메뉴 건너뛰기




Volumn 16, Issue 6, 2016, Pages

Enzyme biosensors for biomedical applications: Strategies for safeguarding analytical performances in biological fluids

Author keywords

Amperometry; Biological fluids; Biomedical applications; Biosensor; Interferents

Indexed keywords

BODY FLUIDS; CHEMICAL DETECTION; ENZYMES; MEDICAL APPLICATIONS;

EID: 84971607481     PISSN: 14248220     EISSN: None     Source Type: Journal    
DOI: 10.3390/s16060780     Document Type: Review
Times cited : (389)

References (160)
  • 2
    • 41549137931 scopus 로고    scopus 로고
    • Electrochemical Biosensors—Sensor Principles and Architectures
    • Grieshaber, D.; MacKenzie, R.; Vörös, J.; Reimhult, E. Electrochemical Biosensors—Sensor Principles and Architectures. Sensors 2008, 8, 1400–1458.
    • (2008) Sensors , vol.8 , pp. 1400-1458
    • Grieshaber, D.1    Mackenzie, R.2    Vörös, J.3    Reimhult, E.4
  • 3
    • 79955564258 scopus 로고    scopus 로고
    • Overview of Biosensor and Bioarray Technologies
    • Wiley: Weinheim, Germany
    • Lowe, R.S. Overview of Biosensor and Bioarray Technologies. In Handbook of Biosensors and Biochips; Wiley: Weinheim, Germany, 2007.
    • Handbook of Biosensors and Biochips , pp. 2007
    • Lowe, R.S.1
  • 4
    • 10244223555 scopus 로고
    • Electrode systems for continuous monitoring in cardiovascular surgery
    • Clark, L.C.; Lyons, C. Electrode systems for continuous monitoring in cardiovascular surgery. Ann. N.Y. Acad. Sci. 1962, 102, 29–45.
    • (1962) Ann. N.Y. Acad. Sci , vol.102 , pp. 29-45
    • Clark, L.C.1    Lyons, C.2
  • 5
    • 45849088857 scopus 로고    scopus 로고
    • Electrochemical biosensors-principles and applications
    • Pohanka, M.; Skládal, P. Electrochemical biosensors-principles and applications. J. Appl. Biomed. 2008, 6, 57–64.
    • (2008) J. Appl. Biomed , vol.6 , pp. 57-64
    • Pohanka, M.1    Skládal, P.2
  • 6
    • 12444330291 scopus 로고    scopus 로고
    • Biosensors in clinical chemistry
    • D’Orazio, P. Biosensors in clinical chemistry. Clin. Chim. Acta 2003, 334, 41–69.
    • (2003) Clin. Chim. Acta , vol.334 , pp. 41-69
    • D’Orazio, P.1
  • 7
    • 14744278807 scopus 로고    scopus 로고
    • Electrochemical immunosensors for the simultaneous detection of two tumor markers
    • Wilson, M.S. Electrochemical immunosensors for the simultaneous detection of two tumor markers. Anal. Chem. 2005, 77, 1496–1502.
    • (2005) Anal. Chem , vol.77 , pp. 1496-1502
    • Wilson, M.S.1
  • 8
    • 0036738408 scopus 로고    scopus 로고
    • Real-time electrochemical monitoring: Toward green analytical chemistry
    • Wang, J. Real-time electrochemical monitoring: toward green analytical chemistry. Acc. Chem. Res. 2002, 35, 811–816.
    • (2002) Acc. Chem. Res , vol.35 , pp. 811-816
    • Wang, J.1
  • 9
    • 0031161889 scopus 로고    scopus 로고
    • Composite Transducers for Amperometric Biosensors. The Glucose Sensor
    • Švorc, J.; Miertuš, S.; Katrlík, J.; Stred’anský, M. Composite Transducers for Amperometric Biosensors. The Glucose Sensor. Anal. Chem. 1997, 69, 2086–2090.
    • (1997) Anal. Chem. , vol.69 , pp. 2086-2090
    • Švorc, J.1    Miertuš, S.2    Katrlík, J.M.3
  • 12
    • 1842453356 scopus 로고    scopus 로고
    • Comparisons of platinum, gold, palladium and glassy carbon as electrode materials in the design of biosensors for glutamate
    • O’Neill, R.D.; Chang, S.C.; Lowry, J.P.; McNeil, C.J. Comparisons of platinum, gold, palladium and glassy carbon as electrode materials in the design of biosensors for glutamate. Biosens. Bioelectron. 2004, 19, 1521–1528.
    • (2004) Biosens. Bioelectron. , vol.19 , pp. 1521-1528
    • O’Neill, R.D.1    Chang, S.C.2    Lowry, J.P.3    McNeil, C.J.4
  • 13
    • 84899796713 scopus 로고    scopus 로고
    • Aptamer-based biosensors for biomedical diagnostics
    • Zhou, W.; Huang, P.J.; Ding, J.; Liu, J. Aptamer-based biosensors for biomedical diagnostics. Analyst 2014, 139, 2627–2640.
    • (2014) Analyst , vol.139 , pp. 2627-2640
    • Zhou, W.1    Huang, P.J.2    Ding, J.3    Liu, J.4
  • 15
    • 41549106353 scopus 로고    scopus 로고
    • Assembling Amperometric Biosensors for Clinical Diagnostics
    • Belluzo, M.S.; Ribone, M.E.; Lagier, C.M. Assembling Amperometric Biosensors for Clinical Diagnostics. Sensors 2008, 8, 1366–1399.
    • (2008) Sensors , vol.8 , pp. 1366-1399
    • Belluzo, M.S.1    Ribone, M.E.2    Lagier, C.M.3
  • 16
    • 84931040838 scopus 로고    scopus 로고
    • Blood, sweat, and tears: Developing clinically relevant protein biosensors for integrated body fluid analysis
    • Corrie, S.R.; Coffey, J.W.; Islam, J.; Markey, K.A.; Kendall, M.A. Blood, sweat, and tears: Developing clinically relevant protein biosensors for integrated body fluid analysis. Analyst 2015, 140, 4350–4364.
    • (2015) Analyst , vol.140 , pp. 4350-4364
    • Corrie, S.R.1    Coffey, J.W.2    Islam, J.3    Markey, K.A.4    Kendall, M.A.5
  • 17
    • 24744433042 scopus 로고    scopus 로고
    • Million-fold preconcentration of proteins and peptides by nanofluidic filter
    • Wang, Y.C.; Stevens, A.L.; Han, J. Million-fold preconcentration of proteins and peptides by nanofluidic filter. Anal. Chem. 2005, 77, 4293–4299.
    • (2005) Anal. Chem. , vol.77 , pp. 4293-4299
    • Wang, Y.C.1    Stevens, A.L.2    Han, J.3
  • 19
  • 21
    • 77958007974 scopus 로고    scopus 로고
    • Electrochemical Glucose Sensors—Developments Using Electrostatic Assembly and Carbon Nanotubes for Biosensor Construction
    • Harper, A.; Anderson, M.R. Electrochemical Glucose Sensors—Developments Using Electrostatic Assembly and Carbon Nanotubes for Biosensor Construction. Sensors 2010, 10, 8248–8274.
    • (2010) Sensors , vol.10 , pp. 8248-8274
    • Harper, A.1    Anderson, M.R.2
  • 22
    • 84871174854 scopus 로고    scopus 로고
    • An Amperometric Biosensor Based on Direct Immobilization of Horseradish Peroxidase on Electrochemically Reduced Graphene Oxide Modified Screen Printed Carbon Electrode
    • Palanisamy, S.; Unnikrishnan, B.; Chen, S. An Amperometric Biosensor Based on Direct Immobilization of Horseradish Peroxidase on Electrochemically Reduced Graphene Oxide Modified Screen Printed Carbon Electrode. Int. J. Electrochem. Sci. 2012, 7, 7935–7947.
    • (2012) Int. J. Electrochem. Sci , vol.7 , pp. 7935-7947
    • Palanisamy, S.1    Unnikrishnan, B.2    Chen, S.3
  • 23
    • 40449109054 scopus 로고    scopus 로고
    • Electrochemical Glucose Biosensors
    • Wang, J. Electrochemical Glucose Biosensors. Chem. Rev. 2008, 108, 814–825.
    • (2008) Chem. Rev , vol.108 , pp. 814-825
    • Wang, J.1
  • 24
    • 33645688056 scopus 로고    scopus 로고
    • Control of the oxygen dependence of an implantable polymer/enzyme composite biosensor for glutamate
    • McMahon, C.P.; Rocchitta, G.; Serra, P.A.; Kirwan, S.M.; Lowry, J.P.; O’Neill, R.D. Control of the oxygen dependence of an implantable polymer/enzyme composite biosensor for glutamate. Anal. Chem. 2006, 78, 2352–2359.
    • (2006) Anal. Chem , vol.78 , pp. 2352-2359
    • McMahon, C.P.1    Rocchitta, G.2    Serra, P.A.3    Kirwan, S.M.4    Lowry, J.P.5    O’Neill, R.D.6
  • 25
    • 84958280163 scopus 로고    scopus 로고
    • Plain to point network reduced graphene oxide—Activated carbon composites decorated with platinum nanoparticles for urine glucose detection
    • Hossain, M.F.; Park, J.Y. Plain to point network reduced graphene oxide—Activated carbon composites decorated with platinum nanoparticles for urine glucose detection. Sci. Rep. 2016.
    • (2016) Sci. Rep
    • Hossain, M.F.1    Park, J.Y.2
  • 26
    • 84944096447 scopus 로고    scopus 로고
    • Biosensing of glucose in flow injection analysis system based on glucose oxidase-quantum dot modified pencil graphite electrode
    • Sağlam, Ö.; Kızılkaya, B.; Uysal, H.; Dilgin, Y. Biosensing of glucose in flow injection analysis system based on glucose oxidase-quantum dot modified pencil graphite electrode. Talanta 2016.
    • (2016) Talanta
    • Sağlam, Ö.1    Kızılkaya, B.2    Uysal, H.3    Dilgin, Y.4
  • 29
    • 84971654615 scopus 로고    scopus 로고
    • An amperometric biosensor for L-glutamate determination prepared from L-glutamate oxidase immobilized in polypyrrole-polyvinylsulphonate film
    • Şimşek, Ş.; Aynacļ E.; Arslaņ F. An amperometric biosensor for L-glutamate determination prepared from L-glutamate oxidase immobilized in polypyrrole-polyvinylsulphonate film. Artif. Cells Nanomed. Biotechnol. 2016, 44, 356–361.
    • (2016) Artif. Cells Nanomed. Biotechnol , vol.44 , pp. 356-361
    • Şimşek, Ş.1    Aynacļ, E.2    Arslaņ, F.3
  • 31
    • 30844474185 scopus 로고    scopus 로고
    • The efficiency of immobilised glutamate oxidase decreases with surface enzyme loading: An electrostatic effect, and reversal by a polycation significantly enhances biosensor sensitivity
    • McMahon, C.P.; Rocchitta, G.; Serra, P.A.; Kirwan, S.M.; Lowry, J.P.; O’Neill, R.D. The efficiency of immobilised glutamate oxidase decreases with surface enzyme loading: An electrostatic effect, and reversal by a polycation significantly enhances biosensor sensitivity. Analyst 2006, 131, 68–72.
    • (2006) Analyst , vol.131 , pp. 68-72
    • McMahon, C.P.1    Rocchitta, G.2    Serra, P.A.3    Kirwan, S.M.4    Lowry, J.P.5    O’Neill, R.D.6
  • 32
    • 84923287559 scopus 로고    scopus 로고
    • Alcohol oxidase protein mediated in-situ synthesized and stabilized gold nanoparticles for developing amperometric alcohol biosensor
    • Chinnadayyala, S.R.; Santhosh, M.; Singh, N.K.; Goswami, P. Alcohol oxidase protein mediated in-situ synthesized and stabilized gold nanoparticles for developing amperometric alcohol biosensor. Biosens. Bioelectron. 2015, 69, 155–161.
    • (2015) Biosens. Bioelectron , vol.69 , pp. 155-161
    • Chinnadayyala, S.R.1    Santhosh, M.2    Singh, N.K.3    Goswami, P.4
  • 33
    • 84890116639 scopus 로고    scopus 로고
    • Novel non-invasive electrochemical biosensing device for in situ determination of the alcohol content in blood by monitoring ethanol in sweat
    • Gamella, M.; Campuzano, S.; Manso, J.; González de Rivera, G.; López-Colino, F.; Reviejo, A.J.; Pingarrón, J.M. A novel non-invasive electrochemical biosensing device for in situ determination of the alcohol content in blood by monitoring ethanol in sweat. Anal. Chim. Acta 2014, 806, 1–7.
    • (2014) Anal. Chim. Acta , vol.806 , pp. 1-7
    • Gamella, M.1    Campuzano, S.2    Manso, J.3    González De Rivera, G.4    López-Colino, F.5    Reviejo, A.J.6    Pingarrón, J.7
  • 35
    • 84865512263 scopus 로고    scopus 로고
    • Development and characterization of an implantable biosensor for telemetric monitoring of ethanol in the brain of freely moving rats
    • Rocchitta, G.; Secchi, O.; Alvau, M.D.; Migheli, R.; Calia, G.; Bazzu, G.; Farina, D.; Desole, M.S.; O’Neill, R.D.; Serra, P.A. Development and characterization of an implantable biosensor for telemetric monitoring of ethanol in the brain of freely moving rats. Anal. Chem. 2012, 84, 7072–7079.
    • (2012) Anal. Chem , vol.84 , pp. 7072-7079
    • Rocchitta, G.1    Secchi, O.2    Alvau, M.D.3    Migheli, R.4    Calia, G.5    Bazzu, G.6    Farina, D.7    Desole, M.S.8    O’Neill, R.D.9    Serra, P.A.10
  • 37
    • 84946729731 scopus 로고    scopus 로고
    • Electrochemical lactate biosensor based upon chitosan/carbon nanotubes modified screen-printed graphite electrodes for the determination of lactate in embryonic cell cultures
    • Hernández-Ibáñez, N.; García-Cruz, L.; Montiel, V.; Foster, C.W.; Banks, C.E.; Iniesta, J. Electrochemical lactate biosensor based upon chitosan/carbon nanotubes modified screen-printed graphite electrodes for the determination of lactate in embryonic cell cultures. Biosens. Bioelectron. 2016, 77, 1168–1174.
    • (2016) Biosens. Bioelectron , vol.77 , pp. 1168-1174
    • Hernández-Ibáñez, N.1    García-Cruz, L.2    Montiel, V.3    Foster, C.W.4    Banks, C.E.5    Iniesta, J.6
  • 38
    • 84944317490 scopus 로고    scopus 로고
    • Characterization of Lactate Sensors Based on Lactate Oxidase and Palladium Benzoporphyrin Immobilized in Hydrogels
    • Andrus, L.P.; Unruh, R.; Wisniewski, N.A.; McShane, M.J. Characterization of Lactate Sensors Based on Lactate Oxidase and Palladium Benzoporphyrin Immobilized in Hydrogels. Biosensors 2015, 5, 398–416.
    • (2015) Biosensors , vol.5 , pp. 398-416
    • Andrus, L.P.1    Unruh, R.2    Wisniewski, N.A.3    McShane, M.J.4
  • 39
    • 85027955482 scopus 로고    scopus 로고
    • Biosensor based on the immobilization of ascorbate oxidase into the biocompatible sandwich-type composite film
    • Wen, Y.; Xu, J.; Liu, M.; Li, D.; He, H. Amperometric vitamin C biosensor based on the immobilization of ascorbate oxidase into the biocompatible sandwich-type composite film. Appl. Biochem. Biotechnol. 2012, 167, 2023–2038.
    • (2012) Appl. Biochem. Biotechnol , vol.167 , pp. 2023-2038
    • Wen, Y.1    Xu, J.2    Liu, M.3    Li, D.4    He, H.5    Amperometric Vitamin, C.6
  • 40
    • 79957534543 scopus 로고    scopus 로고
    • An amperometric biosensor based on ascorbate oxidase immobilized in poly(3,4-ethylenedioxythiophene)/multi-walled carbon nanotubes composite films for the determination of L-ascorbic acid
    • Liu, M.; Wen, Y.; Xu, J.; He, H.; Li, D.; Yue, R.; Liu, G. An amperometric biosensor based on ascorbate oxidase immobilized in poly(3,4-ethylenedioxythiophene)/multi-walled carbon nanotubes composite films for the determination of L-ascorbic acid. Anal. Sci. 2011, 27, 477.
    • (2011) Anal. Sci , vol.27 , pp. 477
    • Liu, M.1    Wen, Y.2    Xu, J.3    He, H.4    Li, D.5    Yue, R.6    Liu, G.7
  • 41
    • 84958279804 scopus 로고    scopus 로고
    • Fabrication and Optimization of ChE/ChO/HRP-AuNPs/c-MWCNTs Based Silver Electrode for Determining Total Cholesterol in Serum
    • Lata, K.; Dhull, V.; Hooda, V. Fabrication and Optimization of ChE/ChO/HRP-AuNPs/c-MWCNTs Based Silver Electrode for Determining Total Cholesterol in Serum. Biochem. Res. Int. 2016.
    • (2016) Biochem. Res. Int
    • Lata, K.1    Dhull, V.2    Hooda, V.3
  • 42
    • 84959461859 scopus 로고    scopus 로고
    • Amperometric determination of serum total cholesterol with nanoparticles of cholesterol esterase and cholesterol oxidase
    • Aggarwal, V.; Malik, J.; Prashant, A.; Jaiwal, P.K.; Pundir, C.S. Amperometric determination of serum total cholesterol with nanoparticles of cholesterol esterase and cholesterol oxidase. Anal. Biochem. 2016.
    • (2016) Anal. Biochem
    • Aggarwal, V.1    Malik, J.2    Prashant, A.3    Jaiwal, P.K.4    Pundir, C.S.5
  • 43
    • 84920277104 scopus 로고    scopus 로고
    • Cholesterol Oxidase Functionalised Polyaniline/Carbon Nanotube Hybrids for an Amperometric Biosensor
    • Shukla, S.K.; Turner, A.P.; Tiwari, A. Cholesterol Oxidase Functionalised Polyaniline/Carbon Nanotube Hybrids for an Amperometric Biosensor. J. Nanosci. Nanotechnol. 2015, 15, 3373–3377.
    • (2015) J. Nanosci. Nanotechnol , vol.15 , pp. 3373-3377
    • Shukla, S.K.1    Turner, A.P.2    Tiwari, A.3
  • 44
    • 84946866771 scopus 로고    scopus 로고
    • Selective choline biosensors based on choline oxidase co-immobilized into self-assembled monolayers on micro-chips at low potential
    • Rahman, M.M.; Asiria, A.M. Selective choline biosensors based on choline oxidase co-immobilized into self-assembled monolayers on micro-chips at low potential. Anal. Methods 2015, 7, 9426–9434.
    • (2015) Anal. Methods , vol.7 , pp. 9426-9434
    • Rahman, M.M.1    Asiria, A.M.2
  • 46
    • 84945584983 scopus 로고    scopus 로고
    • Fabrication of an Amperometric Flow-Injection Microfluidic Biosensor Based on Laccase for In Situ Determination of Phenolic Compounds
    • Gonzalez-Rivera, J.C.; Osma, J.F. Fabrication of an Amperometric Flow-Injection Microfluidic Biosensor Based on Laccase for In Situ Determination of Phenolic Compounds. Biomed. Res. Int. 2015, 2015, 845261.
    • (2015) Biomed. Res. Int , vol.2015
    • Gonzalez-Rivera, J.C.1    Osma, J.F.2
  • 47
    • 84922294203 scopus 로고    scopus 로고
    • New amperometric biosensor based on Fe3O4/polyaniline/ laccase/chitosan biocomposite-modified carbon paste electrode for determination of catechol in tea leaves
    • 4/polyaniline/ laccase/chitosan biocomposite-modified carbon paste electrode for determination of catechol in tea leaves. Appl. Biochem. Biotechnol. 2015, 175, 1603–1616.
    • (2015) Appl. Biochem. Biotechnol , vol.175 , pp. 1603-1616
    • Sadeghi, S.1    Fooladi, E.2    Malekaneh, M.A.3
  • 49
    • 84951738909 scopus 로고    scopus 로고
    • Fatibello-Filho, O. A biosensor based on gold nanoparticles, dihexadecylphosphate, and tyrosinase for the determination of catechol in natural water
    • Campanhã Vicentini, F.; Garcia, L.L.; Figueiredo-Filho, L.C.; Janegitz, B.C.; Fatibello-Filho, O. A biosensor based on gold nanoparticles, dihexadecylphosphate, and tyrosinase for the determination of catechol in natural water. Enzyme Microb. Technol. 2016, 84, 17–23.
    • (2016) Enzyme Microb. Technol , vol.84 , pp. 17-23
    • Campanhã Vicentini, F.1    Garcia, L.L.2    Figueiredo-Filho, L.C.3    Janegitz, B.C.4
  • 51
    • 76149086819 scopus 로고    scopus 로고
    • Amperometric detection of dopamine in vivo with an enzyme based carbon fiber microbiosensor
    • Njagi, J.; Chernov, M.M.; Leiter, J.C.; Andreescu, S. Amperometric detection of dopamine in vivo with an enzyme based carbon fiber microbiosensor. Anal. Chem. 2010, 82, 989–996.
    • (2010) Anal. Chem , vol.82 , pp. 989-996
    • Njagi, J.1    Chernov, M.M.2    Leiter, J.C.3    Andreescu, S.4
  • 52
    • 84859941215 scopus 로고    scopus 로고
    • Amperometric biosensors key work principles and features of transducers of different generations
    • Dzyadevych, S.V. Amperometric biosensors key work principles and features of transducers of different generations. Biopol. Cell. 2002, 18, 13–25.
    • (2002) Biopol. Cell , vol.18 , pp. 13-25
    • Dzyadevych, S.V.1
  • 53
    • 64549085346 scopus 로고    scopus 로고
    • Preparation of multiwalled carbon nanotube-chitosan-alcohol dehydrogenase nanobiocomposite for amperometric detection of ethanol
    • Lee, C.A.; Tsai, Y.C. Preparation of multiwalled carbon nanotube-chitosan-alcohol dehydrogenase nanobiocomposite for amperometric detection of ethanol. Sens. Actuators B Chem. 2009, 138, 518–523.
    • (2009) Sens. Actuators B Chem , vol.138 , pp. 518-523
    • Lee, C.A.1    Tsai, Y.C.2
  • 54
    • 84941261814 scopus 로고    scopus 로고
    • Scaffold electrodes based on thioctic acid-capped gold nanoparticles coordinated Alcohol Dehydrogenase and Azure A films for high performance biosensor
    • Gómez-Anquela, C.; García-Mendiola, T.; Abad, J.M.; Pita, M.; Pariente, F.; Lorenzo, E. Scaffold electrodes based on thioctic acid-capped gold nanoparticles coordinated Alcohol Dehydrogenase and Azure A films for high performance biosensor. Bioelectrochemistry 2015, 106, 335–342.
    • (2015) Bioelectrochemistry , vol.106 , pp. 335-342
    • Gómez-Anquela, C.1    García-Mendiola, T.2    Abad, J.M.3    Pita, M.4    Pariente, F.5    Lorenzo, E.6
  • 55
    • 84912574762 scopus 로고    scopus 로고
    • Amperometric measurements of ethanol on paper with a glucometer
    • Wu, G.; Zaman, M.H. Amperometric measurements of ethanol on paper with a glucometer. Talanta 2015, 134, 194–199.
    • (2015) Talanta , vol.134 , pp. 194-199
    • Wu, G.1    Zaman, M.H.2
  • 56
    • 84876705312 scopus 로고    scopus 로고
    • A sensitive NADH and ethanol biosensor based on Graphene-Au nanorods nanocomposites
    • Li, L.; Lu, H.; Deng, L. A sensitive NADH and ethanol biosensor based on Graphene-Au nanorods nanocomposites. Talanta 2013, 113, 1–6.
    • (2013) Talanta , vol.113 , pp. 1-6
    • Li, L.1    Lu, H.2    Deng, L.3
  • 57
    • 84870770426 scopus 로고    scopus 로고
    • Anovel electrochemiluminescence ethanol biosensor based on tris(2,21-bipyridine) ruthenium (II) and alcohol dehydrogenase immobilized in graphene/bovine serum albumin composite film
    • Gao, W.; Chen, Y.; Xi, J.; Lin, S.; Chen, Y.; Lin, Y.; Chen, Z. Anovel electrochemiluminescence ethanol biosensor based on tris(2,21-bipyridine) ruthenium (II) and alcohol dehydrogenase immobilized in graphene/bovine serum albumin composite film. Biosens. Bioelectron. 2013, 41, 776–782.
    • (2013) Biosens. Bioelectron , vol.41 , pp. 776-782
    • Gao, W.1    Chen, Y.2    Xi, J.3    Lin, S.4    Chen, Y.5    Lin, Y.6    Chen, Z.7
  • 58
    • 84930821477 scopus 로고    scopus 로고
    • Amperometric L-glutamate biosensor based on bacterial cell-surface displayed glutamate dehydrogenase
    • Liang, B.; Zhang, S.; Lang, Q.; Song, J.; Han, L.; Liu, A. Amperometric L-glutamate biosensor based on bacterial cell-surface displayed glutamate dehydrogenase. Anal. Chim. Acta 2015, 884, 83–89.
    • (2015) Anal. Chim. Acta , vol.884 , pp. 83-89
    • Liang, B.1    Zhang, S.2    Lang, Q.3    Song, J.4    Han, L.5    Liu, A.6
  • 59
    • 84894461495 scopus 로고    scopus 로고
    • Quantitative determination of glycine in aqueous solution using glutamate dehydrogenase-immobilized glyoxal agarose beads
    • Keskin, S.Y.; Keskin, C.S. Quantitative determination of glycine in aqueous solution using glutamate dehydrogenase-immobilized glyoxal agarose beads. Appl. Biochem. Biotechnol. 2014, 172, 289–297.
    • (2014) Appl. Biochem. Biotechnol , vol.172 , pp. 289-297
    • Keskin, S.Y.1    Keskin, C.S.2
  • 60
    • 84455169580 scopus 로고    scopus 로고
    • Mediator-less highly sensitive voltammetric detection of glutamate using glutamate dehydrogenase/ vertically aligned CNTs grown on silicon substrate
    • Gholizadeh, A.; Shahrokhian, S.; zad, A.I.; Mohajerzadeh, S.; Vosoughi, M.; Darbari, S.; Sanaee, Z. Mediator-less highly sensitive voltammetric detection of glutamate using glutamate dehydrogenase/ vertically aligned CNTs grown on silicon substrate. Biosens. Bioelectron. 2012, 31, 110–115.
    • (2012) Biosens. Bioelectron , vol.31 , pp. 110-115
    • Gholizadeh, A.1    Shahrokhian, S.2    Zad, A.I.3    Mohajerzadeh, S.4    Vosoughi, M.5    Darbari, S.6    Sanaee, Z.7
  • 62
    • 84898843844 scopus 로고    scopus 로고
    • Continuous and simultaneous electrochemical measurements of glucose, lactate, and ascorbate in rat brain following brain ischemia
    • Lin, Y.; Yu, P.; Hao, J.; Wang, Y.; Ohsaka, T.; Mao, L. Continuous and simultaneous electrochemical measurements of glucose, lactate, and ascorbate in rat brain following brain ischemia. Anal. Chem. 2014, 86, 3895–3901.
    • (2014) Anal. Chem , vol.86 , pp. 3895-3901
    • Lin, Y.1    Yu, P.2    Hao, J.3    Wang, Y.4    Ohsaka, T.5    Mao, L.6
  • 63
    • 84889017108 scopus 로고    scopus 로고
    • Electron-transfer mediator for a NAD-glucose dehydrogenase-based glucose sensor
    • Kim, D.M.; Kim, M.Y.; Reddy, S.S.; Cho, J.; Cho, C.H.; Jung, S.; Shim, Y.B. Electron-transfer mediator for a NAD-glucose dehydrogenase-based glucose sensor. Anal. Chem. 2013, 85, 11643–11649.
    • (2013) Anal. Chem , vol.85 , pp. 11643-11649
    • Kim, D.M.1    Kim, M.Y.2    Reddy, S.S.3    Cho, J.4    Cho, C.H.5    Jung, S.6    Shim, Y.B.7
  • 65
    • 84937204860 scopus 로고    scopus 로고
    • Development of L-lactate dehydrogenase biosensor based on porous silicon resonant microcavities as fluorescence enhancers
    • Jenie, S.N.; Prieto-Simon, B.; Voelcker, N.H. Development of L-lactate dehydrogenase biosensor based on porous silicon resonant microcavities as fluorescence enhancers. Biosens. Bioelectron. 2015, 74, 637–643.
    • (2015) Biosens. Bioelectron , vol.74 , pp. 637-643
    • Jenie, S.N.1    Prieto-Simon, B.2    Voelcker, N.H.3
  • 66
    • 84924705782 scopus 로고    scopus 로고
    • A novel amperometric biosensor based on gold nanoparticles anchored on reduced graphene oxide for sensitive detection of L-lactate tumor biomarker
    • Azzouzi, S.; Rotariu, L.; Benito, A.M.; Maser, W.K.; Ben Ali, M.; Bala, C. A novel amperometric biosensor based on gold nanoparticles anchored on reduced graphene oxide for sensitive detection of L-lactate tumor biomarker. Biosens. Bioelectron. 2015, 69, 280–286.
    • (2015) Biosens. Bioelectron , vol.69 , pp. 280-286
    • Azzouzi, S.1    Rotariu, L.2    Benito, A.M.3    Maser, W.K.4    Ben Ali, M.5    Bala, C.6
  • 67
    • 0036204377 scopus 로고    scopus 로고
    • Enzyme Based Amperometric Biosensors for Food Analysis
    • Prodromidis, M.I.; Karayannis, M.I. Enzyme Based Amperometric Biosensors for Food Analysis. Electroanalysis 2002, 14, 241–261.
    • (2002) Electroanalysis , vol.14 , pp. 241-261
    • Prodromidis, M.I.1    Karayannis, M.I.2
  • 68
    • 44949273562 scopus 로고
    • Enzyme electrode studies of glucose oxidase modified with a redox mediator
    • Bartlett, P.N.; Bradford, V.Q.; Whitaker, R.G. Enzyme electrode studies of glucose oxidase modified with a redox mediator. Talanta 1991, 38, 57–63.
    • (1991) Talanta , vol.38 , pp. 57-63
    • Bartlett, P.N.1    Bradford, V.Q.2    Whitaker, R.G.3
  • 70
    • 0031033309 scopus 로고    scopus 로고
    • Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases
    • Xu, F. Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases. J. Biol. Chem. 1997, 272, 924–928.
    • (1997) J. Biol. Chem , vol.272 , pp. 924-928
    • Xu, F.1
  • 71
    • 77950488214 scopus 로고    scopus 로고
    • Laccase: Proprieties and applications
    • Madhavi, V.; Lele, S.S. Laccase: Proprieties and applications. Bioresources 2009, 4, 1694–1717.
    • (2009) Bioresources , vol.4 , pp. 1694-1717
    • Madhavi, V.1    Lele, S.S.2
  • 72
    • 84971608915 scopus 로고    scopus 로고
    • Soft Computing Techniques in Modelling the Influence of pH and Temperature on Dopamine Biosensor
    • INTECH: Rijeka, Croatia
    • Rangelova, V.; Tsankova, D.; Dimcheva, N. Soft Computing Techniques in Modelling the Influence of pH and Temperature on Dopamine Biosensor. In Intelligent and Biosensors; INTECH: Rijeka, Croatia, 2010; pp. 100–122.
    • (2010) Intelligent and Biosensors , pp. 100-122
    • Rangelova, V.1    Tsankova, D.2    Dimcheva, N.3
  • 74
    • 0042330462 scopus 로고    scopus 로고
    • Amperometric immunosensor based on polypyrrole/poly(M-pheylenediamine) multilayer on glassy carbon electrode for cytokinin N6-(Delta2-isopentenyl) adenosine assay
    • Li, J.; Xiao, L.T.; Zeng, G.M.; Huang, G.H.; Shen, G.L.; Yu, R.Q. Amperometric immunosensor based on polypyrrole/poly(m-pheylenediamine) multilayer on glassy carbon electrode for cytokinin N6-(Delta2-isopentenyl) adenosine assay. Anal. Biochem. 2003, 321, 89–95.
    • (2003) Anal. Biochem , vol.321 , pp. 89-95
    • Li, J.1    Xiao, L.T.2    Zeng, G.M.3    Huang, G.H.4    Shen, G.L.5    Yu, R.Q.6
  • 75
    • 9744237987 scopus 로고    scopus 로고
    • Electrochemical Detection of Protein Using a Double Aptamer Sandwich
    • Ikebukuro, K.; Kiyohara, C.; Sode, K. Electrochemical Detection of Protein Using a Double Aptamer Sandwich. Anal. Lett. 2004, 37, 2901–2909.
    • (2004) Anal. Lett , vol.37 , pp. 2901-2909
    • Ikebukuro, K.1    Kiyohara, C.2    Sode, K.3
  • 76
    • 33847196810 scopus 로고    scopus 로고
    • Aptamer-based detection of plasma proteins by an electrochemical assay coupled to magnetic beads
    • Centi, S.; Tombelli, S.; Minunni, M.; Mascini, M. Aptamer-based detection of plasma proteins by an electrochemical assay coupled to magnetic beads. Anal. Chem. 2007, 79, 1466–1473.
    • (2007) Anal. Chem , vol.79 , pp. 1466-1473
    • Centi, S.1    Tombelli, S.2    Minunni, M.3    Mascini, M.4
  • 77
    • 0033911295 scopus 로고    scopus 로고
    • Methods for reducing biosensor membrane biofouling. Colloids Surf
    • Wisniewski, N.; Reichert, M. Methods for reducing biosensor membrane biofouling. Colloids Surf. B Biointerfaces 2000, 18, 197–219.
    • (2000) B Biointerfaces , vol.18 , pp. 197-219
    • Wisniewski, N.1    Reichert, M.2
  • 78
    • 33748956288 scopus 로고    scopus 로고
    • Electrode passivation caused by polymerization of different phenolic compounds
    • Ferreira, M.; Varela, H.; Torresi, R.M.; Tremiliosi-Filho, G. Electrode passivation caused by polymerization of different phenolic compounds. Electrochim. Acta 2006, 52, 434–442.
    • (2006) Electrochim. Acta , vol.52 , pp. 434-442
    • Ferreira, M.1    Varela, H.2    Torresi, R.M.3    Tremiliosi-Filho, G.4
  • 79
    • 84875168832 scopus 로고    scopus 로고
    • Modeling analysis of electrode fouling during electrolysis of phenolic compounds
    • Yang, X.; Kirsch, J.; Fergus, J.; Simonian, A. Modeling analysis of electrode fouling during electrolysis of phenolic compounds. Electrochim. Acta 2013, 94, 259–268.
    • (2013) Electrochim. Acta , vol.94 , pp. 259-268
    • Yang, X.1    Kirsch, J.2    Fergus, J.3    Simonian, A.4
  • 81
    • 33748959956 scopus 로고    scopus 로고
    • Biosensors and Sensor Systems
    • Springer: New York, NY, USA
    • O’Hare, D. Biosensors and Sensor Systems. In Body Sensor Networks; Springer: New York, NY, USA, 2014.
    • (2014) Body Sensor Networks
    • O’Hare, D.1
  • 83
    • 84940469878 scopus 로고    scopus 로고
    • Amperometric Glucose Sensors for Whole Blood Measurement Based on Dehydrogenase Enzymes
    • Canuto, R.A., Ed.; InTech: Rijeka, Croatia
    • Cardosi, M.; Liu, Z. Amperometric Glucose Sensors for Whole Blood Measurement Based on Dehydrogenase Enzymes. In Dehydrogenases; Canuto, R.A., Ed.; InTech: Rijeka, Croatia, 2012.
    • (2012) Dehydrogenases
    • Cardosi, M.1    Liu, Z.2
  • 85
    • 1942523437 scopus 로고    scopus 로고
    • Construction and application of highly selectively sensors and biosensors using non-conducting electropolymerized films
    • Rome, Italy, 18–19 March
    • Curulli, A.; Palleschi, G. Construction and application of highly selectively sensors and biosensors using non-conducting electropolymerized films. In Proceedings of the 2ndWorkshop on Chemical Sensors and Biosensors, Rome, Italy, 18–19 March 2000.
    • (2000) Proceedings of the 2Ndworkshop on Chemical Sensors and Biosensors
    • Curulli, A.1    Palleschi, G.2
  • 86
    • 0037178188 scopus 로고    scopus 로고
    • Enhancement of operational stability of an enzyme biosensor for glucose and sucrose using protein based stabilizing agent
    • Gouda, M.D.; Kumar, M.A.; Thakur, M.S.; Karantha, N.G. Enhancement of operational stability of an enzyme biosensor for glucose and sucrose using protein based stabilizing agent. Biosens. Bioelectron. 2002, 17, 503–507.
    • (2002) Biosens. Bioelectron , vol.17 , pp. 503-507
    • Gouda, M.D.1    Kumar, M.A.2    Thakur, M.S.3    Karantha, N.G.4
  • 87
    • 0032751027 scopus 로고    scopus 로고
    • Biosensors: The stabilité problem
    • Gibson, T.D. Biosensors: The stabilité problem. Analusis 1999, 27, 630–638.
    • (1999) Analusis , vol.27 , pp. 630-638
    • Gibson, T.D.1
  • 88
    • 4143054917 scopus 로고    scopus 로고
    • Enzyme stabilization strategies based on electrolytes and polyelectrolytes for biosensor applications
    • Chaniotakis, N.A. Enzyme stabilization strategies based on electrolytes and polyelectrolytes for biosensor applications. Anal. Bioanal. Chem. 2004, 378, 89–95.
    • (2004) Anal. Bioanal. Chem , vol.378 , pp. 89-95
    • Chaniotakis, N.A.1
  • 89
    • 84857501859 scopus 로고    scopus 로고
    • Immobilization strategies to develop enzymatic biosensors
    • Sassolas, A.; Blum, L.J.; Leca-Bouvier, B.D. Immobilization strategies to develop enzymatic biosensors. Biotechnol. Adv. 2012, 30, 489–511.
    • (2012) Biotechnol. Adv , vol.30 , pp. 489-511
    • Sassolas, A.1    Blum, L.J.2    Leca-Bouvier, B.D.3
  • 91
    • 84904793107 scopus 로고    scopus 로고
    • Immobilization as a Strategy for Improving Enzyme Properties-Application to Oxidoreductases
    • Guzik, U.; Hupert-Kocurek, K.; Wojcieszy ´ nska, D. Immobilization as a Strategy for Improving Enzyme Properties-Application to Oxidoreductases. Molecules 2014, 19, 8995–9018.
    • (2014) Molecules , vol.19 , pp. 8995-9018
    • Guzik, U.1    Hupert-Kocurek, K.2    Wojcieszy, ´.3    Nska, D.4
  • 92
    • 79951639658 scopus 로고    scopus 로고
    • Enzyme-immobilized nanofiltration membrane to mitigate biofouling based on quorum quenching
    • Kim, J.H.; Choi, D.C.; Yeon, K.M.; Kim, S.R.; Lee, C.H. Enzyme-immobilized nanofiltration membrane to mitigate biofouling based on quorum quenching. Environ. Sci. Technol. 2011, 45, 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
  • 93
    • 38749101357 scopus 로고    scopus 로고
    • Recent advances in cholesterol biosensor. Biosens
    • Arya, S.K.; Datta, M.; Malhotra, B.D. Recent advances in cholesterol biosensor. Biosens. Bioelectron. 2008, 23, 1083–1100.
    • (2008) Bioelectron , vol.23 , pp. 1083-1100
    • Arya, S.K.1    Datta, M.2    Malhotra, B.D.3
  • 94
    • 32644444408 scopus 로고    scopus 로고
    • Twenty years research in cholinesterase biosensors: From basic research to practical applications
    • Andreescu, S.; Marty, J.L. Twenty years research in cholinesterase biosensors: from basic research to practical applications. Biomol. Eng. 2006, 23, 1–15.
    • (2006) Biomol. Eng , vol.23 , pp. 1-15
    • Andreescu, S.1    Marty, J.L.2
  • 95
    • 12144255029 scopus 로고    scopus 로고
    • Progress in enzyme-based biosensors using optical transducers
    • Choi, M.F.M. Progress in enzyme-based biosensors using optical transducers. Microchim. Acta 2004, 148, 107–132.
    • (2004) Microchim. Acta , vol.148 , pp. 107-132
    • Choi, M.F.M.1
  • 96
    • 84971666369 scopus 로고    scopus 로고
    • Protective membranes at electrochemical biosensors
    • Ambrozy, A.; Hlavata, L.; Labuda, J. Protective membranes at electrochemical biosensors. Acta Chim. Slovaca 2013, 6, 35–41.
    • (2013) Acta Chim. Slovaca , vol.6 , pp. 35-41
    • Ambrozy, A.1    Hlavata, L.2    Labuda, J.3
  • 97
    • 0037201686 scopus 로고    scopus 로고
    • Characterization in vitro and in vivo of the oxygen dependence of an enzyme/polymer biosensor for monitoring brain glucose
    • Dixon, B.M.; Lowry, J.P.; O’Neill, R.D. Characterization in vitro and in vivo of the oxygen dependence of an enzyme/polymer biosensor for monitoring brain glucose. J. Neurosci. Methods 2002, 119, 135–142.
    • (2002) J. Neurosci. Methods , vol.119 , pp. 135-142
    • Dixon, B.M.1    Lowry, J.P.2    O’Neill, R.D.3
  • 98
    • 77957143584 scopus 로고    scopus 로고
    • Enzyme immobilization strategies and electropolymerization conditions to control sensitivity and selectivity parameters of a polymer-enzyme composite glucose biosensor
    • Rothwell, S.A.; Killoran, S.J.; O’Neill, R.D. Enzyme immobilization strategies and electropolymerization conditions to control sensitivity and selectivity parameters of a polymer-enzyme composite glucose biosensor. Sensors 2010, 10, 6439–6462.
    • (2010) Sensors , vol.10 , pp. 6439-6462
    • Rothwell, S.A.1    Killoran, S.J.2    O’Neill, R.D.3
  • 99
    • 0035920531 scopus 로고    scopus 로고
    • Encapsulation of biomolecules in silica gels
    • Livage, J.; Coradin, T.; Roux, C. Encapsulation of biomolecules in silica gels. J. Phys. Condens. Matter. 2001, 13, 673–691.
    • (2001) J. Phys. Condens. Matter , vol.13 , pp. 673-691
    • Livage, J.1    Coradin, T.2    Roux, C.3
  • 100
    • 0034099693 scopus 로고    scopus 로고
    • Entrapment of lipases in hydrophobic sol-gel materials: Efficient heterogenous biocatalysts in aqueous medium
    • Reetz, M.T.; Wenkel, R.; Avnir, D. Entrapment of lipases in hydrophobic sol-gel materials: Efficient heterogenous biocatalysts in aqueous medium. Synthesis 2000, 6, 781–783.
    • (2000) Synthesis , vol.6 , pp. 781-783
    • Reetz, M.T.1    Wenkel, R.2    Avnir, D.3
  • 102
    • 33751158445 scopus 로고
    • Enzymes and other proteins entrapped in sol-gel materials
    • Avnir, D.; Braun, S.; Lev, O.; Ottolenghi, M. Enzymes and other proteins entrapped in sol-gel materials. Chem. Mater. 1994, 6, 1605–1614.
    • (1994) Chem. Mater , vol.6 , pp. 1605-1614
    • Avnir, D.1    Braun, S.2    Lev, O.3    Ottolenghi, M.4
  • 103
    • 84989779767 scopus 로고    scopus 로고
    • Diamond nanoparticles as a way to improve electron transfer in sol-gel L-lactate biosensing platforms
    • Briones, M.; Casero, E.; Vázquez, L.; Pariente, F.; Lorenzo, E.; Petit-Domínguez, M.D. Diamond nanoparticles as a way to improve electron transfer in sol-gel L-lactate biosensing platforms. Anal. Chim. Acta 2016, 908, 141–149.
    • (2016) Anal. Chim. Acta , vol.908 , pp. 141-149
    • Briones, M.1    Casero, E.2    Vázquez, L.3    Pariente, F.4    Lorenzo, E.5    Petit-Domínguez, M.D.6
  • 105
  • 106
    • 84898028467 scopus 로고    scopus 로고
    • Polymers in Biosensors
    • Woodhead Publishing: Cambridge, UK
    • Davis, F.; Higson, S. Polymers in Biosensors. In Biomedical Polymers; Woodhead Publishing: Cambridge, UK, 2007.
    • (2007) Biomedical Polymers
    • Davis, F.1    Higson, S.2
  • 107
    • 29744459306 scopus 로고    scopus 로고
    • Eliminating the Interference of Ascorbic Acid and Uric Acid to the Amperometric Glucose Biosensor by Cation Exchangers Membrane and Size Exclusion Membrane
    • Yuan, C.J.; Hsu, C.L.; Wang, S.C.; Changb, K.S. Eliminating the Interference of Ascorbic Acid and Uric Acid to the Amperometric Glucose Biosensor by Cation Exchangers Membrane and Size Exclusion Membrane. Electroanalysis 2005, 17, 2239–2245.
    • (2005) Electroanalysis , vol.17 , pp. 2239-2245
    • Yuan, C.J.1    Hsu, C.L.2    Wang, S.C.3    Changb, K.S.4
  • 108
    • 84873706177 scopus 로고    scopus 로고
    • Development of an amperometric screen-printed galactose biosensor for serum analysis
    • Kanyong, P.; Pemberton, R.M.; Jackson, S.K.; Hart, J.P. Development of an amperometric screen-printed galactose biosensor for serum analysis. Anal. Biochem. 2013, 435, 114–119.
    • (2013) Anal. Biochem , vol.435 , pp. 114-119
    • Kanyong, P.1    Pemberton, R.M.2    Jackson, S.K.3    Hart, J.P.4
  • 110
    • 0022476714 scopus 로고
    • Permeability of small nonelectrolytes through lipid bilayer membranes
    • Walter, A.; Gutknecht, J. Permeability of small nonelectrolytes through lipid bilayer membranes. J. Membr. Biol. 1986, 90, 207–217.
    • (1986) J. Membr. Biol , vol.90 , pp. 207-217
    • Walter, A.1    Gutknecht, J.2
  • 111
    • 66149114037 scopus 로고    scopus 로고
    • Contributions by a novel edge effect to the permselectivity of an electrosynthesized polymer for microbiosensor applications
    • Rothwell, S.A.; Kinsella, M.E.; Zain, Z.M.; Serra, P.A.; Rocchitta, G.; Lowry, J.P.; O’Neill, R.D. Contributions by a novel edge effect to the permselectivity of an electrosynthesized polymer for microbiosensor applications. Anal. Chem. 2009, 81, 3911–3918.
    • (2009) Anal. Chem , vol.81 , pp. 3911-3918
    • Rothwell, S.A.1    Kinsella, M.E.2    Zain, Z.M.3    Serra, P.A.4    Rocchitta, G.5    Lowry, J.P.6    O’Neill, R.D.7
  • 113
    • 84868232085 scopus 로고    scopus 로고
    • Theoretical Analysis of the Performance of Glucose Sensors with Layer-by-Layer Assembled Outer Membranes
    • Croce, R.A.; Vaddiraju, S.; Papadimitrakopoulos, F.; Jain, F.C. Theoretical Analysis of the Performance of Glucose Sensors with Layer-by-Layer Assembled Outer Membranes. Sensors 2012, 12, 13402–13416.
    • (2012) Sensors , vol.12 , pp. 13402-13416
    • Croce, R.A.1    Vaddiraju, S.2    Papadimitrakopoulos, F.3    Jain, F.C.4
  • 114
    • 79952646558 scopus 로고    scopus 로고
    • Effects of applied potential on the mass of non-conducting poly(Ortho-phenylenediamine) electro-deposited on EQCM electrodes: Comparison with biosensor selectivity parameters
    • Rothwell, S.A.; O’Neill, R.D. Effects of applied potential on the mass of non-conducting poly(ortho-phenylenediamine) electro-deposited on EQCM electrodes: comparison with biosensor selectivity parameters. Phys. Chem. Chem. Phys. 2011, 13, 5413–5421.
    • (2011) Phys. Chem. Chem. Phys , vol.13 , pp. 5413-5421
    • Rothwell, S.A.1    O’Neill, R.D.2
  • 116
    • 6344285504 scopus 로고    scopus 로고
    • The selectivity of electrosynthesised polymer membranes depends on the electrode dimensions: Implications for biosensor applications
    • McMahon, C.P.; Killoran, S.J.; Kirwan, S.M.; O’Neill, R.D. The selectivity of electrosynthesised polymer membranes depends on the electrode dimensions: Implications for biosensor applications. Chem. Commun. 2004, 18, 2128–2130.
    • (2004) Chem. Commun , vol.18 , pp. 2128-2130
    • McMahon, C.P.1    Killoran, S.J.2    Kirwan, S.M.3    O’Neill, R.D.4
  • 118
    • 84958962718 scopus 로고    scopus 로고
    • A novel DNA biosensor integrated with Polypyrrole/streptavidin and Au-PAMAM-CP bionanocomposite probes to detect the rs4839469 locus of the vangl1 gene for dysontogenesis prediction
    • Li, Q.; Yu, C.; Gao, R.; Xia, C.; Yuan, G.; Li, Y.; Zhao, Y.; Chen, Q.; He, J. A novel DNA biosensor integrated with Polypyrrole/streptavidin and Au-PAMAM-CP bionanocomposite probes to detect the rs4839469 locus of the vangl1 gene for dysontogenesis prediction. Biosens. Bioelectron. 2016, 80, 674–681.
    • (2016) Biosens. Bioelectron , vol.80 , pp. 674-681
    • Li, Q.1    Yu, C.2    Gao, R.3    Xia, C.4    Yuan, G.5    Li, Y.6    Zhao, Y.7    Chen, Q.8    He, J.9
  • 119
    • 84947080804 scopus 로고    scopus 로고
    • Rapid amperometric detection of trace metals by inhibition of an ultrathin polypyrrole-based glucose biosensor
    • Ayenimo, J.G.; Adeloju, S.B. Rapid amperometric detection of trace metals by inhibition of an ultrathin polypyrrole-based glucose biosensor. Talanta 2016, 148, 502–510.
    • (2016) Talanta , vol.148 , pp. 502-510
    • Ayenimo, J.G.1    Adeloju, S.B.2
  • 120
    • 84930940370 scopus 로고    scopus 로고
    • Improvement in glucose biosensing response of electrochemically grown polypyrrole nanotubes by incorporating crosslinked glucose oxidase
    • Palod, P.A.; Singh, V. Improvement in glucose biosensing response of electrochemically grown polypyrrole nanotubes by incorporating crosslinked glucose oxidase. Mater. Sci. Eng. C Mater. Biol. Appl. 2015, 55, 420–430.
    • (2015) Mater. Sci. Eng. C Mater. Biol. Appl , vol.55 , pp. 420-430
    • Palod, P.A.1    Singh, V.2
  • 121
    • 84961286979 scopus 로고    scopus 로고
    • An intimately bonded titanate nanotube-polyaniline-gold nanoparticle ternary composite as a scaffold for electrochemical enzyme biosensors
    • Liu, X.; Zhu, J.; Huo, X.; Yan, R.; Wong, D.K. An intimately bonded titanate nanotube-polyaniline-gold nanoparticle ternary composite as a scaffold for electrochemical enzyme biosensors. Anal. Chim. Acta 2016, 911, 59–68.
    • (2016) Anal. Chim. Acta , vol.911 , pp. 59-68
    • Liu, X.1    Zhu, J.2    Huo, X.3    Yan, R.4    Wong, D.K.5
  • 122
    • 84947418126 scopus 로고    scopus 로고
    • Amperometric urea biosensors based on sulfonated graphene/polyaniline nanocomposite
    • Das, G.; Yoon, H.H. Amperometric urea biosensors based on sulfonated graphene/polyaniline nanocomposite. Int. J. Nanomed. 2015, 10, 55–66.
    • (2015) Int. J. Nanomed , vol.10 , pp. 55-66
    • Das, G.1    Yoon, H.H.2
  • 123
    • 84961616402 scopus 로고    scopus 로고
    • Highly sensitive biosensor for tumor maker alpha fetoprotein based on poly(Ethylene glycol) doped conducting polymer PEDOT
    • Cui, M.; Song, Z.; Wu, Y.; Guo, B.; Fan, X.; Luo, X. A highly sensitive biosensor for tumor maker alpha fetoprotein based on poly(ethylene glycol) doped conducting polymer PEDOT. Biosens. Bioelectron. 2016, 79, 736–741.
    • (2016) Biosens. Bioelectron , vol.79 , pp. 736-741
    • Cui, M.1    Song, Z.2    Wu, Y.3    Guo, B.4    Fan, X.5    Luo, X.A.6
  • 125
    • 0036125073 scopus 로고    scopus 로고
    • Application of conducting polymers to biosensors. Biosens
    • Gerard, M.; Chaubey, A.; Malhotra, B.D. Application of conducting polymers to biosensors. Biosens. Bioelectron. 2002, 17, 345–359.
    • (2002) Bioelectron , vol.17 , pp. 345-359
    • Gerard, M.1    Chaubey, A.2    Malhotra, B.D.3
  • 127
    • 0032977013 scopus 로고    scopus 로고
    • Molecularly imprinted polymers for biosensor applications
    • Yano, K.; Karube, I. Molecularly imprinted polymers for biosensor applications. TrAC Trends Anal. Chem. 1999, 18, 199–204.
    • (1999) Trac Trends Anal. Chem , vol.18 , pp. 199-204
    • Yano, K.1    Karube, I.2
  • 128
    • 0032211544 scopus 로고    scopus 로고
    • Improved operational stability of biosensors based on enzyme-polyelectrolyte complex adsorbed into a porous carbon electrode
    • Gavalas, V.G.; Chaniotakis, N.A.; Gibson, T.D. Improved operational stability of biosensors based on enzyme-polyelectrolyte complex adsorbed into a porous carbon electrode. Biosens. Bioelectron. 1998, 13, 1205–1211.
    • (1998) Biosens. Bioelectron , vol.13 , pp. 1205-1211
    • Gavalas, V.G.1    Chaniotakis, N.A.2    Gibson, T.D.3
  • 129
    • 0000785936 scopus 로고
    • Stabilization of analytical enzymes using a novel polymer-carbonate system and the production of a stabilized, single reagent for alcohol analysis
    • Gibson, T.D.; Higgins, I.J.; Woodward, J.R. Stabilization of analytical enzymes using a novel polymer-carbonate system and the production of a stabilized, single reagent for alcohol analysis. Analyst 1992, 117, 1293–1297.
    • (1992) Analyst , vol.117 , pp. 1293-1297
    • Gibson, T.D.1    Higgins, I.J.2    Woodward, J.R.3
  • 130
    • 42649120099 scopus 로고    scopus 로고
    • Physical immobilization of laccase on an electrode by means of poly(Ethyleneimine) microcapsules
    • Rochefort, D.; Kouisni, L.; Gendron, K. Physical immobilization of laccase on an electrode by means of poly(ethyleneimine) microcapsules. J. Electroanal. Chem. 2008, 217, 53–63.
    • (2008) J. Electroanal. Chem , vol.217 , pp. 53-63
    • Rochefort, D.1    Kouisni, L.2    Gendron, K.3
  • 132
    • 33846341424 scopus 로고    scopus 로고
    • Oxygen tolerance of an implantable polymer/enzyme composite glutamate biosensor displaying polycation-enhanced substrate sensitivity
    • McMahon, C.P.; Rocchitta, G.; Kirwan, S.M.; Killoran, S.J.; Serra, P.A.; Lowry, J.P.; O’Neill, R.D. Oxygen tolerance of an implantable polymer/enzyme composite glutamate biosensor displaying polycation-enhanced substrate sensitivity. Biosens. Bioelectron. 2007, 22, 1466–1473.
    • (2007) Biosens. Bioelectron , vol.22 , pp. 1466-1473
    • McMahon, C.P.1    Rocchitta, G.2    Kirwan, S.M.3    Killoran, S.J.4    Serra, P.A.5    Lowry, J.P.6    O’Neill, R.D.7
  • 133
    • 0141760588 scopus 로고    scopus 로고
    • Evaluation of Polycation-Stabilized Lactate Oxidase in a Silica Sol–Gel as a Biosensor Platform
    • Cox, J.A.; Hensley, P.M.; Loch, C.L. Evaluation of Polycation-Stabilized Lactate Oxidase in a Silica Sol–Gel as a Biosensor Platform. Microchim. Acta 2003, 142, 1–5.
    • (2003) Microchim.Acta , vol.142 , pp. 1-5
    • Cox, J.A.1    Hensley, P.M.2    Loch, C.L.3
  • 134
    • 0015402739 scopus 로고
    • Glycerol as an Enzyme-Stabilizing Agent: Effects on Aldehyde Dehydrogenase
    • Bradbury, S.L.; Jakoby, W.B. Glycerol as an Enzyme-Stabilizing Agent: Effects on Aldehyde Dehydrogenase. Proc. Nat. Acad. Sci. USA 1972, 69, 2373–2376.
    • (1972) Proc. Nat. Acad. Sci. USA , vol.69 , pp. 2373-2376
    • Bradbury, S.L.1    Jakoby, W.B.2
  • 138
    • 0035916228 scopus 로고    scopus 로고
    • Monovalent Cation-Induced Conformational Change in Glucose Oxidase Leading to Stabilization of the Enzyme
    • Atta, A.; Akhtar, M.S.; Bhakuni, V. Monovalent Cation-Induced Conformational Change in Glucose Oxidase Leading to Stabilization of the Enzyme. Biochemistry 2001, 40, 1945–1955.
    • (2001) Biochemistry , vol.40 , pp. 1945-1955
    • Atta, A.1    Akhtar, M.S.2    Bhakuni, V.3
  • 140
    • 0000707017 scopus 로고
    • Electropolymerized 1,2-diaminobenzene as a means to prevent interferences and fouling and to stabilize immobilized enzyme in electrochemical biosensors
    • Sasso, S.V.; Pierce, R.J.; Walla, R.; Yacynych, A.M. Electropolymerized 1,2-diaminobenzene as a means to prevent interferences and fouling and to stabilize immobilized enzyme in electrochemical biosensors. Anal. Chem. 1990, 62, 1111–1117.
    • (1990) Anal. Chem , vol.62 , pp. 1111-1117
    • Sasso, S.V.1    Pierce, R.J.2    Walla, R.3    Yacynych, A.M.4
  • 141
    • 0025762538 scopus 로고
    • Electropolymerized films to prevent interferences and electrode fouling in biosensors
    • Geise, R.J.; Adams, J.M.; Barone, N.J.; Yacynych, A.M. Electropolymerized films to prevent interferences and electrode fouling in biosensors. Biosens. Bioelectron. 1991, 6, 151–160.
    • (1991) Biosens. Bioelectron , vol.6 , pp. 151-160
    • Geise, R.J.1    Adams, J.M.2    Barone, N.J.3    Yacynych, A.M.4
  • 142
    • 0035257183 scopus 로고    scopus 로고
    • A review of saliva: Normal composition, flow, and function
    • Humphrey, S.P.; Williamson, R.T.J. A review of saliva: Normal composition, flow, and function. Prosthet. Dent. 2001, 85, 162–169.
    • (2001) Prosthet. Dent , vol.85 , pp. 162-169
    • Humphrey, S.P.1    Williamson, R.T.J.2
  • 143
    • 0032078428 scopus 로고    scopus 로고
    • Noninvasively measuring blood glucose using saliva: A bloodless procedure based on an enzyme-sensor system
    • Yamaguchi, M.; Mitsumori, M.; Kano, Y. Noninvasively measuring blood glucose using saliva: A bloodless procedure based on an enzyme-sensor system. IEEE Eng. Med. Biol. 1998, 17, 59–63.
    • (1998) IEEE Eng. Med. Biol , vol.17 , pp. 59-63
    • Yamaguchi, M.1    Mitsumori, M.2    Kano, Y.3
  • 145
    • 79960007409 scopus 로고    scopus 로고
    • Human a-amylase and starch digestion: An interesting marriage
    • Butterworth, P.J.;Warren, F.J.; Ellis, P.R. Human a-amylase and starch digestion: An interesting marriage. Starch Starke 2011, 63, 395–405.
    • (2011) Starch Starke , vol.63 , pp. 395-405
    • Butterworth, P.J.1    Warren, F.J.2    Ellis, P.R.3
  • 146
    • 84971666088 scopus 로고    scopus 로고
    • Biochemical Composition of Normal Urine
    • Baig, A. Biochemical Composition of Normal Urine. Nat. Precedings 2011.
    • (2011) Nat. Precedings
    • Baig, A.1
  • 147
    • 84971650386 scopus 로고    scopus 로고
    • (accessed on 29 February 2016)
    • Blood, Plasma, and Cellular Blood Components. Available online: http://www.usp.org/sites/default/files/ usp_pdf/EN/USPNF/chapter5.pdf (accessed on 29 February 2016).
  • 148
    • 0002160273 scopus 로고
    • Brain Dialysis of Monoamines
    • Robinson, T.E., Justice, J.B., Eds.; Elsevier: Amsterdam, The Netherlands
    • Di Chiara, G. Brain Dialysis of Monoamines. In Microdialysis in the Neurosciences; Robinson, T.E., Justice, J.B., Eds.; Elsevier: Amsterdam, The Netherlands, 1991.
    • (1991) Microdialysis in the Neurosciences
    • Di Chiara, G.1
  • 149
    • 0028277744 scopus 로고
    • Microvoltammetric techniques and sensors for monitoring neurochemical dynamics in vivo
    • O’Neill, R.D. Microvoltammetric techniques and sensors for monitoring neurochemical dynamics in vivo. A review. Analyst 1994, 119, 767–779.
    • (1994) A Review. Analyst , vol.119 , pp. 767-779
    • O’Neill, R.D.1
  • 152
    • 84903580004 scopus 로고    scopus 로고
    • Non-invasive wearable electrochemical sensors: A review
    • Bandodkar, A.J.; Wang, J. Non-invasive wearable electrochemical sensors: A review. Trends Biotechnol. 2014, 32, 363–371.
    • (2014) Trends Biotechnol , vol.32 , pp. 363-371
    • Bandodkar, A.J.1    Wang, J.2
  • 153
    • 0000606171 scopus 로고
    • Chemical Composition of Sweat
    • Robinson, S.; Robinson, A.H. Chemical Composition of Sweat. Physiol. Rev. 1954, 34, 202–220.
    • (1954) Physiol. Rev , vol.34 , pp. 202-220
    • Robinson, S.1    Robinson, A.H.2
  • 154
    • 80053605315 scopus 로고    scopus 로고
    • Evaluation of striatal oxidative stress in patients with Parkinson’s disease using [62Cu] ATSM PET
    • Ikawa, M.; Okazawa, H.; Kudo, T.; Kuriyama, M.; Fujibayashi, Y.; Yoneda, M. Evaluation of striatal oxidative stress in patients with Parkinson’s disease using [62Cu] ATSM PET. Nuclear Med. Biol. 2011, 38, 945–951.
    • (2011) Nuclear Med. Biol , vol.38 , pp. 945-951
    • Ikawa, M.1    Okazawa, H.2    Kudo, T.3    Kuriyama, M.4    Fujibayashi, Y.5    Yoneda, M.6
  • 157
    • 71749119260 scopus 로고    scopus 로고
    • Emerging roles of mitochondrial proteases in neurodegeneration
    • Martinelli, P.; Rugarli, E.I. Emerging roles of mitochondrial proteases in neurodegeneration. Biochim. Biophys. Acta 2010, 1197, 1–10.
    • (2010) Biochim. Biophys. Acta , vol.1197 , pp. 1-10
    • Martinelli, P.1    Rugarli, E.I.2
  • 158
    • 77954663588 scopus 로고    scopus 로고
    • Mast cell proteases: Multifaceted regulators of inflammatory disease
    • Pejler, G.; Ronnberg, E.; Waern, I.; Wernersson, S. Mast cell proteases: Multifaceted regulators of inflammatory disease. Blood 2010, 115, 4981–4990.
    • (2010) Blood , vol.115 , pp. 4981-4990
    • Pejler, G.1    Ronnberg, E.2    Waern, I.3    Wernersson, S.4
  • 160
    • 84957543969 scopus 로고    scopus 로고
    • Neutrophil-Derived Proteases in the Microenvironment of Pancreatic Cancer—Active Players in Tumor Progression
    • Felix, K.; Gaida, M.M. Neutrophil-Derived Proteases in the Microenvironment of Pancreatic Cancer—Active Players in Tumor Progression. Int. J. Biol. Sci. 2016, 12, 302–313.
    • (2016) Int. J. Biol. Sci , vol.12 , pp. 302-313
    • Felix, K.1    Gaida, M.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.