메뉴 건너뛰기




Volumn 113, Issue , 2015, Pages 56-62

Expression, purification and immobilization of recombinant AiiA enzyme onto magnetic nanoparticles

Author keywords

Acyl homoserine lactone; Immobilization; Magnetic nanoparticle; Quorum quenching; Quorum sensing; r AiiA

Indexed keywords

BACILLUS SP.; BACTERIA (MICROORGANISMS); POSIBACTERIA;

EID: 84930091508     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2015.04.014     Document Type: Article
Times cited : (15)

References (29)
  • 1
    • 33645080474 scopus 로고    scopus 로고
    • Quorum sensing: the many languages of bacteria
    • N.C. Reading, and V. Sperandio Quorum sensing: the many languages of bacteria FEMS Microbial. Lett. 254 2006 1 11
    • (2006) FEMS Microbial. Lett. , vol.254 , pp. 1-11
    • Reading, N.C.1    Sperandio, V.2
  • 2
    • 15944414231 scopus 로고    scopus 로고
    • Quorum sensing: the power of cooperation in the world of Pseudomonas
    • M. Juhas, L. Eberl, and B. Tummler Quorum sensing: the power of cooperation in the world of Pseudomonas Environ. Microbiol. 7 2005 459 471
    • (2005) Environ. Microbiol. , vol.7 , pp. 459-471
    • Juhas, M.1    Eberl, L.2    Tummler, B.3
  • 3
    • 78651386518 scopus 로고    scopus 로고
    • Perception and degradation of N-acyl homoserine lactone quorum sensing signals by mammalian and plant cells
    • M. Teplitski, U. Mathesius, and K.P. Rumbaugh Perception and degradation of N-acyl homoserine lactone quorum sensing signals by mammalian and plant cells Chem. Rev. 111 2011 100 116
    • (2011) Chem. Rev. , vol.111 , pp. 100-116
    • Teplitski, M.1    Mathesius, U.2    Rumbaugh, K.P.3
  • 4
    • 33644849230 scopus 로고    scopus 로고
    • Quorum-sensing inhibitors as anti-pathogenic drugs
    • T.B. Rasmussen, and M. Givskov Quorum-sensing inhibitors as anti-pathogenic drugs Int. J. Med. Microbiol. 296 2006 149 161
    • (2006) Int. J. Med. Microbiol. , vol.296 , pp. 149-161
    • Rasmussen, T.B.1    Givskov, M.2
  • 5
    • 79953219953 scopus 로고    scopus 로고
    • Paraoxonase 1, quorum sensing, and P. aeruginosa infection: a novel model
    • M.L. Estin, D.A. Stoltz, and J. Zabner Paraoxonase 1, quorum sensing, and P. aeruginosa infection: a novel model Adv. Exp. Med. Biol. 660 2010 183 193
    • (2010) Adv. Exp. Med. Biol. , vol.660 , pp. 183-193
    • Estin, M.L.1    Stoltz, D.A.2    Zabner, J.3
  • 6
    • 15944383000 scopus 로고    scopus 로고
    • Quorum sensing and quorum-quenching enzymes
    • Y.H. Dong, and L.H. Zhang Quorum sensing and quorum-quenching enzymes J. Microbiol. 43 2005 101 109
    • (2005) J. Microbiol. , vol.43 , pp. 101-109
    • Dong, Y.H.1    Zhang, L.H.2
  • 7
    • 62749134485 scopus 로고    scopus 로고
    • Quorum sensing: a new biofouling control paradigm in a membrane bioreactor for advanced wastewater treatment
    • K.M. Yeon, C.-H. Lee, and J. Kim Quorum sensing: a new biofouling control paradigm in a membrane bioreactor for advanced wastewater treatment Environ. Sci. Technol. 43 2009 380 385
    • (2009) Environ. Sci. Technol. , vol.43 , pp. 380-385
    • Yeon, K.M.1    Lee, C.-H.2    Kim, J.3
  • 8
    • 0034724191 scopus 로고    scopus 로고
    • AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora
    • Y.H. Dong, J.L. Xu, X.Z. Li, and L.H. Zhang AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora Proc. Natl. Acad. Sci. U.S.A. 97 2000 3526 3531
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 3526-3531
    • Dong, Y.H.1    Xu, J.L.2    Li, X.Z.3    Zhang, L.H.4
  • 9
    • 84871320219 scopus 로고    scopus 로고
    • AiiA quorum-sensing quenching controls proteolytic activity and biofilm formation by Enterobacter cloacae
    • P.A. dos Reis, M.L. Martins, E.F. de Araujo, H.C. Mantovani, and M.C. Vanetti AiiA quorum-sensing quenching controls proteolytic activity and biofilm formation by Enterobacter cloacae Curr. Microbiol. 65 6 2012 758 763
    • (2012) Curr. Microbiol. , vol.65 , Issue.6 , pp. 758-763
    • Dos Reis, P.A.1    Martins, M.L.2    De Araujo, E.F.3    Mantovani, H.C.4    Vanetti, M.C.5
  • 10
    • 78651394745 scopus 로고    scopus 로고
    • Macromolecular inhibition of quorum sensing: enzymes, antibodies, and beyond
    • N. Amara, B.P. Krom, G.F. Kaufmann, and M.M. Meijler Macromolecular inhibition of quorum sensing: enzymes, antibodies, and beyond Chem. Rev. 111 1 2011 195 208
    • (2011) Chem. Rev. , vol.111 , Issue.1 , pp. 195-208
    • Amara, N.1    Krom, B.P.2    Kaufmann, G.F.3    Meijler, M.M.4
  • 12
    • 84879373701 scopus 로고    scopus 로고
    • Quorum sensing inhibitors: a patent review
    • T. Jiang, and M. Li Quorum sensing inhibitors: a patent review Expert Opin. Ther. Pat. 23 2013 867 894
    • (2013) Expert Opin. Ther. Pat. , vol.23 , pp. 867-894
    • Jiang, T.1    Li, M.2
  • 13
    • 84857501798 scopus 로고    scopus 로고
    • Potential applications of enzymes immobilized on/in nano materials: a review
    • S.A. Ansari, and Q. Husain Potential applications of enzymes immobilized on/in nano materials: a review Biotechnol. Adv. 30 2012 512 523
    • (2012) Biotechnol. Adv. , vol.30 , pp. 512-523
    • Ansari, S.A.1    Husain, Q.2
  • 14
    • 84876664699 scopus 로고    scopus 로고
    • Enzyme-based formulations for decontamination: current state and perspectives
    • N. Grover, C.Z. Dinu, R.S. Kane, and J.S. Dordick Enzyme-based formulations for decontamination: current state and perspectives Appl. Microbiol. Biotechnol. 97 2013 3293 3300
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 3293-3300
    • Grover, N.1    Dinu, C.Z.2    Kane, R.S.3    Dordick, J.S.4
  • 15
    • 84865959000 scopus 로고    scopus 로고
    • Superparamagnetic nanoparticles as versatile carriers and supporting materials for enzymes
    • C.G.C.M. Netto, H.E. Toma, and L.H. Andrade Superparamagnetic nanoparticles as versatile carriers and supporting materials for enzymes J. Mol. Catal. B Enzym. 85-86 2013 71 92
    • (2013) J. Mol. Catal. B Enzym. , vol.85-86 , pp. 71-92
    • Netto, C.G.C.M.1    Toma, H.E.2    Andrade, L.H.3
  • 16
    • 84907857537 scopus 로고    scopus 로고
    • Interplay between amino acid residues at positions 192 and 115 in modulating hydrolytic activities of human paraoxonase 1
    • P. Bajaj, G. Aggarwal, R.K. Tripathy, and A.H. Pande Interplay between amino acid residues at positions 192 and 115 in modulating hydrolytic activities of human paraoxonase 1 Biochimie 105 2014 202 210
    • (2014) Biochimie , vol.105 , pp. 202-210
    • Bajaj, P.1    Aggarwal, G.2    Tripathy, R.K.3    Pande, A.H.4
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 84892904852 scopus 로고    scopus 로고
    • Characterization of human paraoxonase 1 variants suggest that His residues at 115 and 134 positions are not always needed for the lactonase/arylesterase activities of the enzyme
    • P. Bajaj, R.K. Tripathy, G. Aggarwal, and A.H. Pande Characterization of human paraoxonase 1 variants suggest that His residues at 115 and 134 positions are not always needed for the lactonase/arylesterase activities of the enzyme Protein Sci. 22 2013 1799 1807
    • (2013) Protein Sci. , vol.22 , pp. 1799-1807
    • Bajaj, P.1    Tripathy, R.K.2    Aggarwal, G.3    Pande, A.H.4
  • 21
    • 54749085873 scopus 로고    scopus 로고
    • LacZ-based detection of acyl-homoserine lactone quorum-sensing signals
    • 3:C:1C.2
    • A.C. Joelsson, and J. Zhu LacZ-based detection of acyl-homoserine lactone quorum-sensing signals Curr. Protoc. Microbiol. 3:C:1C.2 2006 1C.2.1-1C.2.9
    • (2006) Curr. Protoc. Microbiol. , pp. 1C.2.1-1C.2.9
    • Joelsson, A.C.1    Zhu, J.2
  • 23
    • 33846402453 scopus 로고    scopus 로고
    • Spreading of proteins and its effect on adsorption and desorption kinetics
    • M. Van der Veen, M.C. Stuart, and W. Norde Spreading of proteins and its effect on adsorption and desorption kinetics Colloids Surf. B. Biointerfaces 54 2007 136 142
    • (2007) Colloids Surf. B. Biointerfaces , vol.54 , pp. 136-142
    • Van Der Veen, M.1    Stuart, M.C.2    Norde, W.3
  • 25
    • 84911442164 scopus 로고    scopus 로고
    • A comparative study of immobilized lipase produced from Penicillum chrysogenum SNP5 on two different anionic carriers for its pH and thermostability
    • S. Kumar, R.K. Yadav, and S. Negi A comparative study of immobilized lipase produced from Penicillum chrysogenum SNP5 on two different anionic carriers for its pH and thermostability Indian J. Biotechnol. 13 2014 301 305
    • (2014) Indian J. Biotechnol. , vol.13 , pp. 301-305
    • Kumar, S.1    Yadav, R.K.2    Negi, S.3
  • 26
    • 79954627107 scopus 로고    scopus 로고
    • Immobilization of Candida rugosa lipase on electrospun cellulose nanofiber membrane
    • X.J. Huang, P.C. Chen, F. Huang, Y. Ou, M.R. Chen, and Z.K. Xu Immobilization of Candida rugosa lipase on electrospun cellulose nanofiber membrane J. Mol. Catal. B Enzym. 70 2011 95 100
    • (2011) J. Mol. Catal. B Enzym. , vol.70 , pp. 95-100
    • Huang, X.J.1    Chen, P.C.2    Huang, F.3    Ou, Y.4    Chen, M.R.5    Xu, Z.K.6
  • 27
    • 80053121939 scopus 로고    scopus 로고
    • Immobilization and stabilization of papain on poly(hydroxyethyl methacrylate-ethylenglycol dimethacrylate) beads grafted with epoxy functional polymer chains via surface-initiatedatom transfer radical polymerization (SI-ATRP)
    • G. Bayramoglu, B.F. Senkal, M. Yilmaz, and M.Y. Arica Immobilization and stabilization of papain on poly(hydroxyethyl methacrylate-ethylenglycol dimethacrylate) beads grafted with epoxy functional polymer chains via surface-initiatedatom transfer radical polymerization (SI-ATRP) Bioresour. Technol. 102 2010 9833 9837
    • (2010) Bioresour. Technol. , vol.102 , pp. 9833-9837
    • Bayramoglu, G.1    Senkal, B.F.2    Yilmaz, M.3    Arica, M.Y.4
  • 28
    • 79951639658 scopus 로고    scopus 로고
    • Enzyme-immobilized nanofiltration membrane to mitigate biofouling based on quorum quenching
    • J.H. Kim, D.C. Choi, K.M. Yeon, S.R. Kim, and C.H. Lee Enzyme-immobilized nanofiltration membrane to mitigate biofouling based on quorum quenching Environ. Sci. Technol. 45 2011 1601 1607
    • (2011) Environ. Sci. Technol. , vol.45 , pp. 1601-1607
    • Kim, J.H.1    Choi, D.C.2    Yeon, K.M.3    Kim, S.R.4    Lee, C.H.5
  • 29
    • 79953192545 scopus 로고    scopus 로고
    • Characterization of a phosphotriesterase-like lactonase from Sulfolobus solfataricus and its immobilization for disruption of quorum sensing
    • F.S.W. Ng, D.M. Wright, and S.Y. Seah Characterization of a phosphotriesterase-like lactonase from Sulfolobus solfataricus and its immobilization for disruption of quorum sensing Appl. Environ. Microbiol. 77 2011 1181 1186
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 1181-1186
    • Ng, F.S.W.1    Wright, D.M.2    Seah, S.Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.