pp. 317-332
    • Sekhon, B.S.1
  • 41
    • 0345665954 scopus 로고
    • Multiple joined genes prevent product degradation in Escherichia coli
    • Shen S-H. 1984. Multiple joined genes prevent product degradation in Escherichia coli. Proc Natl Acad Sci USA 81:4627-4631.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 4627-4631
    • Shen, S.-H.1
  • 42
    • 1242270554 scopus 로고    scopus 로고
    • Potential applications of microbial surfactants in biomedical sciences
    • Singh P, Cameotra SS. 2004. Potential applications of microbial surfactants in biomedical sciences. Trends Biotechnol 22(3):142-146.
    • (2004) Trends Biotechnol , vol.22 , Issue.3 , pp. 142-146
    • Singh, P.1    Cameotra, S.S.2
  • 43
    • 33845928039 scopus 로고    scopus 로고
    • Surfactants in microbiology and biotechnology. Part 2. Application aspects
    • Singh A, Van Hamme JD, Ward OP. 2007. Surfactants in microbiology and biotechnology. Part 2. Application aspects. Biotechnol Adv 25(1):99-121.
    • (2007) Biotechnol Adv , vol.25 , Issue.1 , pp. 99-121
    • Singh, A.1    Van Hamme, J.D.2    Ward, O.P.3
  • 44
    • 0034665455 scopus 로고    scopus 로고
    • Design of high-throughput methods ofprotein production for structural biology
    • Stevens RC. 2000. Design of high-throughput methods ofprotein production for structural biology. Structure 8(9):R177-R185.
    • (2000) Structure , vol.8 , Issue.9
    • Stevens, R.C.1
  • 45
    • 33749327044 scopus 로고    scopus 로고
    • Physiological aspects. Part 1 in a series of papers devoted to surfactants in microbiology and biotechnology
    • Van Hamme JD, Singh A, Ward OP. 2006. Physiological aspects. Part 1 in a series of papers devoted to surfactants in microbiology and biotechnology. Biotechnol Adv 24(6):604-620.
    • (2006) Biotechnol Adv , vol.24 , Issue.6 , pp. 604-620
    • Van Hamme, J.D.1    Singh, A.2    Ward, O.P.3
  • 47
    • 33747735624 scopus 로고    scopus 로고
    • High-level production of bioactive human beta-defensin-4 in Escherichia coli by soluble fusion expression
    • Xu Z, Zhong Z, Huang L, Peng L, Wang F, Cen P. 2006. High-level production of bioactive human beta-defensin-4 in Escherichia coli by soluble fusion expression. Appl Microbiol Biotechnol 72(3):471- 479.
    • (2006) Appl Microbiol Biotechnol , vol.72 , Issue.3 , pp. 471-479
    • Xu, Z.1    Zhong, Z.2    Huang, L.3    Peng, L.4    Wang, F.5    Cen, P.6
  • 48
    • 33947369797 scopus 로고    scopus 로고
    • Expression and purification of a recombinant antibacterial peptide, cecropin, from Escherichia coli
    • Xu X, Jin F, Yu X, Ji S, Wang J, Cheng H, Wang C, Zhang W. 2007. Expression and purification of a recombinant antibacterial peptide, cecropin, from Escherichia coli. Prot Expr Purif 53(2):293-301.
    • (2007) Prot Expr Purif , vol.53 , Issue.2 , pp. 293-301
    • Xu, X.1    Jin, F.2    Yu, X.3    Ji, S.4    Wang, J.5    Cheng, H.6    Wang, C.7    Zhang, W.8
  • 49
    • 33846464611 scopus 로고    scopus 로고
    • Functional expression of a Drosophila antifungal peptide in Escherichia coli
    • Yuan Y, Gao B, Zhu S. 2007. Functional expression of a Drosophila antifungal peptide in Escherichia coli. Prot Expr Purif 52(2):457- 462.
    • (2007) Prot Expr Purif , vol.52 , Issue.2 , pp. 457-462
    • Yuan, Y.1    Gao, B.2    Zhu, S.3
  • 50
    • 34248395017 scopus 로고    scopus 로고
    • High-level production of a novel antimicrobial peptide perinerin in Escherichia coli by fusion expression
    • Zhou Q-F, Luo X-G, Ye L, Xi T. 2007. High-level production of a novel antimicrobial peptide perinerin in Escherichia coli by fusion expression. Curr Microbiol 54(5):366-370.
    • (2007) Curr Microbiol , vol.54 , Issue.5 , pp. 366-370
    • Zhou, Q.-F.1    Luo, X.-G.2    Ye, L.3    Xi, T.4


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