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Volumn , Issue , 2007, Pages 441-459

Hydrogen peroxide producing and decomposing enzymes: Their use in biosensors and other applications

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EID: 84892322092     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/1-4020-5377-0_25     Document Type: Chapter
Times cited : (12)

References (131)
  • 1
    • 0001677927 scopus 로고    scopus 로고
    • Multi-enzyme biosensors with amperometric detection of lactose in milk and dairy products
    • Adányi, N., Szabó, E.E. and Váradi, M. (1999) Multi-enzyme biosensors with amperometric detection of lactose in milk and dairy products. Z. Lebensm. Unters.-Forsch. A. 209, 220-226.
    • (1999) Z. Lebensm. Unters.-Forsch. A. , vol.209 , pp. 220-226
    • Adányi, N.1    Szabó, E.E.2    Váradi, M.3
  • 2
    • 21144434378 scopus 로고    scopus 로고
    • Catalase-based thin-layer enzyme cell used in organic-phase FIA system for determination of moisture in oily foods
    • Adányi, N. and Váradi, M. (2004) Catalase-based thin-layer enzyme cell used in organic-phase FIA system for determination of moisture in oily foods. Eur. Food Res. Technol. 219, 432-437.
    • (2004) Eur. Food Res. Technol. , vol.219 , pp. 432-437
    • Adányi, N.1    Váradi, M.2
  • 3
    • 51249162824 scopus 로고
    • Characterization of immobilized catalases and their application in pasteurization of milk with H2O2
    • Akertek, E. and Tarhan, L. (1995) Characterization of immobilized catalases and their application in pasteurization of milk with H2O2. Appl. Biochem. Biotech. 50, 291-303.
    • (1995) Appl. Biochem. Biotech. , vol.50 , pp. 291-303
    • Akertek, E.1    Tarhan, L.2
  • 5
    • 0040671751 scopus 로고    scopus 로고
    • The application of catalase for the elimination of hydrogen peroxide residues after bleaching of cotton fabrics
    • Amorim, A.M., Gasques, M.D.G., Andreaus, J. and Scharf, M. (2002) The application of catalase for the elimination of hydrogen peroxide residues after bleaching of cotton fabrics. Anais Acad. Brasil. Cièncias 74, 433-435.
    • (2002) Anais Acad. Brasil. Cièncias , vol.74 , pp. 433-435
    • Amorim, A.M.1    Gasques, M.D.G.2    Andreaus, J.3    Scharf, M.4
  • 6
    • 19044370237 scopus 로고    scopus 로고
    • Determination of total cholesterol content in food by flow injection analysis with immobilized cholesterol oxidase enzyme reactor
    • Baticz, O. and Tömösközi, S. (2002) Determination of total cholesterol content in food by flow injection analysis with immobilized cholesterol oxidase enzyme reactor. Nahrung 46, 46-50.
    • (2002) Nahrung , vol.46 , pp. 46-50
    • Baticz, O.1    Tömösközi, S.2
  • 7
    • 0346504026 scopus 로고    scopus 로고
    • Towards the development of an integrated capillary electrophoresis optical biosensor
    • Bossi, A., Castelletti, L., Piletsky, S.A. and Righetti, P.G. (2003) Towards the development of an integrated capillary electrophoresis optical biosensor. Electrophoresis 24, 3356-3363.
    • (2003) Electrophoresis , vol.24 , pp. 3356-3363
    • Bossi, A.1    Castelletti, L.2    Piletsky, S.A.3    Righetti, P.G.4
  • 8
    • 4243485130 scopus 로고
    • New insights into the enzymic catalysis of the oxidation of glucose by native and recombinant glucose oxidase mediated by electrochemically generated one-electron redox cosubstrates
    • Bourdillon, C., Demaille, C., Moiroux, J. and Saveant, J.M. (1993) New insights into the enzymic catalysis of the oxidation of glucose by native and recombinant glucose oxidase mediated by electrochemically generated one-electron redox cosubstrates. J. Am. Chem. Soc. 115, 1-10.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 1-10
    • Bourdillon, C.1    Demaille, C.2    Moiroux, J.3    Saveant, J.M.4
  • 9
    • 0023647271 scopus 로고
    • The reactivity of galactose oxidase with snail galactans, galactosides and D-galactose-composed oligosaccharides
    • Bretting, H. and Jacobs, G. (1987) The reactivity of galactose oxidase with snail galactans, galactosides and D-galactose-composed oligosaccharides. Biochim. Biophys. Acta. 913, 342-348.
    • (1987) Biochim. Biophys. Acta. , vol.913 , pp. 342-348
    • Bretting, H.1    Jacobs, G.2
  • 10
    • 0034247984 scopus 로고    scopus 로고
    • A new tool for superoxide and nitric oxide radicals determination using suitable enzymatic sensors
    • Campanella, L., Persi, L. and Tomassetti M. (2000) A new tool for superoxide and nitric oxide radicals determination using suitable enzymatic sensors. Sensor. Actuat. B-Chem. 68, 351-359.
    • (2000) Sensor. Actuat. B-Chem. , vol.68 , pp. 351-359
    • Campanella, L.1    Persi, L.2    Tomassetti, M.3
  • 11
    • 0035369574 scopus 로고    scopus 로고
    • Hydroperoxide determination by a catalase OPEE: Application to the study of extra virgin olive oil rancidification process
    • Campanella, L., Sammartino, M.P., Tomassetti, M. and Zannella S., (2001) Hydroperoxide determination by a catalase OPEE: application to the study of extra virgin olive oil rancidification process. Sensor. Actuat. B-Chem. 76, 158-165.
    • (2001) Sensor. Actuat. B-Chem. , vol.76 , pp. 158-165
    • Campanella, L.1    Sammartino, M.P.2    Tomassetti, M.3    Zannella, S.4
  • 12
    • 0034342166 scopus 로고    scopus 로고
    • Effects of high hydrostatic pressure processing and of glucose oxidase-catalase addition on the color stability and sensorial score of grape juice
    • Castellari, M., Matricardi, L., Arfelli, G., Carpi, G. and Galassi, S. (2000) Effects of high hydrostatic pressure processing and of glucose oxidase-catalase addition on the color stability and sensorial score of grape juice. Food Sci.Technol. Int. 6, 17-23.
    • (2000) Food Sci.Technol. Int. , vol.6 , pp. 17-23
    • Castellari, M.1    Matricardi, L.2    Arfelli, G.3    Carpi, G.4    Galassi, S.5
  • 13
    • 0017786127 scopus 로고
    • One and two electron transfer reactions of glucose oxidase
    • Chan, T.W. and Bruice, T.C. (1977) One and two electron transfer reactions of glucose oxidase. J. Am. Chem. Soc. 99, 2387-2389.
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 2387-2389
    • Chan, T.W.1    Bruice, T.C.2
  • 14
    • 0019973014 scopus 로고
    • The characterization and interconversion of three forms of cholesterol oxidase extracted from Nocardia rhodochrous
    • Cheetham, P.S., Dunnill, P. and Lilly, M.D. (1982) The characterization and interconversion of three forms of cholesterol oxidase extracted from Nocardia rhodochrous. Biochem. J. 201, 515-521.
    • (1982) Biochem. J. , vol.201 , pp. 515-521
    • Cheetham, P.S.1    Dunnill, P.2    Lilly, M.D.3
  • 15
    • 0842309140 scopus 로고    scopus 로고
    • Diversity of structures and properties among catalases
    • Chelikani, P., Fita, I. and Loewen, P.C. (2004) Diversity of structures and properties among catalases. Cell. Mol. Life Sci. 61, 192-208.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 192-208
    • Chelikani, P.1    Fita, I.2    Loewen, P.C.3
  • 16
    • 54749121269 scopus 로고    scopus 로고
    • Interactive effects of flour, starter and enzyme on bread dough machinability
    • Collar, C., Andreu, P. and Martinez-Anaya, M.A. (1998) Interactive effects of flour, starter and enzyme on bread dough machinability. Z. Lebensm. Unters.-Forsch. A. 207, 133-139.
    • (1998) Z. Lebensm. Unters.-Forsch. A. , vol.207 , pp. 133-139
    • Collar, C.1    Andreu, P.2    Martinez-Anaya, M.A.3
  • 17
  • 18
    • 0002941117 scopus 로고
    • Glucose transforming enzyme
    • (Fogarty, W.M. and Kelly, C.T. Eds.) Elsevier Applied Science, London
    • Crueger, A. and Crueger, W. (1990) Glucose transforming enzyme. In: Microbial Enzymes and Biotechnology (Fogarty, W.M. and Kelly, C.T. Eds.) Elsevier Applied Science, London, pp. 177-226.
    • (1990) Microbial Enzymes and Biotechnology , pp. 177-226
    • Crueger, A.1    Crueger, W.2
  • 19
    • 0029167915 scopus 로고
    • Antibacterial activity of the glucose oxidase/glucose system in liquid whole egg
    • Dobbenie, D., Uyttendaele, M. and Debevere, J. (1995) Antibacterial activity of the glucose oxidase/glucose system in liquid whole egg. J. Food Protect. 58, 273-279.
    • (1995) J. Food Protect. , vol.58 , pp. 273-279
    • Dobbenie, D.1    Uyttendaele, M.2    Debevere, J.3
  • 20
    • 0001516304 scopus 로고
    • Glucose oxidase/catalase improves preservation of shrimp (Heterocarpus reedi)
    • Dondero, M., Egaña, W., Tarky, W., Cifuentes, A. and Torres, J.A. (1993) Glucose oxidase/catalase improves preservation of shrimp (Heterocarpus reedi). J. Food Sci. 58, 774-779.
    • (1993) J. Food Sci. , vol.58 , pp. 774-779
    • Dondero, M.1    Egaña, W.2    Tarky, W.3    Cifuentes, A.4    Torres, J.A.5
  • 21
    • 0036840488 scopus 로고    scopus 로고
    • Effect of oxidative enzymes on bulk rheological properties of wheat flour doughs
    • Dunnewind, B., van Vliet, T. and Orsel, R. (2002) Effect of oxidative enzymes on bulk rheological properties of wheat flour doughs. J. Cereal Sci. 36, 357-366.
    • (2002) J. Cereal Sci. , vol.36 , pp. 357-366
    • Dunnewind, B.1    Van Vliet, T.2    Orsel, R.3
  • 23
    • 12844264142 scopus 로고    scopus 로고
    • Glucose nanosensors based on redox polymer/glucose oxidase modified carbon fiber nanoelectrodes
    • Fei, J.J., Wu, K.B., Wang, F. and Hu, S.S. (2005) Glucose nanosensors based on redox polymer/glucose oxidase modified carbon fiber nanoelectrodes. Talanta 65, 918-924.
    • (2005) Talanta , vol.65 , pp. 918-924
    • Fei, J.J.1    Wu, K.B.2    Wang, F.3    Hu, S.S.4
  • 24
    • 0029974668 scopus 로고    scopus 로고
    • Cholesterol oxidase from Rhodococcus equi is likely the major factor involved in the cooperative lytic process (CAMP reaction) with Listeria monocytogenes
    • Fernanandez-Garayzabal, J.F., Delgado, C., Blanco, M.M., Suarez, G. and Dominguez, L. (1996) Cholesterol oxidase from Rhodococcus equi is likely the major factor involved in the cooperative lytic process (CAMP reaction) with Listeria monocytogenes. Lett. Appl. Microbiol. 22, 249-252.
    • (1996) Lett. Appl. Microbiol. , vol.22 , pp. 249-252
    • Fernanandez-Garayzabal, J.F.1    Delgado, C.2    Blanco, M.M.3    Suarez, G.4    Dominguez, L.5
  • 25
    • 8444230831 scopus 로고    scopus 로고
    • Development and evaluation of electrochemical glucose enzyme biosensors based on carbon film electrodes
    • Florescu, M. and Brett C.M.A. (2005) Development and evaluation of electrochemical glucose enzyme biosensors based on carbon film electrodes. Talanta 65, 306-312.
    • (2005) Talanta , vol.65 , pp. 306-312
    • Florescu, M.1    Brett, C.M.A.2
  • 26
    • 0035982546 scopus 로고    scopus 로고
    • The influence of structure in the reaction of electrochemically generated ferrocenium derivatives with reduced glucose oxidase
    • Forrow, N.J., Sanghera, G.S. and Walters, S.J. (2002) The influence of structure in the reaction of electrochemically generated ferrocenium derivatives with reduced glucose oxidase. Dalton Trans. 16, 3187-3194.
    • (2002) Dalton Trans. , vol.16 , pp. 3187-3194
    • Forrow, N.J.1    Sanghera, G.S.2    Walters, S.J.3
  • 27
    • 0347985820 scopus 로고    scopus 로고
    • Transition metal half-sandwich complexes as redox mediators to glucose oxidase
    • Forrow, N.J. and Walters, S.J. (2004) Transition metal half-sandwich complexes as redox mediators to glucose oxidase. Biosens. Bioelectron. 19, 763-770.
    • (2004) Biosens. Bioelectron. , vol.19 , pp. 763-770
    • Forrow, N.J.1    Walters, S.J.2
  • 28
    • 0037210586 scopus 로고    scopus 로고
    • An immobilized catalase peroxidase from the alkalothermophilic Bacillus SF for the treatment of textilebleaching effluents
    • Fruhwirth, G.O., Paar, A., Gudelj, M., Cavaco-Paulo, A., Robra, K.H. and Gübitz, G.M. (2002) An immobilized catalase peroxidase from the alkalothermophilic Bacillus SF for the treatment of textilebleaching effluents. Appl. Microbiol. Biotechnol. 60, 313-319.
    • (2002) Appl. Microbiol. Biotechnol. , vol.60 , pp. 313-319
    • Fruhwirth, G.O.1    Paar, A.2    Gudelj, M.3    Cavaco-Paulo, A.4    Robra, K.H.5    Gübitz, G.M.6
  • 30
    • 0015811914 scopus 로고
    • A method to screen anticholesterol substances produced by microbes and a new cholesterol oxidase produced by Streptomyces violascens
    • Fukuda, H., Kawakami, Y. and Nakamura, S. (1973) A method to screen anticholesterol substances produced by microbes and a new cholesterol oxidase produced by Streptomyces violascens. Chem. Pharm. Bull. (Tokyo) 21, 2057-2060.
    • (1973) Chem. Pharm. Bull. (Tokyo) , vol.21 , pp. 2057-2060
    • Fukuda, H.1    Kawakami, Y.2    Nakamura, S.3
  • 33
    • 0041733533 scopus 로고    scopus 로고
    • Enzyme applications in detergency and in manufacturing industries
    • Galante, Y.M. and Formantici, C. (2003) Enzyme applications in detergency and in manufacturing industries. Curr. Org. Chem. 7, 1399-1422.
    • (2003) Curr. Org. Chem. , vol.7 , pp. 1399-1422
    • Galante, Y.M.1    Formantici, C.2
  • 34
    • 4944255262 scopus 로고    scopus 로고
    • Amperometric biosensor-based flow-through microdetector for microdialysis applications
    • Gáspár, S, Wang, X., Suzuki, H. and Csöregi, E. (2004) Amperometric biosensor-based flow-through microdetector for microdialysis applications. Anal. Chim. Acta 525, 75-82.
    • (2004) Anal. Chim. Acta , vol.525 , pp. 75-82
    • Gáspár, S.1    Wang, X.2    Suzuki, H.3    Csöregi, E.4
  • 35
    • 0016397910 scopus 로고
    • Stereoelectronic properties of metalloenzymes. II. Effects of ligand coordination on the electron spin resonance spectrum of galactose oxidase as a probe of structure and function
    • Giordano, R.S., Bereman, R.D., Kosman, D.J. and Ettinger, M.J. (1974) Stereoelectronic properties of metalloenzymes. II. Effects of ligand coordination on the electron spin resonance spectrum of galactose oxidase as a probe of structure and function. J. Am. Chem. Soc. 96, 1023-1026.
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 1023-1026
    • Giordano, R.S.1    Bereman, R.D.2    Kosman, D.J.3    Ettinger, M.J.4
  • 36
    • 0035545685 scopus 로고    scopus 로고
    • Layer-by-layer construction of an active multilayer enzyme electrode applicable for direct amperometric determination of cholesterol
    • Gobi, K.V. and Mizutani, F. (2001). Layer-by-layer construction of an active multilayer enzyme electrode applicable for direct amperometric determination of cholesterol. Sensor. Actuat. B-Chem. 80, 272-277.
    • (2001) Sensor. Actuat. B-Chem. , vol.80 , pp. 272-277
    • Gobi, K.V.1    Mizutani, F.2
  • 37
    • 34948830565 scopus 로고
    • Prevention of oxidative browning during wine storage
    • Gomez, E., Martinez, A. and Laencina, J. (1995) Prevention of oxidative browning during wine storage. Food Res. Int. 28, 213-217.
    • (1995) Food Res. Int. , vol.28 , pp. 213-217
    • Gomez, E.1    Martinez, A.2    Laencina, J.3
  • 39
    • 0037178188 scopus 로고    scopus 로고
    • Enhancement of operational stability of an enzyme biosensor for glucose and sucrose using protein based stabilizing agents
    • Gouda, M.D., Kumar, M.A., Thakur, M.S. and Karanth, N.G. (2002). Enhancement of operational stability of an enzyme biosensor for glucose and sucrose using protein based stabilizing agents. Biosens. Bioelectron. 17, 503-507.
    • (2002) Biosens. Bioelectron. , vol.17 , pp. 503-507
    • Gouda, M.D.1    Kumar, M.A.2    Thakur, M.S.3    Karanth, N.G.4
  • 40
    • 0042591234 scopus 로고    scopus 로고
    • Thermal inactivation of glucose oxidase. Mechanism and stabilization using additives
    • Gouda, M.D., Singh, S.A., Rao, A.G., Thakur, M.S. and Karanth, N.G. (2003) Thermal inactivation of glucose oxidase. Mechanism and stabilization using additives. J. Biol. Chem. 278, 24324-24333.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24324-24333
    • Gouda, M.D.1    Singh, S.A.2    Rao, A.G.3    Thakur, M.S.4    Karanth, N.G.5
  • 41
    • 0021759320 scopus 로고
    • Substrate specificity of D-galactose oxidase. Evidence for the oxidation of internally linked galactosyl residues of Helix pomatia galactogen
    • Goudsmit, E.M., Matsuura, F. and Blake, D.A. (1984) Substrate specificity of D-galactose oxidase. Evidence for the oxidation of internally linked galactosyl residues of Helix pomatia galactogen. J. Biol. Chem. 259, 2875-2878.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2875-2878
    • Goudsmit, E.M.1    Matsuura, F.2    Blake, D.A.3
  • 42
    • 10644252823 scopus 로고    scopus 로고
    • Carbon nanotubes-based amperometric cholesterol biosensor fabricated through layer-by-layer technique
    • Guo, M.L., Chen, J.H., Li, J., Nie, L.H. and Yao, S.Z. (2004) Carbon nanotubes-based amperometric cholesterol biosensor fabricated through layer-by-layer technique. Electroanalysis 16, 1992-1998.
    • (2004) Electroanalysis , vol.16 , pp. 1992-1998
    • Guo, M.L.1    Chen, J.H.2    Li, J.3    Nie, L.H.4    Yao, S.Z.5
  • 44
    • 84951400121 scopus 로고
    • An organic phase enzyme electrode for cholesterol
    • Hall, G.F. and Turner, A.P.F. (1991) An organic phase enzyme electrode for cholesterol. Anal. Lett. 24, 1375-1388.
    • (1991) Anal. Lett. , vol.24 , pp. 1375-1388
    • Hall, G.F.1    Turner, A.P.F.2
  • 45
    • 0030031148 scopus 로고    scopus 로고
    • Amperometric enzyme biosensors for metabolites the analysis of drugs and metabolites
    • Harwood, G.W.J. and Pouton, C.W. (1996) Amperometric enzyme biosensors for metabolites the analysis of drugs and metabolites. Adv. Drug Deliver. Rev. 18, 163-191.
    • (1996) Adv. Drug Deliver. Rev. , vol.18 , pp. 163-191
    • Harwood, G.W.J.1    Pouton, C.W.2
  • 46
    • 0033708224 scopus 로고    scopus 로고
    • Amperometric flow-type L-histidine sensor using an immobilized galactose oxidase reactor, based on a novel catalytic activity induced by exogenous histidine
    • Hasebe, Y. and Uchiyama, S. (2000). Amperometric flow-type L-histidine sensor using an immobilized galactose oxidase reactor, based on a novel catalytic activity induced by exogenous histidine. Sensor. Actuat. B-Chem. 66, 12-15.
    • (2000) Sensor. Actuat. B-Chem. , vol.66 , pp. 12-15
    • Hasebe, Y.1    Uchiyama, S.2
  • 47
    • 0032726014 scopus 로고    scopus 로고
    • Baking performance, rheology, and chemical composition of wheat dough and gluten affected by xylanase and oxidative enzymes
    • Hilhorst, R., Dunnewind, B., Orsel, R., Stegeman, P., van Vliet, T., Gruppen, H. and Schols, H.A. (1999) Baking performance, rheology, and chemical composition of wheat dough and gluten affected by xylanase and oxidative enzymes. J. Food Sci. 64, 808-813.
    • (1999) J. Food Sci. , vol.64 , pp. 808-813
    • Hilhorst, R.1    Dunnewind, B.2    Orsel, R.3    Stegeman, P.4    Van Vliet, T.5    Gruppen, H.6    Schols, H.A.7
  • 48
    • 0030981564 scopus 로고    scopus 로고
    • Reactive liposomes encapsulating a glucose oxidase-peroxidase system with antibacterial activity
    • Hill, K.J., Kaszuba, M., Creeth, J.E. and Jones, M.N. (1997) Reactive liposomes encapsulating a glucose oxidase-peroxidase system with antibacterial activity. Biochim. Biophys. Acta 1326, 37-46.
    • (1997) Biochim. Biophys. Acta , vol.1326 , pp. 37-46
    • Hill, K.J.1    Kaszuba, M.2    Creeth, J.E.3    Jones, M.N.4
  • 49
    • 0036888732 scopus 로고    scopus 로고
    • Study of catalase electrode for organic peroxidase assays
    • Horozova, E., Dimcheva, N. and Jordanova Z. (2002) Study of catalase electrode for organic peroxidase assays. Bioelectrochemistry 58, 181-187.
    • (2002) Bioelectrochemistry , vol.58 , pp. 181-187
    • Horozova, E.1    Dimcheva, N.2    Jordanova, Z.3
  • 50
    • 0346958133 scopus 로고    scopus 로고
    • Scanning electron microscopy, rheological characteristics, and bread-baking performance of wheat-flour dough as affected by enzymes
    • Indrani, D., Prabhasankar, P., Rajiv, J. and Rao, G.V. (2003) Scanning electron microscopy, rheological characteristics, and bread-baking performance of wheat-flour dough as affected by enzymes. J. Food Sci. 68, 2804-2809.
    • (2003) J. Food Sci. , vol.68 , pp. 2804-2809
    • Indrani, D.1    Prabhasankar, P.2    Rajiv, J.3    Rao, G.V.4
  • 52
    • 0031441780 scopus 로고    scopus 로고
    • Antioxidative effect of glucose oxidase and catalase in mayonnaises of different oxidative susceptibility. I. Product trials
    • Isaksen, A. and Adler-Nissen, J. (1997) Antioxidative effect of glucose oxidase and catalase in mayonnaises of different oxidative susceptibility. I. Product trials. LWT-Food Sci. Technol. 30, 841-846.
    • (1997) LWT-Food Sci. Technol. , vol.30 , pp. 841-846
    • Isaksen, A.1    Adler-Nissen, J.2
  • 54
    • 84892253952 scopus 로고    scopus 로고
    • Multienzymic system encapsulation: Application to the lactoperoxidase system
    • Jacquot, M. and Poncelet, D. (2003) Multienzymic system encapsulation: application to the lactoperoxidase system. J. Chem. Chem. Eng. Tech. 12, 581-584.
    • (2003) J. Chem. Chem. Eng. Tech. , vol.12 , pp. 581-584
    • Jacquot, M.1    Poncelet, D.2
  • 56
    • 0043022100 scopus 로고    scopus 로고
    • Development of a common biosensor format for an enzyme based biosensor array to monitor fruit quality
    • Jawaheer, S., White, S.F, Rughooputh, S.D.D.V. and Cullen D.C. (2003) Development of a common biosensor format for an enzyme based biosensor array to monitor fruit quality. Biosens. Bioelectron. 18, 1429-1437.
    • (2003) Biosens. Bioelectron. , vol.18 , pp. 1429-1437
    • Jawaheer, S.1    White, S.F.2    Rughooputh, S.D.D.V.3    Cullen, D.C.4
  • 57
    • 0030799166 scopus 로고    scopus 로고
    • Enzymatic removal and disinfection of bacterial biofilms
    • Johansen, C., Falholt, P. and Gram, L. (1997) Enzymatic removal and disinfection of bacterial biofilms. Appl. Environ. Microbiol. 63, 3724-3728.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3724-3728
    • Johansen, C.1    Falholt, P.2    Gram, L.3
  • 58
    • 0000636925 scopus 로고    scopus 로고
    • Antibacterial reactive liposomes encapsulating coupled enzyme systems
    • Jones, M.N., Hill, K.J., Kaszuba, M. and Creeth, J.E. (1998) Antibacterial reactive liposomes encapsulating coupled enzyme systems. Int. J. Pharm. 162, 107-117.
    • (1998) Int. J. Pharm. , vol.162 , pp. 107-117
    • Jones, M.N.1    Hill, K.J.2    Kaszuba, M.3    Creeth, J.E.4
  • 59
    • 0030200283 scopus 로고    scopus 로고
    • A biosensor stabilized by polyethylene glycol for monitoring of hydrogen peroxide in organic solvent media
    • Joo, H., Yoo, Y.J. and Ryu, D.D.Y. (1996) A biosensor stabilized by polyethylene glycol for monitoring of hydrogen peroxide in organic solvent media. Enzyme Microb. Tech. 19, 50-56.
    • (1996) Enzyme Microb. Tech. , vol.19 , pp. 50-56
    • Joo, H.1    Yoo, Y.J.2    Ryu, D.D.Y.3
  • 60
    • 0020493949 scopus 로고
    • Stereospecific oxidation of aliphatic alcohols catalyzed by galactose oxidase
    • Klibanov, A.M., Alberti, B.N. and Marletta, M.A. (1982) Stereospecific oxidation of aliphatic alcohols catalyzed by galactose oxidase. Biochem. Biophys. Res. Commun. 108, 804-808.
    • (1982) Biochem. Biophys. Res. Commun. , vol.108 , pp. 804-808
    • Klibanov, A.M.1    Alberti, B.N.2    Marletta, M.A.3
  • 61
    • 0030854046 scopus 로고    scopus 로고
    • Phylogenetic relationships among prokaryotic and eukaryotic catalases
    • Klotz, M.G. and Klassen, G.R. and Loewen, P.C. (1997) Phylogenetic relationships among prokaryotic and eukaryotic catalases. Mol. Biol. Evol. 14, 951-958.
    • (1997) Mol. Biol. Evol. , vol.14 , pp. 951-958
    • Klotz, M.G.1    Klassen, G.R.2    Loewen, P.C.3
  • 62
    • 0035099819 scopus 로고    scopus 로고
    • Production of glucose oxidase using Aspergillus niger and corn steep liquor
    • Kona, R.P., Qureshi, N. and Pai, J.S. (2001) Production of glucose oxidase using Aspergillus niger and corn steep liquor. Bioresource Technol. 78, 123-126.
    • (2001) Bioresource Technol. , vol.78 , pp. 123-126
    • Kona, R.P.1    Qureshi, N.2    Pai, J.S.3
  • 63
    • 19944362819 scopus 로고    scopus 로고
    • Determination of hydrogen peroxide, glucose and hypoxanthine using (bio)sensors based on ruthenium-dioxide modified screen-printed electrodes
    • Kotzian, P., Brázdilová, P., Kalcher, K. and Vytras, K. (2005). Determination of hydrogen peroxide, glucose and hypoxanthine using (bio)sensors based on ruthenium-dioxide modified screen-printed electrodes. Anal. Lett. 38, 1099-1113.
    • (2005) Anal. Lett. , vol.38 , pp. 1099-1113
    • Kotzian, P.1    Brázdilová, P.2    Kalcher, K.3    Vytras, K.4
  • 65
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 66
    • 9644266721 scopus 로고    scopus 로고
    • Penicillium chrysogenum glucose oxidase - A study on its antifungal effects
    • Leiter, É., Marx, F., Pusztahelyi, T., Haas, H. and Pócsi, I. (2004) Penicillium chrysogenum glucose oxidase - a study on its antifungal effects. J. Appl. Microbiol. 97, 1201-1209.
    • (2004) J. Appl. Microbiol. , vol.97 , pp. 1201-1209
    • Leiter1    É2    Marx, F.3    Pusztahelyi, T.4    Haas, H.5    Pócsi, I.6
  • 67
    • 0038575236 scopus 로고    scopus 로고
    • Expression of the Aspergillus niger glucose oxidase gene in Saccharomyces cerevisiae and its potential applications in wine production
    • Malherbe, D.F., du Toit, M., Cordero Otero, R.R., van Rensburg, P. and Pretorius, I.S. (2003) Expression of the Aspergillus niger glucose oxidase gene in Saccharomyces cerevisiae and its potential applications in wine production. Appl. Microbiol. Biot. 61, 502-511.
    • (2003) Appl. Microbiol. Biot. , vol.61 , pp. 502-511
    • Malherbe, D.F.1    Du Toit, M.2    Cordero Otero, R.R.3    Van Rensburg, P.4    Pretorius, I.S.5
  • 68
    • 0041318879 scopus 로고    scopus 로고
    • Conducting polymer based biomolecular electronic devices Pramana
    • Malhotra, B.D. and Singhal, R. (2003) Conducting polymer based biomolecular electronic devices Pramana. J. Phys. 61, 331-343.
    • (2003) J. Phys. , vol.61 , pp. 331-343
    • Malhotra, B.D.1    Singhal, R.2
  • 70
    • 1642518503 scopus 로고    scopus 로고
    • Maltose biosensor for determining gelatinized starch in processed cereal foods
    • Marconi, E., Messia, M.C., Palleschi, G. and Cubadda, R. (2004) Maltose biosensor for determining gelatinized starch in processed cereal foods. Cereal Chem. 81, 6-9.
    • (2004) Cereal Chem. , vol.81 , pp. 6-9
    • Marconi, E.1    Messia, M.C.2    Palleschi, G.3    Cubadda, R.4
  • 71
    • 0002962296 scopus 로고    scopus 로고
    • Physical properties of enzyme-supplemented doughs and relationship with bread quality parameters
    • Martinez-Anaya, M.A. and Jimenez, T. (1998) Physical properties of enzyme-supplemented doughs and relationship with bread quality parameters. Z. Lebensm. Unters.-Forsch. A. 206, 134-142.
    • (1998) Z. Lebensm. Unters.-Forsch. A. , vol.206 , pp. 134-142
    • Martinez-Anaya, M.A.1    Jimenez, T.2
  • 72
    • 0034979862 scopus 로고    scopus 로고
    • Growth inhibition by glucose oxidase system of enterotoxic Escherichia coli and Salmonella derby: In vitro studies
    • Massa, S., Petruccioli, M., Brocchi, G.F., Altieri, C., Sinigaglia, M. and Spano, G. (2001) Growth inhibition by glucose oxidase system of enterotoxic Escherichia coli and Salmonella derby: in vitro studies. World J. Microb. Biot. 17, 287-291.
    • (2001) World J. Microb. Biot. , vol.17 , pp. 287-291
    • Massa, S.1    Petruccioli, M.2    Brocchi, G.F.3    Altieri, C.4    Sinigaglia, M.5    Spano, G.6
  • 74
    • 1842426962 scopus 로고    scopus 로고
    • Peroxide-utilizing biocatalysts: Structural and functional diversity of heme-containing enzymes
    • Matsunaga, I. and Shiro, Y. (2004) Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes. Curr. Opin. Chem. Biol. 8, 127-32.
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 127-132
    • Matsunaga, I.1    Shiro, Y.2
  • 75
    • 0031035123 scopus 로고    scopus 로고
    • Electron spin echo envelope modulation studies of the semiquinone anion radical of cholesterol oxidase from Brevibacterium sterolicum
    • Medina, M. Vrielink, A. and Cammack, R. (1997) Electron spin echo envelope modulation studies of the semiquinone anion radical of cholesterol oxidase from Brevibacterium sterolicum. FEBS Lett. 400, 247-251.
    • (1997) FEBS Lett. , vol.400 , pp. 247-251
    • Medina, M.1    Vrielink, A.2    Cammack, R.3
  • 77
    • 0034900916 scopus 로고    scopus 로고
    • Identification and mutagenesis by allelic exchange of choE, encoding a cholesterol oxidase from the intracellular pathogen Rhodococcus equi
    • Navas, J., Gonzalez-Zorn, B., Ladron, N., Garrido, P. and Vazquez-Boland, J.A. (2001) Identification and mutagenesis by allelic exchange of choE, encoding a cholesterol oxidase from the intracellular pathogen Rhodococcus equi. J. Bacteriol. 183, 4796-4805.
    • (2001) J. Bacteriol. , vol.183 , pp. 4796-4805
    • Navas, J.1    Gonzalez-Zorn, B.2    Ladron, N.3    Garrido, P.4    Vazquez-Boland, J.A.5
  • 78
    • 0037703424 scopus 로고
    • Use of glucose oxidase to stabilize beer
    • Ohlmeyer, D.W. (1957) Use of glucose oxidase to stabilize beer. Food Technol. October 503-507.
    • (1957) Food Technol. October , pp. 503-507
    • Ohlmeyer, D.W.1
  • 79
    • 11144265915 scopus 로고    scopus 로고
    • Immobilization of catalase on textile carrier materials
    • Opwis, K., Knittel, D. and Schollmeyer, E. (2004) Immobilization of catalase on textile carrier materials. AATCC Rev. 4, 25-28.
    • (2004) AATCC Rev. , vol.4 , pp. 25-28
    • Opwis, K.1    Knittel, D.2    Schollmeyer, E.3
  • 80
    • 0002409878 scopus 로고
    • Further investigations with glucose oxidase-catalase systems for use with wine
    • Ough, C.S. (1975) Further investigations with glucose oxidase-catalase systems for use with wine. Am. J. Enol. Viticult. 26, 30-36.
    • (1975) Am. J. Enol. Viticult. , vol.26 , pp. 30-36
    • Ough, C.S.1
  • 81
    • 0035940062 scopus 로고    scopus 로고
    • Thermo-alkali-stable catalases from newly isolated Bacillus sp. for the treatment and recycling of textile bleaching effluents
    • Paar, A., Costa, S., Tzanov, T., Gudelj, M., Robra, K.H., Cavaco-Paulo, A. and Gübitz, G.M. (2001) Thermo-alkali-stable catalases from newly isolated Bacillus sp. for the treatment and recycling of textile bleaching effluents. J. Biotechnol. 89, 147-153.
    • (2001) J. Biotechnol. , vol.89 , pp. 147-153
    • Paar, A.1    Costa, S.2    Tzanov, T.3    Gudelj, M.4    Robra, K.H.5    Cavaco-Paulo, A.6    Gübitz, G.M.7
  • 82
    • 0037700193 scopus 로고    scopus 로고
    • Production of catalase-peroxidase and continuous degradation of hydrogen peroxide by an immobilized alkalothermophilic Bacillus sp
    • Paar, A., Raninger, A., de Sousa, F., Beurer, I., Cavaco-Paulo, A. and Gübitz, G.M. (2003) Production of catalase-peroxidase and continuous degradation of hydrogen peroxide by an immobilized alkalothermophilic Bacillus sp. Food Technol. Biotech. 41, 101-104.
    • (2003) Food Technol. Biotech. , vol.41 , pp. 101-104
    • Paar, A.1    Raninger, A.2    De Sousa, F.3    Beurer, I.4    Cavaco-Paulo, A.5    Gübitz, G.M.6
  • 83
    • 0036039917 scopus 로고    scopus 로고
    • Preliminary study on glucose oxidasecatalase enzyme system to control the browning of apple and pear purées
    • Parpinello, G.P., Chinnici, F., Versari, A. and Riponi, C. (2002) Preliminary study on glucose oxidasecatalase enzyme system to control the browning of apple and pear purées. LWT-Food Sci. Technol. 35, 239-243.
    • (2002) LWT-Food Sci. Technol. , vol.35 , pp. 239-243
    • Parpinello, G.P.1    Chinnici, F.2    Versari, A.3    Riponi, C.4
  • 84
    • 33845205733 scopus 로고
    • The oxidation of glucose and related compounds by glucose oxidase from Aspergillus niger
    • Pazur, J.H. and Kleppe, K. (1964) The oxidation of glucose and related compounds by glucose oxidase from Aspergillus niger. Biochemistry 3, 578-583.
    • (1964) Biochemistry , vol.3 , pp. 578-583
    • Pazur, J.H.1    Kleppe, K.2
  • 85
    • 0035866633 scopus 로고    scopus 로고
    • Graphite-teflon composite bienzyme electrodes for the determination of cholesterol in reversed micelles. Application to food samples
    • Pena, N., Ruiz, G., Reviejo, A.J. and Pingarron, J.M. (2001) Graphite-teflon composite bienzyme electrodes for the determination of cholesterol in reversed micelles. Application to food samples. Anal. Chem. 73, 1190-1195.
    • (2001) Anal. Chem. , vol.73 , pp. 1190-1195
    • Pena, N.1    Ruiz, G.2    Reviejo, A.J.3    Pingarron, J.M.4
  • 86
    • 0005014988 scopus 로고
    • Screening of Penicillium species for the production of glucose oxidase
    • Petruccioli, M., Ceccarelli, M. and Federici, F. (1993) Screening of Penicillium species for the production of glucose oxidase. World J. Microb. Biot. 9, 77-79.
    • (1993) World J. Microb. Biot. , vol.9 , pp. 77-79
    • Petruccioli, M.1    Ceccarelli, M.2    Federici, F.3
  • 87
    • 0032468940 scopus 로고    scopus 로고
    • Optimising glucose conversion in the production of reduced alcohol wine using glucose oxidase
    • Pickering, G.J., Heatherbell, D.A. and Barnes, M.F. (1998) Optimising glucose conversion in the production of reduced alcohol wine using glucose oxidase. Food Res. Int. 31, 685-692.
    • (1998) Food Res. Int. , vol.31 , pp. 685-692
    • Pickering, G.J.1    Heatherbell, D.A.2    Barnes, M.F.3
  • 88
    • 0032702153 scopus 로고    scopus 로고
    • The production of reduced-alcohol wine using glucose oxidase treated juice. Part I. Composition
    • Pickering, G.J., Heatherbell, D.A. and Barnes, M.F. (1999) The production of reduced-alcohol wine using glucose oxidase treated juice. Part I. Composition. Am. J. Enol. Viticult. 50, 291-298.
    • (1999) Am. J. Enol. Viticult. , vol.50 , pp. 291-298
    • Pickering, G.J.1    Heatherbell, D.A.2    Barnes, M.F.3
  • 90
    • 0344140329 scopus 로고    scopus 로고
    • Inactivation of yeast and filamentous fungi by the lactoperoxidasehydrogen peroxide-thiocyanate system
    • Popper, L. and Knorr, D. (1997) Inactivation of yeast and filamentous fungi by the lactoperoxidasehydrogen peroxide-thiocyanate system. Nahrung 41, 29-33.
    • (1997) Nahrung , vol.41 , pp. 29-33
    • Popper, L.1    Knorr, D.2
  • 91
    • 0042303899 scopus 로고    scopus 로고
    • Effect of pentosanase and oxidases on the characteristics of doughs and the glutenin macropolymer (GMP)
    • Primo-Martin, C., Valera, R. and Martinez-Anaya, M.A. (2003) Effect of pentosanase and oxidases on the characteristics of doughs and the glutenin macropolymer (GMP). J. Agric. Food Chem. 51, 4673-4679.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 4673-4679
    • Primo-Martin, C.1    Valera, R.2    Martinez-Anaya, M.A.3
  • 92
    • 12844280891 scopus 로고    scopus 로고
    • Composition of glutenin macropolymer: Effect of flour quality and nonamylolytic enzyme addition
    • Primo-Martin, C., Martinez-Anaya, M.A. and Collar, C. (2004) Composition of glutenin macropolymer: effect of flour quality and nonamylolytic enzyme addition. Eur. Food Res. Technol. 218, 428-436.
    • (2004) Eur. Food Res. Technol. , vol.218 , pp. 428-436
    • Primo-Martin, C.1    Martinez-Anaya, M.A.2    Collar, C.3
  • 95
    • 4444338986 scopus 로고    scopus 로고
    • Crosslinking of wheat dough proteins by glucose oxidase and the resulting effects and bread and croissants
    • Rasiah, I.A., Sutton, K.H., Low, F.L., Lin, H.M. and Gerrard, J.A. (2005) Crosslinking of wheat dough proteins by glucose oxidase and the resulting effects and bread and croissants. Food Chem. 89, 325-332.
    • (2005) Food Chem. , vol.89 , pp. 325-332
    • Rasiah, I.A.1    Sutton, K.H.2    Low, F.L.3    Lin, H.M.4    Gerrard, J.A.5
  • 96
    • 0035638074 scopus 로고    scopus 로고
    • Antibacterial activities of lactoperoxidase systems (LPS) modified by I- and IO- 3 anions
    • Revol-Junelles, A.M., Boussouel, N., Ramet, J.P. and Millière, J.B. (2001) Antibacterial activities of lactoperoxidase systems (LPS) modified by I- and IO- 3 anions. Milchwissenshaft 56, 329-332.
    • (2001) Milchwissenshaft , vol.56 , pp. 329-332
    • Revol-Junelles, A.M.1    Boussouel, N.2    Ramet, J.P.3    Millière, J.B.4
  • 97
    • 11444255974 scopus 로고    scopus 로고
    • Improved platinization conditions produce a 60-fold increase in sensitivity of amperometric biosensors using glucose oxidase immobilized in poly-o-phenylenediamine
    • Reyes De Corcuera J.I., Cavalieri, R.P. and Powers J.R. (2005) Improved platinization conditions produce a 60-fold increase in sensitivity of amperometric biosensors using glucose oxidase immobilized in poly-o-phenylenediamine. J. Electroanal. Chem. 575, 229-241.
    • (2005) J. Electroanal. Chem. , vol.575 , pp. 229-241
    • Reyes De Corcuera, J.I.1    Cavalieri, R.P.2    Powers, J.R.3
  • 98
    • 23044437622 scopus 로고    scopus 로고
    • Sensor and biosensor preparation, optimisation and applications of Prussian Blue modified electrodes
    • Ricci, F. and Palleschi, G. (2005) Sensor and biosensor preparation, optimisation and applications of Prussian Blue modified electrodes. Biosens. Bioelectron. 21, 389-407.
    • (2005) Biosens. Bioelectron. , vol.21 , pp. 389-407
    • Ricci, F.1    Palleschi, G.2
  • 99
    • 0032914590 scopus 로고    scopus 로고
    • Spectrophotometric kinetic study and analytical implications of the glucose oxidase-catalyzed reduction of MIIILL2Cl2+ complexes by D-glucose (M = Os and Ru, LL = 2 2-bipyridine and 1,10-phenanthroline type ligands)
    • Ryabov, A.D., Firsova, Y.N, Ershov, A.Yu. and Dementiev, I.A. (1999) Spectrophotometric kinetic study and analytical implications of the glucose oxidase-catalyzed reduction of MIIILL2Cl2+ complexes by D-glucose (M = Os and Ru, LL = 2 2-bipyridine and 1,10-phenanthroline type ligands). J. Biol. Inorg. Chem. 4, 175-182.
    • (1999) J. Biol. Inorg. Chem. , vol.4 , pp. 175-182
    • Ryabov, A.D.1    Firsova, Y.N.2    Ershov, A.Yu.3    Dementiev, I.A.4
  • 101
    • 27644439600 scopus 로고    scopus 로고
    • Direct electrochemistry and electrocatalytic activity of catalase incorporated onto multiwall carbon nanotubes-modified glassy carbon electrode
    • Salimi, A., Noorbakhsh, A. and Ghadermarz, M. (2005) Direct electrochemistry and electrocatalytic activity of catalase incorporated onto multiwall carbon nanotubes-modified glassy carbon electrode. Anal. Biochem. 344, 16-24.
    • (2005) Anal. Biochem. , vol.344 , pp. 16-24
    • Salimi, A.1    Noorbakhsh, A.2    Ghadermarz, M.3
  • 102
    • 0032554645 scopus 로고    scopus 로고
    • Assessment of the role of an omega loop of cholesterol oxidase: A truncated loop mutant has altered substrate specificity
    • Sampson, N.S., Kass, I.J and Ghoshroy, K.B. (1998) Assessment of the role of an omega loop of cholesterol oxidase: a truncated loop mutant has altered substrate specificity. Biochemistry 37, 5770-5778.
    • (1998) Biochemistry , vol.37 , pp. 5770-5778
    • Sampson, N.S.1    Kass, I.J.2    Ghoshroy, K.B.3
  • 103
    • 0024022633 scopus 로고
    • Glucose oxidase (GOX) as a source of hydrogen peroxide for the lactoperoxidase (LPO) system in milk: Antibacterial effect of the GOX-LPO system against mastitis pathogens
    • Sandholm, M., Ali-Vehmas, T., Kaartinen, L. and Junnila, M. (1988) Glucose oxidase (GOX) as a source of hydrogen peroxide for the lactoperoxidase (LPO) system in milk: antibacterial effect of the GOX-LPO system against mastitis pathogens. J. Vet. Med. B 35, 346-352.
    • (1988) J. Vet. Med. B , vol.35 , pp. 346-352
    • Sandholm, M.1    Ali-Vehmas, T.2    Kaartinen, L.3    Junnila, M.4
  • 104
    • 0028219705 scopus 로고
    • Construction and application of an enzyme electrode for determination of galactose and galactose-containing saccharides
    • Schumacher, D., Vogel, J. and Lerche, U. (1994) Construction and application of an enzyme electrode for determination of galactose and galactose-containing saccharides. Biosens. Bioelectron. 9, 85-90.
    • (1994) Biosens. Bioelectron. , vol.9 , pp. 85-90
    • Schumacher, D.1    Vogel, J.2    Lerche, U.3
  • 105
    • 0345802624 scopus 로고    scopus 로고
    • Amperometric cholesterol biosensor based on immobilized ChEt and cholesterol oxidase on conducting polypyrrole films
    • Singh, S., Chaubey, A. and Malhotra, B.D. (2004) Amperometric cholesterol biosensor based on immobilized ChEt and cholesterol oxidase on conducting polypyrrole films. Anal. Chim. Acta 502, 229-234.
    • (2004) Anal. Chim. Acta , vol.502 , pp. 229-234
    • Singh, S.1    Chaubey, A.2    Malhotra, B.D.3
  • 106
    • 0032812358 scopus 로고    scopus 로고
    • Flow injection potentiometry for enzymatic assay of cholesterol with a tungsten electrode sensor
    • Situmorang, M., Alexander, P.W. and Hibbert, D.B. (1999) Flow injection potentiometry for enzymatic assay of cholesterol with a tungsten electrode sensor. Talanta 49, 639-649.
    • (1999) Talanta , vol.49 , pp. 639-649
    • Situmorang, M.1    Alexander, P.W.2    Hibbert, D.B.3
  • 107
    • 0033616493 scopus 로고    scopus 로고
    • Catalase HPII from Escherichia coli exhibits enhanced resistance to denaturation
    • Switala, J., O'Neil, J.O. and Loewen, P.C. (1999) Catalase HPII from Escherichia coli exhibits enhanced resistance to denaturation. Biochemistry 38, 3895-3901.
    • (1999) Biochemistry , vol.38 , pp. 3895-3901
    • Switala, J.1    O'neil, J.O.2    Loewen, P.C.3
  • 108
    • 0037095620 scopus 로고    scopus 로고
    • Diversity of properties among catalases Arch
    • Switala J. and Loewen P.C. (2002) Diversity of properties among catalases Arch. Biochem. Biophys. 401, 145-154.
    • (2002) Biochem. Biophys. , vol.401 , pp. 145-154
    • Switala, J.1    Loewen, P.C.2
  • 109
    • 0024707969 scopus 로고
    • Effect of deglycosylation of N-linked sugar chains on glucose oxidase from Aspergillus niger
    • Takegawa, K., Fujiwara, K., Iwahara, S., Yamamoto, K. and Tochikura, T. (1989) Effect of deglycosylation of N-linked sugar chains on glucose oxidase from Aspergillus niger. Biochem. Cell Biol. 67, 460-464.
    • (1989) Biochem. Cell Biol. , vol.67 , pp. 460-464
    • Takegawa, K.1    Fujiwara, K.2    Iwahara, S.3    Yamamoto, K.4    Tochikura, T.5
  • 111
    • 11844266646 scopus 로고    scopus 로고
    • An amperometric cholesterol biosensor based on multiwalled carbon nanotubes and organically modified sol-gel/chitosan hybrid composite film
    • Tan, X.C., Li, M.J., Cai, P.X., Luo, L.J. and Zou, X.Y. (2005) An amperometric cholesterol biosensor based on multiwalled carbon nanotubes and organically modified sol-gel/chitosan hybrid composite film. Anal. Biochem. 337, 111-120.
    • (2005) Anal. Biochem. , vol.337 , pp. 111-120
    • Tan, X.C.1    Li, M.J.2    Cai, P.X.3    Luo, L.J.4    Zou, X.Y.5
  • 112
    • 0028850981 scopus 로고
    • Use of immobilized catalase to remove H2O2 used in the sterilisation of milk
    • Tarhan, L. (1995) Use of immobilized catalase to remove H2O2 used in the sterilisation of milk. Proc. Biochem. 30, 623-628.
    • (1995) Proc. Biochem. , vol.30 , pp. 623-628
    • Tarhan, L.1
  • 113
    • 0034926324 scopus 로고    scopus 로고
    • Effect of temperature and bath composition on the dyeing of cotton with catalase-treated bleaching effluent
    • Tzanov, T., Costa, S., Gübitz, G.M. and Cavaco-Paulo, A. (2001) Effect of temperature and bath composition on the dyeing of cotton with catalase-treated bleaching effluent. Color Technol. 117, 166-170.
    • (2001) Color Technol. , vol.117 , pp. 166-170
    • Tzanov, T.1    Costa, S.2    Gübitz, G.M.3    Cavaco-Paulo, A.4
  • 114
    • 0037203576 scopus 로고    scopus 로고
    • Hydrogen peroxide generation with immobilized glucose oxidase for textile bleaching
    • Tzanov, T., Costa, S.A., Gübitz, G.M. and Cavaco-Paulo, A. (2002) Hydrogen peroxide generation with immobilized glucose oxidase for textile bleaching. J. Biotechnol. 93, 87-94.
    • (2002) J. Biotechnol. , vol.93 , pp. 87-94
    • Tzanov, T.1    Costa, S.A.2    Gübitz, G.M.3    Cavaco-Paulo, A.4
  • 116
    • 0025917559 scopus 로고
    • Biochemical and molecular approaches in understanding carbohydrate metabolism in Aspergillus niger
    • Visser, J. (1991) Biochemical and molecular approaches in understanding carbohydrate metabolism in Aspergillus niger. J. Chem. Tech. Biot. 50, 111-113.
    • (1991) J. Chem. Tech. Biot. , vol.50 , pp. 111-113
    • Visser, J.1
  • 117
    • 0032117892 scopus 로고    scopus 로고
    • Determination of glucose, ascorbic and citric acids by two-ISFET multienzyme sensor
    • Volotovsky, V. and Kim, N. (1998) Determination of glucose, ascorbic and citric acids by two-ISFET multienzyme sensor. Sensor. Actuat. B-Chem. 49, 253-257.
    • (1998) Sensor. Actuat. B-Chem. , vol.49 , pp. 253-257
    • Volotovsky, V.1    Kim, N.2
  • 118
    • 0032897266 scopus 로고    scopus 로고
    • Amperometric biosensors for clinical and therapeutic drug monitoring: A review
    • Wang, J. (1999) Amperometric biosensors for clinical and therapeutic drug monitoring: a review. J. Pharmaceut. Biomed. 19, 47-53.
    • (1999) J. Pharmaceut. Biomed. , vol.19 , pp. 47-53
    • Wang, J.1
  • 121
    • 0023947943 scopus 로고
    • The active site of galactose oxidase
    • Whittaker, M.M. and Whittaker, J.W. (1988) The active site of galactose oxidase. J. Biol. Chem. 263, 6074-6080.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6074-6080
    • Whittaker, M.M.1    Whittaker, J.W.2
  • 122
    • 0025278975 scopus 로고
    • A tyrosine-derived free radical in apogalactose oxidase
    • Whittaker, M.M. and Whittaker, J.W. (1990) A tyrosine-derived free radical in apogalactose oxidase. J. Biol. Chem. 265, 9610-9613.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9610-9613
    • Whittaker, M.M.1    Whittaker, J.W.2
  • 123
    • 0033809942 scopus 로고    scopus 로고
    • Expression of recombinant galactose oxidase by Pichia pastoris
    • Whittaker, M.M. and Whittaker, J.W. (2000) Expression of recombinant galactose oxidase by Pichia pastoris. Protein Expres. Purif. 20, 105-111.
    • (2000) Protein Expres. Purif. , vol.20 , pp. 105-111
    • Whittaker, M.M.1    Whittaker, J.W.2
  • 124
    • 18044367556 scopus 로고    scopus 로고
    • Biosensors for real-time in vivo measurements
    • Wilson, G.S. and Gifford, R. (2005) Biosensors for real-time in vivo measurements. Biosens. Bioelectron. 20, 2388-2403.
    • (2005) Biosens. Bioelectron. , vol.20 , pp. 2388-2403
    • Wilson, G.S.1    Gifford, R.2
  • 125
    • 0033135955 scopus 로고    scopus 로고
    • 1. 8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes
    • Wohlfahrt, G., Witt, S., Hendle, J., Schomburg, D., Kalisz, H.M. and Hecht, H.-J. (1999) 1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes. Acta Crystallogr. D Biol. Crystallogr. 55, 969-977.
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 969-977
    • Wohlfahrt, G.1    Witt, S.2    Hendle, J.3    Schomburg, D.4    Kalisz, H.M.5    Hecht, H.-J.6
  • 126
    • 17644402458 scopus 로고    scopus 로고
    • A biosensor with myrosinase and glucose oxidase bienzyme system for determination of glucosinolates in seeds of commonly consumed vegetables
    • Wu, B.L., Zhang, G.M., Shuang, S.M., Dong, C., Choi, M.M.F. and Lee, A.W.M. (2005) A biosensor with myrosinase and glucose oxidase bienzyme system for determination of glucosinolates in seeds of commonly consumed vegetables. Sensor. Actuat. B-Chem. 106, 700-707.
    • (2005) Sensor. Actuat. B-Chem. , vol.106 , pp. 700-707
    • Wu, B.L.1    Zhang, G.M.2    Shuang, S.M.3    Dong, C.4    Choi, M.M.F.5    Lee, A.W.M.6
  • 127
    • 1542274450 scopus 로고    scopus 로고
    • Structural, spectroscopic, and reactivity models for the manganese catalases
    • Wu, A.J., Penner-Hahn, J.E. and Pecoraro, V.L. (2004) Structural, spectroscopic, and reactivity models for the manganese catalases. Chem. Rev. 104, 903-938.
    • (2004) Chem. Rev. , vol.104 , pp. 903-938
    • Wu, A.J.1    Penner-Hahn, J.E.2    Pecoraro, V.L.3
  • 128
    • 0042977468 scopus 로고    scopus 로고
    • Hydrogel network entrapping cholesterol oxidase and octadecylsilica for optical biosensing in hydrophobic organic or aqueous micelle solvents
    • Wu, X.J. and Choi, M.M.F. (2003) Hydrogel network entrapping cholesterol oxidase and octadecylsilica for optical biosensing in hydrophobic organic or aqueous micelle solvents. Anal. Chem. 75, 4019-4027.
    • (2003) Anal. Chem. , vol.75 , pp. 4019-4027
    • Wu, X.J.1    Choi, M.M.F.2
  • 129
    • 0035818466 scopus 로고    scopus 로고
    • Homemade cofactors: Self-processing in galactose oxidase
    • Xie, L.L. and van der Donk, W.A. (2001) Homemade cofactors: self-processing in galactose oxidase. Proc. Natl. Acad. Sci. USA 98, 12863-12865.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12863-12865
    • Xie, L.L.1    Van Der Donk, W.A.2
  • 131
    • 0242486387 scopus 로고    scopus 로고
    • Glucose sensor for flow injection analysis of serum glucose based on immobilization of glucose oxidase in titania sol-gel membrane Biosens
    • Yu, J.H., Liu, S.Q. and Ju, H.X. (2003) Glucose sensor for flow injection analysis of serum glucose based on immobilization of glucose oxidase in titania sol-gel membrane Biosens. Bioelectron. 19, 401-409.
    • (2003) Bioelectron. , vol.19 , pp. 401-409
    • Yu, J.H.1    Liu, S.Q.2    Ju, H.X.3


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