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Volumn 34, Issue 3, 2013, Pages 321-326

Bromofhenol blue discoloration using peroxidase immobilized on highly activated corncob powder;Descoloração de azul de bromofenol utilizando peroxidase imobilizada em pó de sabugo de milho altamente ativado

Author keywords

Aminated enzymes; Corncob powder; Multipoint immobilization of enzymes; Peroxidases

Indexed keywords

BROMOPHENOL BLUE; PEROXIDASE;

EID: 84887545592     PISSN: 18084532     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (8)

References (37)
  • 1
    • 0343293895 scopus 로고    scopus 로고
    • The effect of gel composition on the adsorption of invertase on poly (acrylamide/maleic acid) hydrogels
    • Arslan F, Tümtürk H, Çaykara T, Sen M, Güven O. The effect of gel composition on the adsorption of invertase on poly (acrylamide/maleic acid) hydrogels. Food Chem. 2000;70:33-8.
    • (2000) Food Chem , vol.70 , pp. 33-38
    • Arslan, F.1    Tümtürk, H.2    Çaykara, T.3    Sen, M.4    Güven, O.5
  • 2
    • 0024677047 scopus 로고
    • Stabilization of enzymes by multipoint covalent attachment to agarose-aldehide gels. Borohydrite reduction of trypsin-agarose derivates
    • Blanco RM, Guisán JM. Stabilization of enzymes by multipoint covalent attachment to agarose-aldehide gels. Borohydrite reduction of trypsin-agarose derivates. Enzyme Microb Technol. 1989;11:360-6.
    • (1989) Enzyme Microb Technol , vol.11 , pp. 360-366
    • Blanco, R.M.1    Guisán, J.M.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976;72:248-54.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0025198193 scopus 로고
    • Decolorization of phenolic effluents by soluble and immobilized phenol oxidases
    • Davis S, Burns RG. Decolorization of phenolic effluents by soluble and immobilized phenol oxidases. Applied Microbiol Biotechnol.1990;32:721-6.
    • (1990) Applied Microbiol Biotechnol , vol.32 , pp. 721-726
    • Davis, S.1    Burns, R.G.2
  • 5
    • 0037257813 scopus 로고    scopus 로고
    • Renoval of aqueous phenolic compounds from a model system by oxidative polymerization with turnip (Brassica napus L var purple top white globe) peroxidase
    • Duarte-Vázquez MA, Ortega-Tovar MA, García-Almendarez BE and Regalado C. Renoval of aqueous phenolic compounds from a model system by oxidative polymerization with turnip (Brassica napus L var purple top white globe) peroxidase. J Chem Technol Biotechnol. 2003;78:42-7.
    • (2003) J Chem Technol Biotechnol , vol.78 , pp. 42-47
    • Duarte-Vázquez, M.A.1    Ortega-Tovar, M.A.2    García-Almendarez, B.E.3    Regalado, C.4
  • 6
    • 0000805517 scopus 로고
    • On the function and mechanism of action of peroxidases
    • Dunford HB, Stillman JS. On the function and mechanism of action of peroxidases. Coordin Chem Rev. 1976;19:187-251.
    • (1976) Coordin Chem Rev , vol.19 , pp. 187-251
    • Dunford, H.B.1    Stillman, J.S.2
  • 7
    • 0025743439 scopus 로고
    • Decolorization of Kraft effluent by free and immobilized lignin peroxidases and horseradish peroxidase
    • Ferrer I, Dezotti M, Durán N. Decolorization of Kraft effluent by free and immobilized lignin peroxidases and horseradish peroxidase. Biotechnol Lett. 1991;13:577-82.
    • (1991) Biotechnol Lett , vol.13 , pp. 577-582
    • Ferrer, I.1    Dezotti, M.2    Durán, N.3
  • 8
    • 0029311202 scopus 로고
    • Strategies for enzyme satabilization by intramolecular crosslinking with bifunctional reagents
    • Fernandez-Lafuente R, Rosell CM, Rodriguez V, Guisan JM. Strategies for enzyme satabilization by intramolecular crosslinking with bifunctional reagents. Enzyme Microb Technol. 1995 17(6):517-50.
    • (1995) Enzyme Microb Technol , vol.17 , Issue.6 , pp. 517-550
    • Fernandez-Lafuente, R.1    Rosell, C.M.2    Rodriguez, V.3    Guisan, J.M.4
  • 9
    • 0000005531 scopus 로고
    • Purification and developmental analysis of the major anionic peroxidases from the seed coat of Glysine max
    • Gillikin JW, Graham JS. Purification and developmental analysis of the major anionic peroxidases from the seed coat of Glysine max. Plant Physiol. 1991;96:214-20.
    • (1991) Plant Physiol , vol.96 , pp. 214-220
    • Gillikin, J.W.1    Graham, J.S.2
  • 11
    • 0024029957 scopus 로고
    • Aldehyde-agarose gels as activated supports for immobilization-stabilization of enzymes
    • Guisán JM. Aldehyde-agarose gels as activated supports for immobilization-stabilization of enzymes. Enzyme Microl Technol. 1988;10:375-82.
    • (1988) Enzyme Microl Technol , vol.10 , pp. 375-382
    • Guisán, J.M.1
  • 12
    • 0000287798 scopus 로고    scopus 로고
    • Immobilization of enzymes on glyoxyl agarose - Strategies for enzyme stabilization by multipoint attachment
    • In: Bickerstaff GF (editor), Totowa: Humana Press
    • Guisán JM, Bastida A, Blanco RM, Fernández-Lafuente R, García-Junceda E. Immobilization of enzymes on glyoxyl agarose - Strategies for enzyme stabilization by multipoint attachment. In: Bickerstaff GF (editor). Immobilization of enzymes and cells. Totowa: Humana Press; 1997. p. 277-87.
    • (1997) Immobilization of Enzymes and Cells , pp. 277-287
    • Guisán, J.M.1    Bastida, A.2    Blanco, R.M.3    Fernández-Lafuente, R.4    García-Junceda, E.5
  • 13
    • 79955048698 scopus 로고    scopus 로고
    • st century begins: An already solved problem or still an exciting challenge
    • In: Guisán JM (editor), Totowa: Humana Press
    • st century begins: an already solved problem or still an exciting challenge. In: Guisán JM (editor). Immobilization of Enzymes and Cells. Totowa: Humana Press; 2006. p. 1-13.
    • (2006) Immobilization of Enzymes and Cells , pp. 1-13
    • Guisán, J.M.1
  • 14
    • 0036261247 scopus 로고    scopus 로고
    • Optimization of soybean peroxidase treatment of 2, 4-dichlorephenol
    • Kennedy K, Alemany K, Warith M. Optimization of soybean peroxidase treatment of 2, 4-dichlorephenol. Water Res. 2002;28:149-58.
    • (2002) Water Res , vol.28 , pp. 149-158
    • Kennedy, K.1    Alemany, K.2    Warith, M.3
  • 15
    • 0033968970 scopus 로고    scopus 로고
    • Treatment of aqueous phenol with soybean peroxidase in the presence of polyethylene glycol
    • Kinsley C, Nicell JA. Treatment of aqueous phenol with soybean peroxidase in the presence of polyethylene glycol. Bioresource Technol. 2000;73:139-46.
    • (2000) Bioresource Technol , vol.73 , pp. 139-146
    • Kinsley, C.1    Nicell, J.A.2
  • 16
    • 0020620307 scopus 로고
    • Peroxidase catalyzed removal of phenoes from coal conversion waste waters
    • Klibanov AM, Tu TM, Scott KP. Peroxidase catalyzed removal of phenoes from coal conversion waste waters. Science. 1983;221:259-61.
    • (1983) Science , vol.221 , pp. 259-261
    • Klibanov, A.M.1    Tu, T.M.2    Scott, K.P.3
  • 17
  • 20
    • 4043069789 scopus 로고    scopus 로고
    • Immobilization of lactase from Kluyveromyces lactis greatly reduces the inhibition of promoted by glucose: Full hydrolysis of lactose in milk
    • Mateo C, Monti R, Pessela BC, Fuentes M, Torres R, Guisán JM, Fernández-Lafuente R. Immobilization of lactase from Kluyveromyces lactis greatly reduces the inhibition of promoted by glucose: full hydrolysis of lactose in milk. Biotechnol Prog. 2004;20:1259-62.
    • (2004) Biotechnol Prog , vol.20 , pp. 1259-1262
    • Mateo, C.1    Monti, R.2    Pessela, B.C.3    Fuentes, M.4    Torres, R.5    Guisán, J.M.6    Fernández-Lafuente, R.7
  • 21
    • 0029842169 scopus 로고    scopus 로고
    • Unusual thermal stability of soybean peroxidase
    • McEldoon JP, Dordick JS.Unusual thermal stability of soybean peroxidase. Biotechnol Prog. 1996;12:555-8.
    • (1996) Biotechnol Prog , vol.12 , pp. 555-558
    • McEldoon, J.P.1    Dordick, J.S.2
  • 23
    • 0026588636 scopus 로고
    • Phenol removal from aqueous solutions by peroxidase-catalyzed reaction using additives
    • Nakamoto S, Machida N. Phenol removal from aqueous solutions by peroxidase-catalyzed reaction using additives. Water Res. 1992;26:49-54.
    • (1992) Water Res , vol.26 , pp. 49-54
    • Nakamoto, S.1    Machida, N.2
  • 24
    • 0027692873 scopus 로고
    • Reactor development for peroxidases catalyzed polymerization and precipitation of phenols from wastewater
    • Nicell JA, Bewtra JK, Biswas N, Taylor E. Reactor development for peroxidases catalyzed polymerization and precipitation of phenols from wastewater. Water Res. 1993;27:1629-39.
    • (1993) Water Res , vol.27 , pp. 1629-1639
    • Nicell, J.A.1    Bewtra, J.K.2    Biswas, N.3    Taylor, E.4
  • 26
    • 1642489328 scopus 로고    scopus 로고
    • Enzyme stabilization: Recent experimental progress
    • Ó'Fágáin C. Enzyme stabilization: recent experimental progress. Enzyme Microb Technol. 2003;33:137-49.
    • (2003) Enzyme Microb Technol , vol.33 , pp. 137-149
    • Ó'Fágáin, C.1
  • 27
    • 81455159833 scopus 로고    scopus 로고
    • Screening of supports for Kluyveromyces marxianus var. bulgaricus inulinase immobilization
    • Paula FC, Cazetta ML, Monti R, Contiero J. Screening of supports for Kluyveromyces marxianus var. bulgaricus inulinase immobilization. Curr Trends Biotechnol Pharm. 2007;1:34-40.
    • (2007) Curr Trends Biotechnol Pharm , vol.1 , pp. 34-40
    • Paula, F.C.1    Cazetta, M.L.2    Monti, R.3    Contiero, J.4
  • 28
    • 46049103764 scopus 로고    scopus 로고
    • Sucrose hydrolysis by gelatin-immobilized inulinase from Kluyveromyces marxianus var.bulgaricus
    • Paula FC, Cazetta ML, Monti R, Contiero J. Sucrose hydrolysis by gelatin-immobilized inulinase from Kluyveromyces marxianus var.bulgaricus. Food Chem. 2008;111:691-95.
    • (2008) Food Chem , vol.111 , pp. 691-695
    • Paula, F.C.1    Cazetta, M.L.2    Monti, R.3    Contiero, J.4
  • 32
    • 0002265592 scopus 로고
    • Oxidoreductases
    • In: Reed G (editor), New York: Academic Press
    • Scott D. Oxidoreductases. In: Reed G (editor). Enzymes in food processing. New York: Academic Press; 1975. P. 219-54.
    • (1975) Enzymes In Food Processing , pp. 219-254
    • Scott, D.1
  • 35
    • 0343893703 scopus 로고    scopus 로고
    • Biosensor based on paraffin/graphite modified with sweet potato tissue for the determination of hydroquinone in cosmetic cream in organic phase
    • Vieira IC, Fatibello FO. Biosensor based on paraffin/graphite modified with sweet potato tissue for the determination of hydroquinone in cosmetic cream in organic phase. Talanta. 2000;52:681-9.
    • (2000) Talanta , vol.52 , pp. 681-689
    • Vieira, I.C.1    Fatibello, F.O.2
  • 36
    • 0346271723 scopus 로고    scopus 로고
    • Inmovilización de una peroxidasa de chayote [sechium edule (jacq.) sw] y su potencial aplicación en la remoción de sustancias fenólicas en aguas contaminadas
    • Villegas-Rosas MLO, Geissler G, Handal-Silva A, González-Vergara E. Inmovilización de una peroxidasa de chayote [sechium edule (jacq.) sw] y su potencial aplicación en la remoción de sustancias fenólicas en aguas contaminadas. Rev. Int. Contam. Ambient, 2003;19:73-81.
    • (2003) Rev. Int. Contam. Ambient , vol.19 , pp. 73-81
    • Villegas-Rosas, M.L.O.1    Geissler, G.2    Handal-Silva, A.3    González-Vergara, E.4
  • 37
    • 0032907135 scopus 로고    scopus 로고
    • Characterization of soybean peroxidase for the treatment of aqueous phenols
    • Wright H, Nicell A. Characterization of soybean peroxidase for the treatment of aqueous phenols. Bioresource Technol. 1999;70:69-79.
    • (1999) Bioresource Technol , vol.70 , pp. 69-79
    • Wright, H.1    Nicell, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.