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Volumn 80, Issue 10, 2014, Pages 3062-3071

In vivo self-assembly of stable green fluorescent protein fusion particles and their uses in enzyme immobilization

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASES; BACTERIOLOGY; BIOCONVERSION; BIOREMEDIATION; ESCHERICHIA COLI; FLUORESCENCE; PROTEINS; RECYCLING; SELF ASSEMBLY;

EID: 84899078839     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00323-14     Document Type: Article
Times cited : (17)

References (37)
  • 1
    • 79251494754 scopus 로고    scopus 로고
    • Enzymes and bioconversions of industrial pharmaceutical, and biotechnological significance
    • Sanchez S, Demain AL. 2011. Enzymes and bioconversions of industrial, pharmaceutical, and biotechnological significance. Org. Process Res. Dev. 15:224-230. http://dx.doi.org/10.1021/op100302x.
    • (2011) Org. Process Res. Dev. , vol.15 , pp. 224-230
    • Sanchez, S.1    Demain, A.L.2
  • 3
    • 70350257632 scopus 로고    scopus 로고
    • Advances in enzyme immobilisation
    • Brady D, Jordaan J. 2009. Advances in enzyme immobilisation. Biotechnol. Lett. 31:1639-1650. http://dx.doi.org/10.1007/s10529-009-0076-4.
    • (2009) Biotechnol. Lett. , vol.31 , pp. 1639-1650
    • Brady, D.1    Jordaan, J.2
  • 4
    • 34547209337 scopus 로고    scopus 로고
    • Enzyme immobilization: the quest for optimum performance
    • Sheldon RA. 2007. Enzyme immobilization: the quest for optimum performance. Adv. Synth. Catal. 349:1289-1307. http://dx.doi.org/10.1002/adsc.200700082.
    • (2007) Adv. Synth. Catal. , vol.349 , pp. 1289-1307
    • Sheldon, R.A.1
  • 5
    • 62449121836 scopus 로고    scopus 로고
    • Understanding enzyme immobilisation
    • Hanefeld U, Gardossi L, Magner E. 2009. Understanding enzyme immobilisation. Chem. Soc. Rev. 38:453-468. http://dx.doi.org/10.1039/b711564b.
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 453-468
    • Hanefeld, U.1    Gardossi, L.2    Magner, E.3
  • 7
    • 28244452921 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates (CLEAs): a novel and versatile method for enzyme immobilization (a review)
    • Sheldon RA, Schoevaart R, Van Langen LM. 2005. Cross-linked enzyme aggregates (CLEAs): a novel and versatile method for enzyme immobilization (a review). Biocatal. Biotransformation 23:141-147. http://dx.doi.org/10.1080/10242420500183378.
    • (2005) Biocatal. Biotransformation , vol.23 , pp. 141-147
    • Sheldon, R.A.1    Schoevaart, R.2    Van Langen, L.M.3
  • 8
    • 0000916487 scopus 로고
    • Cross-linked enzyme crystals as robust biocatalysts
    • St. Clair NL, Navia MA. 1992. Cross-linked enzyme crystals as robust biocatalysts. J. Am. Chem. Soc. 114:7314-7316. http://dx.doi.org/10.1021/ja00044a064.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 7314-7316
    • Clair, S.N.L.1    Navia, M.A.2
  • 9
    • 57549115038 scopus 로고    scopus 로고
    • Enzymatically active fibrils generated by the self-assembly of the ApoA-I fibrillogenic domain functionalized with a catalytic moiety
    • Guglielmi F, Monti DM, Arciello A, Torrassa S, Cozzolino F, Pucci P, Relini A, Piccoli R. 2009. Enzymatically active fibrils generated by the self-assembly of the ApoA-I fibrillogenic domain functionalized with a catalytic moiety. Biomaterials 30:829-835. http://dx.doi.org/10.1016/j.biomaterials.2008.10.036.
    • (2009) Biomaterials , vol.30 , pp. 829-835
    • Guglielmi, F.1    Monti, D.M.2    Arciello, A.3    Torrassa, S.4    Cozzolino, F.5    Pucci, P.6    Relini, A.7    Piccoli, R.8
  • 10
    • 84858448799 scopus 로고    scopus 로고
    • Immobilization of organophosphohydrolase OpdA from Agrobacterium radiobacter by overproduction at the surface of polyester inclusions inside engineered Escherichia coli
    • Blatchford PA, Scott C, French N, Rehm BH. 2012. Immobilization of organophosphohydrolase OpdA from Agrobacterium radiobacter by overproduction at the surface of polyester inclusions inside engineered Escherichia coli. Biotechnol. Bioeng. 109:1101-1108. http://dx.doi.org/10.1002/bit.24402.
    • (2012) Biotechnol. Bioeng. , vol.109 , pp. 1101-1108
    • Blatchford, P.A.1    Scott, C.2    French, N.3    Rehm, B.H.4
  • 11
    • 84876322623 scopus 로고    scopus 로고
    • Bioengineering of bacterial polymer inclusions catalyzing the synthesis of N-acetyl neuraminic acid
    • Hooks DO, Blatchford PA, Rehm BHA. 2013. Bioengineering of bacterial polymer inclusions catalyzing the synthesis of N-acetyl neuraminic acid. Appl. Environ. Microbiol. 79:3116-3121. http://dx.doi.org/10.1128/AEM.03947-12.
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 3116-3121
    • Hooks, D.O.1    Blatchford, P.A.2    Rehm, B.H.A.3
  • 12
    • 33644961915 scopus 로고    scopus 로고
    • In vivo enzyme immobilization by use of engineered polyhydroxyalkanoate synthase
    • Peters V, Rehm BH. 2006. In vivo enzyme immobilization by use of engineered polyhydroxyalkanoate synthase. Appl. Environ. Microbiol. 72: 1777-1783. http://dx.doi.org/10.1128/AEM.72.3.1777-1783.2006.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 1777-1783
    • Peters, V.1    Rehm, B.H.2
  • 13
    • 63849236826 scopus 로고    scopus 로고
    • One-step production of immobilized alphaamylase in recombinant Escherichia coli
    • Rasiah IA, Rehm BH. 2009. One-step production of immobilized alphaamylase in recombinant Escherichia coli. Appl. Environ. Microbiol. 75: 2012-2016. http://dx.doi.org/10.1128/AEM.02782-08.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 2012-2016
    • Rasiah, I.A.1    Rehm, B.H.2
  • 14
    • 84883146235 scopus 로고    scopus 로고
    • In vivo self-assembly of fluorescent protein microparticles displaying specific binding domains
    • Jahns AC, Maspolim Y, Chen S, Guthrie JM, Blackwell LF, Rehm BHA. 2013. In vivo self-assembly of fluorescent protein microparticles displaying specific binding domains. Bioconjug. Chem. 24:1314-1323. http://dx.doi.org/10.1021/bc300551j.
    • (2013) Bioconjug. Chem. , vol.24 , pp. 1314-1323
    • Jahns, A.C.1    Maspolim, Y.2    Chen, S.3    Guthrie, J.M.4    Blackwell, L.F.5    Rehm, B.H.A.6
  • 16
    • 69449086810 scopus 로고    scopus 로고
    • Tolerance of the Ralstonia eutropha class I polyhydroxyalkanoate synthase for translational fusions to its C terminus reveals a new mode of functional display
    • Jahns AC, Rehm BH. 2009. Tolerance of the Ralstonia eutropha class I polyhydroxyalkanoate synthase for translational fusions to its C terminus reveals a new mode of functional display. Appl. Environ. Microbiol. 75: 5461-5466. http://dx.doi.org/10.1128/AEM.01072-09.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 5461-5466
    • Jahns, A.C.1    Rehm, B.H.2
  • 17
    • 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 227:680-685. http://dx.doi.org/10.1038/227680a0.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0036489443 scopus 로고    scopus 로고
    • Green fluorescent protein (GFP)-applications, structure, and related photophysical behaviour
    • Zimmer M. 2002. Green fluorescent protein (GFP)-applications, structure, and related photophysical behaviour. Chem. Rev. 102:759-781. http://dx.doi.org/10.1021/cr010142r.
    • (2002) Chem. Rev. , vol.102 , pp. 759-781
    • Zimmer, M.1
  • 20
    • 0028773463 scopus 로고
    • The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli
    • Izard T, Lawrence MC, Malby RL, Lilley GG, Colman PM. 1994. The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli. Structure 2:361-369. http://dx.doi.org/10.1016/S0969-2126(00)00038-1.
    • (1994) Structure , vol.2 , pp. 361-369
    • Izard, T.1    Lawrence, M.C.2    Malby, R.L.3    Lilley, G.G.4    Colman, P.M.5
  • 21
    • 82255173613 scopus 로고    scopus 로고
    • Active protein aggregates produced in Escherichia coli
    • Peternel S, Komel R. 2011. Active protein aggregates produced in Escherichia coli. Int. J. Mol. Sci. 12:8275-8287. http://dx.doi.org/10.3390/ijms12118275.
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 8275-8287
    • Peternel, S.1    Komel, R.2
  • 23
    • 65249103916 scopus 로고    scopus 로고
    • Bacterial polyhydroxyalkanoate granules: biogenesis, structure, and potential use as nano-/micro-beads in biotechnological and biomedical applications
    • Grage K, Jahns AC, Parlane N, Palanisamy R, Rasiah IA, Atwood JA, Rehm BHA. 2009. Bacterial polyhydroxyalkanoate granules: biogenesis, structure, and potential use as nano-/micro-beads in biotechnological and biomedical applications. Biomacromolecules 10:660-669. http://dx.doi.org/10.1021/bm801394s.
    • (2009) Biomacromolecules , vol.10 , pp. 660-669
    • Grage, K.1    Jahns, A.C.2    Parlane, N.3    Palanisamy, R.4    Rasiah, I.A.5    Atwood, J.A.6    Rehm, B.H.A.7
  • 24
    • 20444498924 scopus 로고    scopus 로고
    • In vivo monitoring of PHA granule formation using GFP-labeled PHA synthases
    • Peters V, Rehm BH. 2005. In vivo monitoring of PHA granule formation using GFP-labeled PHA synthases. FEMS Microbiol. Lett. 248:93-100. http://dx.doi.org/10.1016/j.femsle.2005.05.027.
    • (2005) FEMS Microbiol. Lett. , vol.248 , pp. 93-100
    • Peters, V.1    Rehm, B.H.2
  • 26
    • 0037837789 scopus 로고    scopus 로고
    • Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface
    • Machius M, Declerck N, Huber R, Wiegand G. 2003. Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface. J. Biol. Chem. 278:11546-11553. http://dx.doi.org/10.1074/jbc.M212618200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11546-11553
    • Machius, M.1    Declerck, N.2    Huber, R.3    Wiegand, G.4
  • 27
    • 0025860553 scopus 로고
    • Purification, crystallisation and characterisation of N-acetylneuraminate lyase from Escherichia coli
    • Aisaka K, Igarashi A, Yamaguchi K, Uwajima T. 1991. Purification, crystallisation and characterisation of N-acetylneuraminate lyase from Escherichia coli. Biochem. J. 276:541-546.
    • (1991) Biochem. J. , vol.276 , pp. 541-546
    • Aisaka, K.1    Igarashi, A.2    Yamaguchi, K.3    Uwajima, T.4
  • 28
    • 79958190243 scopus 로고    scopus 로고
    • Production of N-acetyl-D-neuraminic acid by use of an efficient spore surface display system
    • Xu X, Gao C, Zhang X, Che B, Ma C, Qiu J, Tao F, Xu P. 2011. Production of N-acetyl-D-neuraminic acid by use of an efficient spore surface display system. Appl. Environ. Microbiol. 77:3197-3201. http://dx.doi.org/10.1128/AEM.00151-11.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 3197-3201
    • Xu, X.1    Gao, C.2    Zhang, X.3    Che, B.4    Ma, C.5    Qiu, J.6    Tao, F.7    Xu, P.8
  • 29
    • 0027416966 scopus 로고
    • Purification and characterization of a thermostable alpha-amylase from Bacillus licheniformis
    • Ivanova VN, Dobreva EP, Emanuilova EI. 1993. Purification and characterization of a thermostable alpha-amylase from Bacillus licheniformis. J. Biotechnol. 28:277-289. http://dx.doi.org/10.1016/0168-1656(93)90176-N.
    • (1993) J. Biotechnol. , vol.28 , pp. 277-289
    • Ivanova, V.N.1    Dobreva, E.P.2    Emanuilova, E.I.3
  • 30
    • 0021475896 scopus 로고
    • Purification and properties of N-acetylneuraminate lyase from Escherichia coli
    • Uchida Y, Tsukada Y, Sugimori T. 1984. Purification and properties of N-acetylneuraminate lyase from Escherichia coli. J. Biochem. 96:507-522.
    • (1984) J. Biochem. , vol.96 , pp. 507-522
    • Uchida, Y.1    Tsukada, Y.2    Sugimori, T.3
  • 31
    • 84859268823 scopus 로고    scopus 로고
    • Purification and characterization of methyl parathion hydrolase from Burkholderia cepacia capable of degrading organophosphate insecticides
    • Ekkhunnatham A, Jongsareejit B, Yamkunthong W, Wichitwechkarn J. 2012. Purification and characterization of methyl parathion hydrolase from Burkholderia cepacia capable of degrading organophosphate insecticides. World J. Microbiol. Biotechnol. 28:1739-1746. http://dx.doi.org/10.1007/s11274-011-0985-y.
    • (2012) World J. Microbiol. Biotechnol. , vol.28 , pp. 1739-1746
    • Ekkhunnatham, A.1    Jongsareejit, B.2    Yamkunthong, W.3    Wichitwechkarn, J.4
  • 32
    • 0025968498 scopus 로고
    • Purification and characterization of a secreted recombinant phosphotriesterase (parathion hydrolase) from Streptomyces lividans
    • Rowland SS, Speedie MK, Pogell BM. 1991. Purification and characterization of a secreted recombinant phosphotriesterase (parathion hydrolase) from Streptomyces lividans. Appl. Environ. Microbiol. 57:440-444.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 440-444
    • Rowland, S.S.1    Speedie, M.K.2    Pogell, B.M.3
  • 33
    • 0024316913 scopus 로고
    • Purification and properties of the phosphotriesterase from Pseudomonas diminuta
    • Dumas DP, Caldwell SR, Wild JR, Raushel FM. 1989. Purification and properties of the phosphotriesterase from Pseudomonas diminuta. J. Biol. Chem. 264:19659-19665.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19659-19665
    • Dumas, D.P.1    Caldwell, S.R.2    Wild, J.R.3    Raushel, F.M.4
  • 34
    • 0002870111 scopus 로고
    • In DeLuca MA, McElroyWD(ed), Bioluminescence and chemiluminescence. Academic Press, New York, NY.
    • Ward WW. 1981. Properties of the coelenterate green-fluorescent protein, p 235-242. In DeLuca MA, McElroyWD(ed), Bioluminescence and chemiluminescence. Academic Press, New York, NY.
    • (1981) Properties of the coelenterate green-fluorescent protein , pp. 235-242
    • Ward, W.W.1
  • 35
    • 84989716053 scopus 로고
    • Spectral perturbations of the Aequorea green-fluorescent protein
    • Ward WW, Prentice HJ, Roth AF, Cody CW, Reeves SC. 1982. Spectral perturbations of the Aequorea green-fluorescent protein. Photochem. Photobiol. 35:803-808. http://dx.doi.org/10.1111/j.1751-1097.1982.tb02651.x.
    • (1982) Photochem. Photobiol. , vol.35 , pp. 803-808
    • Ward, W.W.1    Prentice, H.J.2    Roth, A.F.3    Cody, C.W.4    Reeves, S.C.5
  • 36
    • 0030784698 scopus 로고    scopus 로고
    • Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy
    • Patterson GH, Knobel SM, Sharif WD, Kain SR, Piston DW. 1997. Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy. Biophys. J. 73:2782-2790. http://dx.doi.org/10.1016/S0006-3495(97)78307-3.
    • (1997) Biophys. J. , vol.73 , pp. 2782-2790
    • Patterson, G.H.1    Knobel, S.M.2    Sharif, W.D.3    Kain, S.R.4    Piston, D.W.5
  • 37
    • 0019892005 scopus 로고
    • Renaturation of Aequorea green fluorescent protein
    • Bokman SH, Ward WW. 1981. Renaturation of Aequorea green fluorescent protein. Biochem. Biophys. Res. Comm. 101:1372-1380. http://dx.doi.org/10.1016/0006-291X(81)91599-0.
    • (1981) Biochem. Biophys. Res. Comm. , vol.101 , pp. 1372-1380
    • Bokman, S.H.1    Ward, W.W.2


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