메뉴 건너뛰기




Volumn 160, Issue 1, 2011, Pages 1063-1069

AC-electrophoretic deposition of metalloenzymes: Catalase as a case study for the sensitive and selective detection of H2O2

Author keywords

AC electrophoretic deposition; Catalase; H2O 2 biosensor; Metalloenzymes

Indexed keywords

ACTIVE STATE; APPLIED CURRENT; CATALASE; DEPOSITION CONDITIONS; DEPOSITION TIME; DETECTION LIMITS; ENZYME LAYERS; ENZYME STRUCTURES; FAST RESPONSE TIME; LINEAR RESPONSE; METAL CATION; METALLOENZYMES; POLARIZATION POTENTIAL; POLYMER LAYERS; PULL OUT; SELECTIVE DETECTION; TRIANGULAR WAVEFORM;

EID: 81155148248     PISSN: 09254005     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.snb.2011.09.027     Document Type: Article
Times cited : (32)

References (47)
  • 1
    • 1242270622 scopus 로고    scopus 로고
    • Decontamination of broilers with hydrogen peroxide stabilised with glycerol during processing
    • C.L. Wagenaar, and J.M.A. Snijders Decontamination of broilers with hydrogen peroxide stabilised with glycerol during processing International Journal of Food Microbiology 91 2004 205
    • (2004) International Journal of Food Microbiology , vol.91 , pp. 205
    • Wagenaar, C.L.1    Snijders, J.M.A.2
  • 3
    • 0026762820 scopus 로고
    • Folic acid stability in hydrogen peroxide-potassium thiocyanate-treated milk
    • M.M. Taher, and N. Lakshmaiah Folic acid stability in hydrogen peroxide-potassium thiocyanate-treated milk Food Chemistry 44 1992 343
    • (1992) Food Chemistry , vol.44 , pp. 343
    • Taher, M.M.1    Lakshmaiah, N.2
  • 4
    • 33947189072 scopus 로고    scopus 로고
    • Time-course diffusion of hydrogen peroxide through human dentin: Clinical significance for young tooth internal bleaching
    • J. Camps, H. de Franceschi, F. Idir, C. Roland, and I. About Time-course diffusion of hydrogen peroxide through human dentin: clinical significance for young tooth internal bleaching Journal of Endodontics 33 2007 455
    • (2007) Journal of Endodontics , vol.33 , pp. 455
    • Camps, J.1    De Franceschi, H.2    Idir, F.3    Roland, C.4    About, I.5
  • 6
    • 0037203576 scopus 로고    scopus 로고
    • Hydrogen peroxide generation with immobilized glucose oxidase for textile bleaching
    • T. Tzanov, S.A. Costa, G.M. Gübitz, and A. Cavaco-Paulo Hydrogen peroxide generation with immobilized glucose oxidase for textile bleaching Journal of Biotechnology 93 2002 87
    • (2002) Journal of Biotechnology , vol.93 , pp. 87
    • Tzanov, T.1    Costa, S.A.2    Gübitz, G.M.3    Cavaco-Paulo, A.4
  • 7
    • 27644461493 scopus 로고    scopus 로고
    • Hydrogen peroxide bleaching of cotton in ultrasonic energy
    • S.. Mistik, and S.M. Yükseloglu Hydrogen peroxide bleaching of cotton in ultrasonic energy Ultrasonics 43 2005 811
    • (2005) Ultrasonics , vol.43 , pp. 811
    • Mistik, S.1    Yükseloglu, S.M.2
  • 8
    • 0037180957 scopus 로고    scopus 로고
    • Hydrogen peroxide is required for poly(phenolic) domain formation during wound-induced suberization
    • F.A. Razem, and M.A. Bernards Hydrogen peroxide is required for poly(phenolic) domain formation during wound-induced suberization Journal of Agricultural and Food Chemistry 50 2002 1009
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , pp. 1009
    • Razem, F.A.1    Bernards, M.A.2
  • 9
    • 67649366295 scopus 로고    scopus 로고
    • Kinetic studies on enzyme-catalyzed reactions: Oxidation of glucose, decomposition of hydrogen peroxide and their combination
    • Z. Tao, R.A. Raffel, A.K. Souid, and J. Goodisman Kinetic studies on enzyme-catalyzed reactions: oxidation of glucose, decomposition of hydrogen peroxide and their combination Biophysical Journal 96 2009 2977
    • (2009) Biophysical Journal , vol.96 , pp. 2977
    • Tao, Z.1    Raffel, R.A.2    Souid, A.K.3    Goodisman, J.4
  • 10
    • 0037010693 scopus 로고    scopus 로고
    • Minimization of by-product formation during d-amino acid oxidase catalyzed racemate resolution of d/l-amino acids
    • E.M. Trost, and L. Fischer Minimization of by-product formation during d-amino acid oxidase catalyzed racemate resolution of d/l-amino acids Journal of Molecular Catalysis B: Enzymatic 19-20 2002 189
    • (2002) Journal of Molecular Catalysis B: Enzymatic , vol.1920 , pp. 189
    • Trost, E.M.1    Fischer, L.2
  • 11
    • 0043133227 scopus 로고
    • Thallimetric oxidations - V: Titrimetric and spectrophotometric determination of hydrogen peroxide
    • M.S.P. Rao, A.R.M. Rao, K.V. Ramana, and S.R. Sagi Thallimetric oxidations - V: titrimetric and spectrophotometric determination of hydrogen peroxide Talanta 37 1990 753
    • (1990) Talanta , vol.37 , pp. 753
    • Rao, M.S.P.1    Rao, A.R.M.2    Ramana, K.V.3    Sagi, S.R.4
  • 12
    • 49949148356 scopus 로고
    • Titrimetric determination of hydrogen peroxide in alkaline solution
    • W.H. McCurdy Jr., and H.F. Bell Titrimetric determination of hydrogen peroxide in alkaline solution Talanta 13 1966 925
    • (1966) Talanta , vol.13 , pp. 925
    • McCurdy, Jr.W.H.1    Bell, H.F.2
  • 13
    • 1242306204 scopus 로고    scopus 로고
    • Rapid determination of hydrogen peroxide in the wood pulp bleaching streams by a dual - Wavelength spectroscopic method
    • X.S. Chai, Q.X. Hou, Q. Luo, and J.Y. Zhu Rapid determination of hydrogen peroxide in the wood pulp bleaching streams by a dual - wavelength spectroscopic method Analytica Chimica Acta 507 2004 281
    • (2004) Analytica Chimica Acta , vol.507 , pp. 281
    • Chai, X.S.1    Hou, Q.X.2    Luo, Q.3    Zhu, J.Y.4
  • 14
    • 0037170699 scopus 로고    scopus 로고
    • Determination of hydrogen peroxide by using a flow injection system with immobilized peroxidase and long pathlength capillary spectrophotometry
    • A.C. Pappas, C.D. Stalikas, Y.C. Fiamegos, and M.I. Karayannis Determination of hydrogen peroxide by using a flow injection system with immobilized peroxidase and long pathlength capillary spectrophotometry Analytica Chimica Acta 455 2002 305
    • (2002) Analytica Chimica Acta , vol.455 , pp. 305
    • Pappas, A.C.1    Stalikas, C.D.2    Fiamegos, Y.C.3    Karayannis, M.I.4
  • 15
    • 71349083369 scopus 로고    scopus 로고
    • Fluorometric determination of hydrogen peroxide in milk by using a Fenton reaction system
    • M.E. Abbas, W. Luo, L. Zhu, J. Zou, and H. Tang Fluorometric determination of hydrogen peroxide in milk by using a Fenton reaction system Food Chemistry 120 2010 327
    • (2010) Food Chemistry , vol.120 , pp. 327
    • Abbas, M.E.1    Luo, W.2    Zhu, L.3    Zou, J.4    Tang, H.5
  • 16
    • 0031734190 scopus 로고    scopus 로고
    • Fluorometric determination of microamounts of hydrogen peroxide with an immobilized enzyme prepared by coupling horseradish peroxidase to chitosan beads
    • A. Sakuragawa, T. Taniai, and T. Okutani Fluorometric determination of microamounts of hydrogen peroxide with an immobilized enzyme prepared by coupling horseradish peroxidase to chitosan beads Analytica Chimica Acta 374 1998 191
    • (1998) Analytica Chimica Acta , vol.374 , pp. 191
    • Sakuragawa, A.1    Taniai, T.2    Okutani, T.3
  • 17
    • 34248351966 scopus 로고    scopus 로고
    • A chemiluminescence sensor for the determination of hydrogen peroxide
    • A. Tahirović, A. Čopra, E. Omanović- Mikličanin, and K. Kalcher A chemiluminescence sensor for the determination of hydrogen peroxide Talanta 72 2007 1378
    • (2007) Talanta , vol.72 , pp. 1378
    • Tahirović, A.1    Čopra, A.2    Omanović-Mikličanin, E.3    Kalcher, K.4
  • 18
    • 0005488738 scopus 로고
    • Improved determination of hydrogen peroxide by measurement of peroxyoxalate chemiluminescence
    • G. Scott, W.R. Seitz, and J. Ambrose Improved determination of hydrogen peroxide by measurement of peroxyoxalate chemiluminescence Analytica Chimica Acta 115 1980 221
    • (1980) Analytica Chimica Acta , vol.115 , pp. 221
    • Scott, G.1    Seitz, W.R.2    Ambrose, J.3
  • 19
    • 0000240904 scopus 로고
    • Chemically immobilised enzyme electrodes for hydrogen peroxide determination
    • M. Cosgrove, G.J. Moody, and J.D.R. Thomas Chemically immobilised enzyme electrodes for hydrogen peroxide determination Analyst 113 1988 1811
    • (1988) Analyst , vol.113 , pp. 1811
    • Cosgrove, M.1    Moody, G.J.2    Thomas, J.D.R.3
  • 20
    • 0021969650 scopus 로고
    • Enzyme electrode sensor for hydrogen peroxide
    • A. Ciucu, V. Magearu, and C. Luca Enzyme electrode sensor for hydrogen peroxide Analytical Letters 18 1985 299
    • (1985) Analytical Letters , vol.18 , pp. 299
    • Ciucu, A.1    Magearu, V.2    Luca, C.3
  • 21
    • 0002764110 scopus 로고
    • Catalase biosensor for determination of hydrogen peroxide, fluoride and cyanide
    • K. Stein, and J.U. Hain Catalase biosensor for determination of hydrogen peroxide, fluoride and cyanide Microchimica Acta 118 1995 93
    • (1995) Microchimica Acta , vol.118 , pp. 93
    • Stein, K.1    Hain, J.U.2
  • 22
    • 0345320309 scopus 로고    scopus 로고
    • A novel biosensor for specific determination of hydrogen peroxide: Catalase enzyme electrode based on dissolved oxygen probe
    • S. Akgol, and E. Dinckaya A novel biosensor for specific determination of hydrogen peroxide: catalase enzyme electrode based on dissolved oxygen probe Talanta 48 1999 363
    • (1999) Talanta , vol.48 , pp. 363
    • Akgol, S.1    Dinckaya, E.2
  • 23
    • 5544310558 scopus 로고    scopus 로고
    • Catalase immobilization in cellulose acetate beads and determination of its hydrogen peroxide decomposition level by using a catalase biosensor
    • H. Yildiz, E. Akyilmaz, and E. Dinckaya Catalase immobilization in cellulose acetate beads and determination of its hydrogen peroxide decomposition level by using a catalase biosensor Artificial Cells, Blood Substitutes, and Biotechnology 32 2004 443
    • (2004) Artificial Cells, Blood Substitutes, and Biotechnology , vol.32 , pp. 443
    • Yildiz, H.1    Akyilmaz, E.2    Dinckaya, E.3
  • 25
    • 0043166779 scopus 로고    scopus 로고
    • Direct voltammetry and electrocatalytic properties of catalase incorporated in polyacrylamide hydrogel films
    • H. Lu, Z. Li, and N. Hu Direct voltammetry and electrocatalytic properties of catalase incorporated in polyacrylamide hydrogel films Biophysicscal Chemistry 104 2003 623
    • (2003) Biophysicscal Chemistry , vol.104 , pp. 623
    • Lu, H.1    Li, Z.2    Hu, N.3
  • 26
    • 1642533562 scopus 로고    scopus 로고
    • Synergy between IL-8 and GM-CSF in reproductive tract epithelial cell secretions promotes enhanced neutrophil chemotaxis
    • L. Shen, and N. Hu Synergy between IL-8 and GM-CSF in reproductive tract epithelial cell secretions promotes enhanced neutrophil chemotaxis Biochimica et Biophysica Acta 1608 2004 23
    • (2004) Biochimica et Biophysica Acta , vol.1608 , pp. 23
    • Shen, L.1    Hu, N.2
  • 27
    • 0005312139 scopus 로고
    • A specific bioelectrochemical sensor for hydrogen peroxide
    • M. Aizawa, I. Karube, and S. Suzuki A specific bioelectrochemical sensor for hydrogen peroxide Analytica Chimica Acta 69 1974 431
    • (1974) Analytica Chimica Acta , vol.69 , pp. 431
    • Aizawa, M.1    Karube, I.2    Suzuki, S.3
  • 28
    • 0036140089 scopus 로고    scopus 로고
    • Direct voltammetry and catalysis with Mycobacterium tuberculosis catalaseperoxidase, peroxidases, and catalase in lipid Wlms
    • Z. Zhang, S. Chouchane, R.S. Magiliozzo, and J.F. Rusling Direct voltammetry and catalysis with Mycobacterium tuberculosis catalaseperoxidase, peroxidases, and catalase in lipid Wlms Analytical Chemistry 74 2002 163
    • (2002) Analytical Chemistry , vol.74 , pp. 163
    • Zhang, Z.1    Chouchane, S.2    Magiliozzo, R.S.3    Rusling, J.F.4
  • 29
    • 0036176138 scopus 로고    scopus 로고
    • Bioelectrochemical studies on catalase-modified glassy carbon paste electrodes
    • S. Varma, and C.K. Mitra Bioelectrochemical studies on catalase-modified glassy carbon paste electrodes Electrochemistry Communications 4 2002 151
    • (2002) Electrochemistry Communications , vol.4 , pp. 151
    • Varma, S.1    Mitra, C.K.2
  • 30
    • 0035105120 scopus 로고    scopus 로고
    • Characterization for didodecyldimethylammonium bromide liquid crystal film entrapping catalase with enhanced direct electron transfer rate
    • X. Chen, H. Xie, J. Kong, and J. Deng Characterization for didodecyldimethylammonium bromide liquid crystal film entrapping catalase with enhanced direct electron transfer rate Biosensors and Bioelectronics 16 2001 115
    • (2001) Biosensors and Bioelectronics , vol.16 , pp. 115
    • Chen, X.1    Xie, H.2    Kong, J.3    Deng, J.4
  • 31
    • 4544231687 scopus 로고    scopus 로고
    • Direct electrochemistry of catalase at a gold electrode modified with single-wall carbon nanotubes
    • L. Wang, J. Wang, and F. Zhou Direct electrochemistry of catalase at a gold electrode modified with single-wall carbon nanotubes Electroanalysis 16 2004 627
    • (2004) Electroanalysis , vol.16 , pp. 627
    • Wang, L.1    Wang, J.2    Zhou, F.3
  • 32
    • 77149172544 scopus 로고    scopus 로고
    • Glucose microbiosensor based on glucose oxidase immobilized by AC-EPD: Characteristics and performance in human serum and in blood of critically ill rabbits
    • M. Ammam, and J. Fransaer Glucose microbiosensor based on glucose oxidase immobilized by AC-EPD: characteristics and performance in human serum and in blood of critically ill rabbits Sensors and Actuators B: Chemical 145 2010 46
    • (2010) Sensors and Actuators B: Chemical , vol.145 , pp. 46
    • Ammam, M.1    Fransaer, J.2
  • 33
    • 77952303823 scopus 로고    scopus 로고
    • Highly sensitive and selective glutamate microbiosensor based on cast polyurethane/AC-electrophoresis deposited multiwalled carbon nanotubes and then glutamate oxidase/electro-synthesized polypyrrole/Pt electrode
    • M. Ammam, and J. Fransaer Highly sensitive and selective glutamate microbiosensor based on cast polyurethane/AC-electrophoresis deposited multiwalled carbon nanotubes and then glutamate oxidase/electro-synthesized polypyrrole/Pt electrode Biosensors and Bioelectronics 25 2009 1597
    • (2009) Biosensors and Bioelectronics , vol.25 , pp. 1597
    • Ammam, M.1    Fransaer, J.2
  • 34
    • 77955305472 scopus 로고    scopus 로고
    • Two-enzyme lactose biosensor based on β-galactosidase and glucose oxidase deposited by AC-electrophoresis: Characteristics and performance for lactose determination in milk
    • M. Ammam, and J. Fransaer Two-enzyme lactose biosensor based on β-galactosidase and glucose oxidase deposited by AC-electrophoresis: characteristics and performance for lactose determination in milk Sensors and Actuators B: Chemical 148 2010 583
    • (2010) Sensors and Actuators B: Chemical , vol.148 , pp. 583
    • Ammam, M.1    Fransaer, J.2
  • 37
    • 0037080464 scopus 로고    scopus 로고
    • Fundamental studies of glucose oxidase deposition on a Pt electrode
    • N. Matsumoto, X. Chen, and G.S. Wilson Fundamental studies of glucose oxidase deposition on a Pt electrode Analytical Chemistry 74 2002 362
    • (2002) Analytical Chemistry , vol.74 , pp. 362
    • Matsumoto, N.1    Chen, X.2    Wilson, G.S.3
  • 38
    • 78049232302 scopus 로고    scopus 로고
    • A study on electrodeposition of glucose oxidase from low conductivity solutions
    • M. Ammam, and J. Fransaer A study on electrodeposition of glucose oxidase from low conductivity solutions Electrochimica Acta 55 2010 9125
    • (2010) Electrochimica Acta , vol.55 , pp. 9125
    • Ammam, M.1    Fransaer, J.2
  • 40
    • 68049142965 scopus 로고    scopus 로고
    • AC-electrophoretic deposition of glucose oxidase
    • M. Ammam, and J. Fransaer AC-electrophoretic deposition of glucose oxidase Biosensors and Bioelectronics 25 2009 191
    • (2009) Biosensors and Bioelectronics , vol.25 , pp. 191
    • Ammam, M.1    Fransaer, J.2
  • 41
    • 81155127708 scopus 로고    scopus 로고
    • Mathematical modeling of the amperometric response to glucose of glucose oxidase films deposited by AC-electrophoresis
    • J. Fransaer, and M. Ammam Mathematical modeling of the amperometric response to glucose of glucose oxidase films deposited by AC-electrophoresis Journal of Sensor Technology 1 2011 17
    • (2011) Journal of Sensor Technology , vol.1 , pp. 17
    • Fransaer, J.1    Ammam, M.2
  • 44
    • 0001586934 scopus 로고
    • Characterization of regenerated silk fibroin membrane for immobilizing peroxidase and construction of an amperometric hydrogen peroxide sensor employing phenazine methosulphate as electron shuttle
    • J. Qian, Y. Liu, H. Liu, T. Yu, and J. Deng Characterization of regenerated silk fibroin membrane for immobilizing peroxidase and construction of an amperometric hydrogen peroxide sensor employing phenazine methosulphate as electron shuttle Journal of Electroanalytical Chemistry 397 1995 157
    • (1995) Journal of Electroanalytical Chemistry , vol.397 , pp. 157
    • Qian, J.1    Liu, Y.2    Liu, H.3    Yu, T.4    Deng, J.5
  • 45
    • 0030579569 scopus 로고    scopus 로고
    • Silica sol-gel immobilized amperometric biosensor for hydrogen peroxide
    • J. Li, S.N. Tan, and H. Ge Silica sol-gel immobilized amperometric biosensor for hydrogen peroxide Analytica Chimica Acta 335 1996 137
    • (1996) Analytica Chimica Acta , vol.335 , pp. 137
    • Li, J.1    Tan, S.N.2    Ge, H.3
  • 46
    • 33846328380 scopus 로고    scopus 로고
    • Direct electrochemistry and electrocatalytic activity of catalase immobilized onto electrodeposited nano-scale islands of nickel oxide
    • A. Salimi, E. Sharifi, A. Noorbakhsh, and S. Soltanian Direct electrochemistry and electrocatalytic activity of catalase immobilized onto electrodeposited nano-scale islands of nickel oxide Biophysical Chemistry 125 2007 540
    • (2007) Biophysical Chemistry , vol.125 , pp. 540
    • Salimi, A.1    Sharifi, E.2    Noorbakhsh, A.3    Soltanian, S.4
  • 47
    • 0034360476 scopus 로고    scopus 로고
    • Specific determination of hydrogen peroxide with a catalase biosensor based on mercury thin film electrodes
    • N. Ertas Specific determination of hydrogen peroxide with a catalase biosensor based on mercury thin film electrodes Turkish Journal of Chemistry 24 2000 95
    • (2000) Turkish Journal of Chemistry , vol.24 , pp. 95
    • Ertas, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.