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Volumn 167, Issue 5, 2004, Pages 1151-1157

Comparative studies of the peroxidases from hairy roots of Daucus carota, Ipomoea batatas and Solanum aviculare

Author keywords

Daucus carota; Hairy roots; Ipomoea batatas; Peroxidases; Phytoremediation of phenols; Solanum aviculare

Indexed keywords

ENZYMES; EXTRACTION; OXIDATION;

EID: 4143135480     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2004.06.015     Document Type: Article
Times cited : (30)

References (26)
  • 1
    • 0034956650 scopus 로고    scopus 로고
    • Plant peroxidases: Substrate complexes with mechanistic implications
    • Gajhede M. Plant peroxidases: substrate complexes with mechanistic implications. Biochem. Soc. Trans. 29:2001;91-99
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 91-99
    • Gajhede, M.1
  • 2
    • 0036259575 scopus 로고    scopus 로고
    • Involvement of blueberry peroxidases in the mechanism of anthocyanin degradation in blueberry juice
    • Kader R., Irmoulj M., Nicolas J.P., Metche M. Involvement of blueberry peroxidases in the mechanism of anthocyanin degradation in blueberry juice. J. Food Sci. 67:2002;911-915
    • (2002) J. Food Sci. , vol.67 , pp. 911-915
    • Kader, R.1    Irmoulj, M.2    Nicolas, J.P.3    Metche, M.4
  • 4
    • 0033791439 scopus 로고    scopus 로고
    • Reactivity of horseradish peroxidase compound II toward substrates: Kinetic evidence for a two step mechanism
    • Rodríguez-López J.N., Gilabert M.A., Tudela J., Thornley R.N.F., Garcia-Canovas F. Reactivity of horseradish peroxidase compound II toward substrates: kinetic evidence for a two step mechanism. Biochemistry. 39:2000;1320-13209
    • (2000) Biochemistry , vol.39 , pp. 1320-13209
    • Rodríguez-López, J.N.1    Gilabert, M.A.2    Tudela, J.3    Thornley, R.N.F.4    Garcia-Canovas, F.5
  • 5
    • 0035958073 scopus 로고    scopus 로고
    • Roles of water in heme peroxidase and catalase mechanisms
    • Jones P. Roles of water in heme peroxidase and catalase mechanisms. J. Biol. Chem. 276:2001;13791-13796
    • (2001) J. Biol. Chem. , vol.276 , pp. 13791-13796
    • Jones, P.1
  • 6
    • 0002025713 scopus 로고    scopus 로고
    • Enzymatic activity of root exudates of Dahurian wild rye (Elymus dauricus) that degrades 2-chlorobenzoic acid
    • Siciliano S.D., Goldie H., Germida J.J. Enzymatic activity of root exudates of Dahurian wild rye (Elymus dauricus) that degrades 2-chlorobenzoic acid. J. Agric. Food Chem. 46:1998;5-7
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 5-7
    • Siciliano, S.D.1    Goldie, H.2    Germida, J.J.3
  • 7
    • 0032189361 scopus 로고    scopus 로고
    • Kinetic study on the removal of toxic phenol and chlorophenol from waste water by horseradish peroxidase
    • Tong Z., Qingxiang Z., Hui H., Qin L., Yi Z. Kinetic study on the removal of toxic phenol and chlorophenol from waste water by horseradish peroxidase. Chemosphere. 37:1998;1571-1577
    • (1998) Chemosphere , vol.37 , pp. 1571-1577
    • Tong, Z.1    Qingxiang, Z.2    Hui, H.3    Qin, L.4    Yi, Z.5
  • 8
    • 0033622918 scopus 로고    scopus 로고
    • Toxicity of soluble products from the peroxidase-catalysed polymerization of substituted phenolic compounds
    • Ghioureliotis M., Nicell J.A. Toxicity of soluble products from the peroxidase-catalysed polymerization of substituted phenolic compounds. J. Chem. Toxicol. Biotechnol. 75:2000;98-106
    • (2000) J. Chem. Toxicol. Biotechnol. , vol.75 , pp. 98-106
    • Ghioureliotis, M.1    Nicell, J.A.2
  • 9
    • 0033955219 scopus 로고    scopus 로고
    • Substrate specificity of lignin peroxidase and a S168W variant of manganese peroxidase
    • Timofeevski S.L., Nie G., Reading S., Aust S.D. Substrate specificity of lignin peroxidase and a S168W variant of manganese peroxidase. Arch. Biochem. Biophys. 373:2000;147-153
    • (2000) Arch. Biochem. Biophys. , vol.373 , pp. 147-153
    • Timofeevski, S.L.1    Nie, G.2    Reading, S.3    Aust, S.D.4
  • 10
    • 0038571354 scopus 로고    scopus 로고
    • Removal of aqueous phenol by Arthromyces ramosus peroxidase
    • Villalobos D.A., Buchanan I.D. Removal of aqueous phenol by Arthromyces ramosus peroxidase. J. Environ. Eng. Sci. 1:2002;65-73
    • (2002) J. Environ. Eng. Sci. , vol.1 , pp. 65-73
    • Villalobos, D.A.1    Buchanan, I.D.2
  • 11
    • 0036750893 scopus 로고    scopus 로고
    • Detoxification of phenolic solutions with horseradish peroxidase and hydrogen peroxide
    • Wagner M., Nicell J.A. Detoxification of phenolic solutions with horseradish peroxidase and hydrogen peroxide. Water Res. 36:2002;4041-4052
    • (2002) Water Res. , vol.36 , pp. 4041-4052
    • Wagner, M.1    Nicell, J.A.2
  • 12
    • 0028006782 scopus 로고
    • Phenol conversion and dimeric intermediates in horseradish peroxidase-catalyzed phenol removal from water
    • Yu J., Taylor K.E., Zou H., Biswas N., Bewtra J.K. Phenol conversion and dimeric intermediates in horseradish peroxidase-catalyzed phenol removal from water. Environ. Sci. Technol. 28:1994;2154-2160
    • (1994) Environ. Sci. Technol. , vol.28 , pp. 2154-2160
    • Yu, J.1    Taylor, K.E.2    Zou, H.3    Biswas, N.4    Bewtra, J.K.5
  • 13
    • 0028765761 scopus 로고
    • Use of plant material for the decontamination of water polluted with phenols
    • Dec J., Bollag J.M. Use of plant material for the decontamination of water polluted with phenols. Biotechnol. Bioeng. 44:1994;1131-1139
    • (1994) Biotechnol. Bioeng. , vol.44 , pp. 1131-1139
    • Dec, J.1    Bollag, J.M.2
  • 14
    • 0035909072 scopus 로고    scopus 로고
    • Differential activity and structure of highly similar peroxidases. Spectroscopic crystallographic and enzymatic analyses of lignifying Arabdopsis thaliana peroxidases A2 and horseradish peroxidases A2
    • Nielsen K.L., Indiani C., Henriksen A., Feis A., Becucci M., Gajhede M., Smulevich G., Welinder K. Differential activity and structure of highly similar peroxidases. Spectroscopic crystallographic and enzymatic analyses of lignifying Arabdopsis thaliana peroxidases A2 and horseradish peroxidases A2. Biochemistry. 40:2001;11013-11021
    • (2001) Biochemistry , vol.40 , pp. 11013-11021
    • Nielsen, K.L.1    Indiani, C.2    Henriksen, A.3    Feis, A.4    Becucci, M.5    Gajhede, M.6    Smulevich, G.7    Welinder, K.8
  • 15
    • 0036139575 scopus 로고    scopus 로고
    • Tolerance and metabolism of phenol and chloroderivatives by hairy roots of Daucus carota
    • Araujo B.S., Pletsch M., Charlwood B.V. Tolerance and metabolism of phenol and chloroderivatives by hairy roots of Daucus carota. Environ. Pollut. 117:2002;329-335
    • (2002) Environ. Pollut. , vol.117 , pp. 329-335
    • Araujo, B.S.1    Pletsch, M.2    Charlwood, B.V.3
  • 16
    • 0034124198 scopus 로고    scopus 로고
    • The regulation of solasodine production by Agrobacterium rhizogenes-transformed roots of Solanum aviculare
    • Argôlo A.C.C., Charlwood B.V., Pletsch M. The regulation of solasodine production by Agrobacterium rhizogenes-transformed roots of Solanum aviculare. Planta Med. 66:2000;448-451
    • (2000) Planta Med. , vol.66 , pp. 448-451
    • Argôlo, A.C.C.1    Charlwood, B.V.2    Pletsch, M.3
  • 17
    • 0343494909 scopus 로고    scopus 로고
    • Peroxidase production from carrot hairy root culture
    • Kim Y.H., Yoo Y.J. Peroxidase production from carrot hairy root culture. Enz. Microb. Technol. 18:1996;531-535
    • (1996) Enz. Microb. Technol. , vol.18 , pp. 531-535
    • Kim, Y.H.1    Yoo, Y.J.2
  • 19
    • 0026203946 scopus 로고
    • Peroxidase-catalyzed co-oxidation of halogen-substituted phenols and 4-aminoantipyrine
    • Metelitza D.I., Litvinchuk A.V., Savenkova M.I. Peroxidase-catalyzed co-oxidation of halogen-substituted phenols and 4-aminoantipyrine. J. Mol. Catal. 67:1991;401-411
    • (1991) J. Mol. Catal. , vol.67 , pp. 401-411
    • Metelitza, D.I.1    Litvinchuk, A.V.2    Savenkova, M.I.3
  • 21
    • 0030267947 scopus 로고    scopus 로고
    • Enhancement of peroxidase activity by stress-related chemicals in sweet potato
    • Kwak S.S., Kim S.K., Park I.H., Liu J.R. Enhancement of peroxidase activity by stress-related chemicals in sweet potato. Phytochemistry. 43:1996;565-568
    • (1996) Phytochemistry , vol.43 , pp. 565-568
    • Kwak, S.S.1    Kim, S.K.2    Park, I.H.3    Liu, J.R.4
  • 22
    • 0343852899 scopus 로고    scopus 로고
    • Enhanced secretion of peroxidase from carrot hairy roots using polyethylene glycol
    • Kim Y.H., Kim J.H., Yoo Y.J. Enhanced secretion of peroxidase from carrot hairy roots using polyethylene glycol. J. Ferment. Bioeng. 83:1997;397-400
    • (1997) J. Ferment. Bioeng. , vol.83 , pp. 397-400
    • Kim, Y.H.1    Kim, J.H.2    Yoo, Y.J.3
  • 23
    • 0032573222 scopus 로고    scopus 로고
    • Enhanced peroxidase production by suspension culture of carrot compact callus aggregates
    • Xu J.F., Sun Y., Su Z.G. Enhanced peroxidase production by suspension culture of carrot compact callus aggregates. J. Biotechnol. 65:1998;203-208
    • (1998) J. Biotechnol. , vol.65 , pp. 203-208
    • Xu, J.F.1    Sun, Y.2    Su, Z.G.3
  • 24
    • 0036852851 scopus 로고    scopus 로고
    • Purification and substrate specificity of peroxidase from sweet potato tubers
    • Leon J.C., Alpeeva I.S., Chubar T.A. Purification and substrate specificity of peroxidase from sweet potato tubers. Plant Sci. 163:2002;1011-1019
    • (2002) Plant Sci. , vol.163 , pp. 1011-1019
    • Leon, J.C.1    Alpeeva, I.S.2    Chubar, T.A.3
  • 26
    • 0003518480 scopus 로고
    • Chichester, Wiley
    • I.H. Segel, Enzymes Kinetics, Chichester, Wiley, 1975, pp. 64-71, 830-831.
    • (1975) Enzymes Kinetics , pp. 64-71
    • Segel, I.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.