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Volumn 10, Issue 4, 1999, Pages 370-375

Applications of oxidoreductases

Author keywords

[No Author keywords available]

Indexed keywords

OXIDOREDUCTASE; POLYMER;

EID: 0033179693     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(99)80067-6     Document Type: Article
Times cited : (104)

References (42)
  • 1
    • 0003135810 scopus 로고
    • Enzymatic epoxidation
    • May SW: Enzymatic epoxidation. Enzyme Microb Technol 1979, 1:15-22.
    • (1979) Enzyme Microb Technol , vol.1 , pp. 15-22
    • May, S.W.1
  • 3
    • 0021025281 scopus 로고
    • The potential of oxidoreductase enzymes in biotechnology
    • May SW, Padgette SR: The potential of oxidoreductase enzymes in biotechnology. Nat Biotechnol 1983, 1:677-686.
    • (1983) Nat Biotechnol , vol.1 , pp. 677-686
    • May, S.W.1    Padgette, S.R.2
  • 4
    • 0026569956 scopus 로고
    • Biocatalysis in the 90s: A perspective
    • May SW: Biocatalysis in the 90s: A perspective. Enzyme Microb Technol 1992, 14:80-84.
    • (1992) Enzyme Microb Technol , vol.14 , pp. 80-84
    • May, S.W.1
  • 5
    • 0030897544 scopus 로고    scopus 로고
    • New applications for biocatalysis
    • May SW: New applications for biocatalysis. Curr Opin Biotechnol 1997, 8:181-186.
    • (1997) Curr Opin Biotechnol , vol.8 , pp. 181-186
    • May, S.W.1
  • 6
    • 0031974508 scopus 로고    scopus 로고
    • Evaluation of the optimal test for rapid diagnosis of Plasmodium vivax and Plasmodium falciparum malaria
    • This paper describes evaluation of an oxidoreductase-based diagnostic test which is of great interest from a public health perspective
    • Palmer CJ, Lindo JF, Klaskala WI, Quesada JA, Kaminsky R, Baum MK, Ager AL: Evaluation of the optimal test for rapid diagnosis of Plasmodium vivax and Plasmodium falciparum malaria. J Clin Microbiol 1998, 36:203-206. This paper describes evaluation of an oxidoreductase-based diagnostic test which is of great interest from a public health perspective.
    • (1998) J Clin Microbiol , vol.36 , pp. 203-206
    • Palmer, C.J.1    Lindo, J.F.2    Klaskala, W.I.3    Quesada, J.A.4    Kaminsky, R.5    Baum, M.K.6    Ager, A.L.7
  • 7
    • 0031798467 scopus 로고    scopus 로고
    • Covalently immobilized choline oxidase and cholinesterases on a methacrylate copolymer for disposable membrane biosensors
    • In this work, bienzymatic sensors for the determination of choline esters were constructed by covalent co-immobilization of cholinesterases and choline oxidase on polymer membranes, which were then applied to platinum electrodes
    • Doretti L, Gattolin P, Burla A, Ferrara D, Lora S, Palma G: Covalently immobilized choline oxidase and cholinesterases on a methacrylate copolymer for disposable membrane biosensors. Appl Biochem Biotechnol 1998, 74:1-12. In this work, bienzymatic sensors for the determination of choline esters were constructed by covalent co-immobilization of cholinesterases and choline oxidase on polymer membranes, which were then applied to platinum electrodes.
    • (1998) Appl Biochem Biotechnol , vol.74 , pp. 1-12
    • Doretti, L.1    Gattolin, P.2    Burla, A.3    Ferrara, D.4    Lora, S.5    Palma, G.6
  • 8
    • 0032119612 scopus 로고    scopus 로고
    • Electrochemical characteristics of d-amino acid oxidase immobilized in a conductive redox polymer
    • Arai G, Noma T, Hayashi M, Yasumori I: Electrochemical characteristics of d-amino acid oxidase immobilized in a conductive redox polymer. J Electroanal Chem 1998, 452:43-48.
    • (1998) J Electroanal Chem , vol.452 , pp. 43-48
    • Arai, G.1    Noma, T.2    Hayashi, M.3    Yasumori, I.4
  • 9
    • 0031936489 scopus 로고    scopus 로고
    • Determination of D-amino acids using a D-amino acid oxidase biosensor with spectrophotometric and potentiometric detection
    • SAcchi S, Pollegioni L, Pilone MS, Rossetti C: Determination of D-amino acids using a D-amino acid oxidase biosensor with spectrophotometric and potentiometric detection. Biotechnol Techniques 1998,12:149-153.
    • (1998) Biotechnol Techniques , vol.12 , pp. 149-153
    • Sacchi, S.1    Pollegioni, L.2    Pilone, M.S.3    Rossetti, C.4
  • 10
    • 0031592274 scopus 로고    scopus 로고
    • Amperometric mediated carbon paste biosensor based on D-fructose dehydrogenase for the determination of fructose in food analysis
    • Paredes PA, Parellada J, Fernandez VM, Katakis I, Dominguez E: Amperometric mediated carbon paste biosensor based on D-fructose dehydrogenase for the determination of fructose in food analysis. Biosens Bioelectron 1997, 12:1233-1243.
    • (1997) Biosens Bioelectron , vol.12 , pp. 1233-1243
    • Paredes, P.A.1    Parellada, J.2    Fernandez, V.M.3    Katakis, I.4    Dominguez, E.5
  • 12
    • 0031889621 scopus 로고    scopus 로고
    • Electrosynthesized non-conducting polymers as permselective membranes in amperometric enzyme electrodes: A glucose biosensor based on a co-crosslinked glucose oxidase/overoxidized polypyrrole bilayer
    • Guerrieri A, De Benedetto GE, Palmisano F, Zambonin PG: Electrosynthesized non-conducting polymers as permselective membranes in amperometric enzyme electrodes: A glucose biosensor based on a co-crosslinked glucose oxidase/overoxidized polypyrrole bilayer. Biosens Bioelectron 1998, 13:103-112.
    • (1998) Biosens Bioelectron , vol.13 , pp. 103-112
    • Guerrieri, A.1    De Benedetto, G.E.2    Palmisano, F.3    Zambonin, P.G.4
  • 13
    • 0032214829 scopus 로고    scopus 로고
    • Electrochemistry of reconstituted glucose oxidase on carbon paste electrodes
    • Savitari D, Mitra CK: Electrochemistry of reconstituted glucose oxidase on carbon paste electrodes. Bioelectrochem Bioenerg 1998, 47:67-73.
    • (1998) Bioelectrochem Bioenerg , vol.47 , pp. 67-73
    • Savitari, D.1    Mitra, C.K.2
  • 14
    • 0032131612 scopus 로고    scopus 로고
    • Whole blood assay of glucose-6-phosphate dehydrogenase: Potential for simplified immunoassay
    • Tham SY, Pearson JE, Kane JW, Treloar PH, Vadgama PM: Whole blood assay of glucose-6-phosphate dehydrogenase: Potential for simplified immunoassay. Sensors Actuators 1998, B50:204-209.
    • (1998) Sensors Actuators , vol.B50 , pp. 204-209
    • Tham, S.Y.1    Pearson, J.E.2    Kane, J.W.3    Treloar, P.H.4    Vadgama, P.M.5
  • 15
    • 0032005593 scopus 로고    scopus 로고
    • Amperometric immunosensor for lactate dehydrogenase LD-1
    • Kelly S, Compagnone D, GUilbault G: Amperometric immunosensor for lactate dehydrogenase LD-1. Biosens Bioelectron 1998, 13:173-179.
    • (1998) Biosens Bioelectron , vol.13 , pp. 173-179
    • Kelly, S.1    Compagnone, D.2    Guilbault, G.3
  • 16
    • 0032078557 scopus 로고    scopus 로고
    • Direct electrochemistry of membrane- entrapped horseradish peroxidase part II: Amperometric detection of hydrogen peroxide
    • Ferri T, Poscia A, Santucci R: Direct electrochemistry of membrane- entrappedentrapped horseradish peroxidase part II: Amperometric detection of hydrogen peroxide. Bioelectrochem Bioenerg 1998, 45:221-226.
    • (1998) Bioelectrochem Bioenerg , vol.45 , pp. 221-226
    • Ferri, T.1    Poscia, A.2    Santucci, R.3
  • 18
    • 0031877248 scopus 로고    scopus 로고
    • Cofactor engineering: A novel approach to metabolic engineering in Lactococcus lactis by controlled expression of NADH oxidase
    • De Felipe FL, Kleerebezem M, De Vos WM, Hugenholtz J: Cofactor engineering: A novel approach to metabolic engineering in Lactococcus lactis by controlled expression of NADH oxidase. J Bacteriol 1998, 180:3804-3808.
    • (1998) J Bacteriol , vol.180 , pp. 3804-3808
    • De Felipe, F.L.1    Kleerebezem, M.2    De Vos, W.M.3    Hugenholtz, J.4
  • 19
    • 0032002467 scopus 로고    scopus 로고
    • +-dependent dehydrogenases as catalysts: Application of an electro- Enzymatic method to regenerate nicotinamide adenine dinucleotide at low overpotentials
    • A highly innovative approach to coenzyme recycling is described in this paper
    • +-dependent dehydrogenases as catalysts: Application of an electro- Enzymatic method to regenerate nicotinamide adenine dinucleotide at low overpotentials. J Electroanal Chem 1998, 443:155-161. A highly innovative approach to coenzyme recycling is described in this paper.
    • (1998) J Electroanal Chem , vol.443 , pp. 155-161
    • Tayhas, G.1    Palmore, R.2    Bertschy, H.3    Bergens, S.H.4    Whitesides, G.M.5
  • 20
    • 0031606997 scopus 로고    scopus 로고
    • Escherichia coli transformant expressing the glucose dehydrogenase gene from Bacillus megaterium as a cofactor regenerator in a chiral alcohol production system
    • Kataoka M, Rohani LPS, Wada M, KIta K, Yanase H, Urabe I: Escherichia coli transformant expressing the glucose dehydrogenase gene from Bacillus megaterium as a cofactor regenerator in a chiral alcohol production system. Biosci Biotechnol Biochem 1998, 62:167-169.
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 167-169
    • Kataoka, M.1    Rohani, L.P.S.2    Wada, M.3    Kita, K.4    Yanase, H.5    Urabe, I.6
  • 22
    • 0032055780 scopus 로고    scopus 로고
    • Oxidation of polycyclic aromatic hydrocarbons (PAH) by laccase of Trametes versicolor
    • Majcherczyk A, Johannes C, Huettermann A: Oxidation of polycyclic aromatic hydrocarbons (PAH) by laccase of Trametes versicolor. Enzyme Microb Technol 1998, 22:335-341.
    • (1998) Enzyme Microb Technol , vol.22 , pp. 335-341
    • Majcherczyk, A.1    Johannes, C.2    Huettermann, A.3
  • 23
    • 0032552814 scopus 로고    scopus 로고
    • III-chelate as a chemical oxidant of chlorophenols
    • See annotation to [24••]
    • III-chelate as a chemical oxidant of chlorophenols. Biotechnol Bioeng 1998, 60:204-215. See annotation to [24••].
    • (1998) Biotechnol Bioeng , vol.60 , pp. 204-215
    • Grabski, A.C.1    Grimek, H.J.2    Burgess, R.R.3
  • 25
    • 0031916319 scopus 로고    scopus 로고
    • Influence of culture parameters on extracellular peroxidase activity and transformation of low-rank coal by Phanerochaete chrysosporium
    • Ralph JP, Catcheside DEA: Influence of culture parameters on extracellular peroxidase activity and transformation of low-rank coal by Phanerochaete chrysosporium. Appl Microbiol Biotechnol 1998, 49:438-444.
    • (1998) Appl Microbiol Biotechnol , vol.49 , pp. 438-444
    • Ralph, J.P.1    Catcheside, D.E.A.2
  • 26
    • 0031837944 scopus 로고    scopus 로고
    • Involvement of manganese peroxidase in the transformation of macromolecules from low-rank coal by Phanerochaete chrysosporium
    • Ralph JP, Catcheside DEA: Involvement of manganese peroxidase in the transformation of macromolecules from low-rank coal by Phanerochaete chrysosporium. Appl Microbiol Biotechnol 1998, 49:778-784.
    • (1998) Appl Microbiol Biotechnol , vol.49 , pp. 778-784
    • Ralph, J.P.1    Catcheside, D.E.A.2
  • 27
    • 0031864421 scopus 로고    scopus 로고
    • Detoxification of wood hydrolysates with laccase and peroxidase from the white-rot fungus Trametes versicolor
    • Joensson LJ, Palmqvist E, Nilvebrant N-O, Hahn-Haegerdal B: Detoxification of wood hydrolysates with laccase and peroxidase from the white-rot fungus Trametes versicolor. Appl Microbiol Biotechnol 1998, 49:691 -697.
    • (1998) Appl Microbiol Biotechnol , vol.49 , pp. 691-697
    • Joensson, L.J.1    Palmqvist, E.2    Nilvebrant, N.-O.3    Hahn-Haegerdal, B.4
  • 28
    • 0031869637 scopus 로고    scopus 로고
    • Cloning of a Sphingomonas paucimobilis SYK-6 gene encoding a novel oxygenase that cleaves lignin- Related biphenyl and characterization of the enzyme
    • Peng X, Egashira T, Hanashiro K, Masai E, Nishikawa S, Katayama Y, KImbara K, Fukuda M: Cloning of a Sphingomonas paucimobilis SYK-6 gene encoding a novel oxygenase that cleaves lignin- Related biphenyl and characterization of the enzyme. Appl Environ Microbiol 1998, 64:2520-2527.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2520-2527
    • Peng, X.1    Egashira, T.2    Hanashiro, K.3    Masai, E.4    Nishikawa, S.5    Katayama, Y.6    Kimbara, K.7    Fukuda, M.8
  • 29
    • 0009595261 scopus 로고
    • New oxyfunctionalization capabilities for ω-hydroxylases: Asymmetric sulfoxidation and branched ether demethylation
    • Katopodis AG, Smith HS, May SW: New oxyfunctionalization capabilities for ω-hydroxylases: Asymmetric sulfoxidation and branched ether demethylation. J Am Chem Soc 1988, 110:897-899.
    • (1988) J Am Chem Soc , vol.110 , pp. 897-899
    • Katopodis, A.G.1    Smith, H.S.2    May, S.W.3
  • 30
    • 0000396693 scopus 로고
    • Facile stereoselective allylic hydroxylation by dopamine-β-monooxygenase
    • Sirimanne SR, May SW: Facile stereoselective allylic hydroxylation by dopamine-β-monooxygenase. J Am Chem Soc 1988, 110:7560-7561.
    • (1988) J Am Chem Soc , vol.110 , pp. 7560-7561
    • Sirimanne, S.R.1    May, S.W.2
  • 31
    • 0025092280 scopus 로고
    • Hydrocarbon monooxygenase system of Pseudomonas oleovorans
    • May SW, Katopodis AG: Hydrocarbon monooxygenase system of Pseudomonas oleovorans. Methods Enzymol 1990, 188:3-9.
    • (1990) Methods Enzymol , vol.188 , pp. 3-9
    • May, S.W.1    Katopodis, A.G.2
  • 33
    • 0031983265 scopus 로고    scopus 로고
    • Synthesis of alkane hydroxylase of Pseudomonas oleovorans increases the iron requirement of alk super(+) bacterial strains
    • Staijen I, Witholt B: Synthesis of alkane hydroxylase of Pseudomonas oleovorans increases the iron requirement of alk super(+) bacterial strains. Biotechnol Bioeng 1998, 57:228-237.
    • (1998) Biotechnol Bioeng , vol.57 , pp. 228-237
    • Staijen, I.1    Witholt, B.2
  • 34
    • 0345451054 scopus 로고    scopus 로고
    • Alkane hydroxylase from Acinetobacter sp. strain ADP1 is encoded by alkM and belongs to a new family of bacterial integral-membrane hydrocarbon hydroxylases
    • Ratajczak A, Geissdoerfer W, Hillen W: Alkane hydroxylase from Acinetobacter sp. strainstrain ADP1 is encoded by alkM and belongs to a new family of bacterial integral-membrane hydrocarbon hydroxylases. Appl Environ Microbiol 1998, 64:1175-1179.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 1175-1179
    • Ratajczak, A.1    Geissdoerfer, W.2    Hillen, W.3
  • 35
    • 0032552110 scopus 로고    scopus 로고
    • Structure of a cephalosporin synthase
    • This landmark paper reports high-resolution crystal structures of three catalytically significant forms of deacetoxycephalosporin C synthase from Streptomyces clavuligerus. This represents the first crystal structure of a 2-oxoacid-dependent oxygenase
    • Valegaard K, van Scheltinga ACT, Lloyd MD, Hara T, Ramaswamy S, Perrakis A, Thompson A, Lee HJ, Baldwin JE, Schofield CJ et al.: Structure of a cephalosporin synthase. Nature 1998, 394:805-809. This landmark paper reports high-resolution crystal structures of three catalytically significant forms of deacetoxycephalosporin C synthase from Streptomyces clavuligerus. This represents the first crystal structure of a 2-oxoacid-dependent oxygenase.
    • (1998) Nature , vol.394 , pp. 805-809
    • Valegaard, K.1    Van Scheltinga, A.C.T.2    Lloyd, M.D.3    Hara, T.4    Ramaswamy, S.5    Perrakis, A.6    Thompson, A.7    Lee, H.J.8    Baldwin, J.E.9    Schofield, C.J.10
  • 36
    • 0032520243 scopus 로고    scopus 로고
    • Spectrophotometric method for kinetic studies with quinone-dependent oxidoreductases. Application to detection in membranes of nitrate reductase activity with menadione and duroquinone as electron donors
    • Buc J, Giordani R: Spectrophotometric method for kinetic studies with quinone-dependent oxidoreductases. Application to detection in membranes of nitrate reductase activity with menadione and duroquinone as electron donors. Enzyme Microb Technol 1998, 22:165-169.
    • (1998) Enzyme Microb Technol , vol.22 , pp. 165-169
    • Buc, J.1    Giordani, R.2
  • 37
    • 0032053780 scopus 로고    scopus 로고
    • A novel phenol hydroxylase and catechol 2,3- dioxygenase from the thermophilic Bacillus thermoleovorans strain A2: Nucleotide sequence and analysis of the genes
    • Duffner FM, Muller R: A novel phenol hydroxylase and catechol 2,3- dioxygenasedioxygenase from the thermophilic Bacillus thermoleovorans strain A2: Nucleotide sequence and analysis of the genes. FEMS Microbiol Lett 1998, 161:37-45.
    • (1998) FEMS Microbiol Lett , vol.161 , pp. 37-45
    • Duffner, F.M.1    Muller, R.2
  • 38
    • 0032214585 scopus 로고    scopus 로고
    • Enzymatic synthesis and various properties of poly(catechol)
    • Dubey S, Singh D, Misra RA: Enzymatic synthesis and various properties of poly(catechol). Enzyme Microb Technol 1998, 23:432-437.
    • (1998) Enzyme Microb Technol , vol.23 , pp. 432-437
    • Dubey, S.1    Singh, D.2    Misra, R.A.3
  • 39
    • 0031643099 scopus 로고    scopus 로고
    • Peroxidase-catalyzed dispersion polymerization of phenol derivatives
    • Kurioka H, Uyama H, Kobayashi S: Peroxidase-catalyzed dispersion polymerization of phenol derivatives. Polym J 1998, 30:526-529.
    • (1998) Polym J , vol.30 , pp. 526-529
    • Kurioka, H.1    Uyama, H.2    Kobayashi, S.3
  • 40
    • 0031673226 scopus 로고    scopus 로고
    • Enzymatically prepared poly(hydroquinone) as a mediator for amperometric glucose sensors
    • In this innovative biosensor, the enzymatically synthesized poly(hydroquinone) polymer functions itself as the redox mediator for glucose detection
    • Wang P, Amarasinghe S, Leddy J, Arnold M, Dordick JS: Enzymatically prepared poly(hydroquinone) as a mediator for amperometric glucose sensors. Polymer 1998, 39:123-127. In this innovative biosensor, the enzymatically synthesized poly(hydroquinone) polymer functions itself as the redox mediator for glucose detection.
    • (1998) Polymer , vol.39 , pp. 123-127
    • Wang, P.1    Amarasinghe, S.2    Leddy, J.3    Arnold, M.4    Dordick, J.S.5
  • 41
    • 0030798289 scopus 로고    scopus 로고
    • Toxicity screening of biodegradable polymers. II. Evaluation of cell culture test with medium extract
    • Dang M-H, Birchler F, Wintermantel E: Toxicity screening of biodegradable polymers. II. Evaluation of cell culture test with medium extract. J Environ Polym Degrad 1997, 5:49-56.
    • (1997) J Environ Polym Degrad , vol.5 , pp. 49-56
    • Dang, M.-H.1    Birchler, F.2    Wintermantel, E.3


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