메뉴 건너뛰기




Volumn 4, Issue 3, 2009, Pages 408-416

Adsorption of peroxidase on Celite 545 directly from ammonium sulfate fractionated white radish (Raphanus sativus) proteins

Author keywords

Celite; Cross linking; Immobilization; Peroxidase; White radish

Indexed keywords

CELITE; CROSS-LINKING; IMMOBILIZATION; PEROXIDASE; WHITE RADISH;

EID: 64549150657     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.200800261     Document Type: Article
Times cited : (9)

References (36)
  • 1
    • 0035178275 scopus 로고    scopus 로고
    • Remediation of dyes in textile effluents: A critical review on current treatment technologies with a proposed alternative
    • Robinson, T., McMullan. G., Marchant, R., Nigam, P., Remediation of dyes in textile effluents: A critical review on current treatment technologies with a proposed alternative. Biores. Technol. 2001, 77, 247-255.
    • (2001) Biores. Technol , vol.77 , pp. 247-255
    • Robinson, T.1    McMullan, G.2    Marchant, R.3    Nigam, P.4
  • 2
    • 33845226423 scopus 로고    scopus 로고
    • Comparative study of immobilized Trametes versicolor laccase on nanoparticles and kaolinite
    • Hu, X., Zhao, X., Hwang, H., Comparative study of immobilized Trametes versicolor laccase on nanoparticles and kaolinite. Chemosphere 2007, 66, 1618-1626.
    • (2007) Chemosphere , vol.66 , pp. 1618-1626
    • Hu, X.1    Zhao, X.2    Hwang, H.3
  • 3
    • 0034613457 scopus 로고    scopus 로고
    • Potential applications of oxidative enzymes and phenoloxidase-like compounds in wastewater and soil treatment: A review
    • Duran, N., Esposito, E., Potential applications of oxidative enzymes and phenoloxidase-like compounds in wastewater and soil treatment: A review. Appl. Catal. B: Environ. 2000, 28, 83-99.
    • (2000) Appl. Catal. B: Environ , vol.28 , pp. 83-99
    • Duran, N.1    Esposito, E.2
  • 4
    • 33750919303 scopus 로고    scopus 로고
    • Potential applications of the oxidoreductive enzymes in the decolorization and detoxification of textile and other synthetic dyes from polluted water: A review
    • Husain, Q., Potential applications of the oxidoreductive enzymes in the decolorization and detoxification of textile and other synthetic dyes from polluted water: A review. Crit. Rev. Biotechnol. 2006, 60, 201-221.
    • (2006) Crit. Rev. Biotechnol , vol.60 , pp. 201-221
    • Husain, Q.1
  • 5
    • 38549120258 scopus 로고    scopus 로고
    • Applications of redox mediators in the treatment of organic pollutants by using oxidoreductive enzymes: A review
    • Husain, M., Husain, Q., Applications of redox mediators in the treatment of organic pollutants by using oxidoreductive enzymes: A review. Crit. Rev. Environ. Sci. Technol. 2008, 38, 1-41.
    • (2008) Crit. Rev. Environ. Sci. Technol , vol.38 , pp. 1-41
    • Husain, M.1    Husain, Q.2
  • 6
    • 33745965506 scopus 로고    scopus 로고
    • Immobilization of peroxidases on glass beads: An improved alternative for phenol removal
    • Gomez, J. L., Bodalo, A., Gomez, E., Bastida, J. et al., Immobilization of peroxidases on glass beads: An improved alternative for phenol removal. Enzyme Microb.Technol. 2006, 39, 1016-1022.
    • (2006) Enzyme Microb.Technol , vol.39 , pp. 1016-1022
    • Gomez, J.L.1    Bodalo, A.2    Gomez, E.3    Bastida, J.4
  • 7
    • 1642489328 scopus 로고    scopus 로고
    • Enzyme stabilization-Recent experimental progress
    • Fagain, C. O., Enzyme stabilization-Recent experimental progress. Enzyme Microb.Technol. 2003, 33, 137-149.
    • (2003) Enzyme Microb.Technol , vol.33 , pp. 137-149
    • Fagain, C.O.1
  • 9
    • 33747097811 scopus 로고    scopus 로고
    • Chemically surface modified gel: An excellent enzyme-immobilization matrix for industrial processes
    • David, A. E., Wang, N. S., Yang, V. C., Yang, A. J., Chemically surface modified gel: An excellent enzyme-immobilization matrix for industrial processes. J. Biotechnol. 2006, 125, 395-407.
    • (2006) J. Biotechnol , vol.125 , pp. 395-407
    • David, A.E.1    Wang, N.S.2    Yang, V.C.3    Yang, A.J.4
  • 10
    • 28844472482 scopus 로고    scopus 로고
    • Adsorption of peroxidase on DEAE-cellulose directly from ammonium sulphate fractionated proteins of bitter gourd
    • Kulshrestha, Y., Husain, Q., Adsorption of peroxidase on DEAE-cellulose directly from ammonium sulphate fractionated proteins of bitter gourd. Enzyme Microb. Technol. 2006, 38, 470-477.
    • (2006) Enzyme Microb. Technol , vol.38 , pp. 470-477
    • Kulshrestha, Y.1    Husain, Q.2
  • 11
    • 0027439598 scopus 로고
    • Improved activity retention of enzymes deposited on solid supports
    • Wehtje, E., Adlercreutz, P., Mattiasson, B., Improved activity retention of enzymes deposited on solid supports. Biotechnol. Bioeng. 1993, 41, 171-178.
    • (1993) Biotechnol. Bioeng , vol.41 , pp. 171-178
    • Wehtje, E.1    Adlercreutz, P.2    Mattiasson, B.3
  • 12
    • 0034799448 scopus 로고    scopus 로고
    • Leontievsky, A., Myasoedova, N., Baskunov, B., Golovleva, L. et al., Transformation of 2, 4, 6-trichlorophenol by free and immobilized fungal laccase, Appl. Microb. Biotechnol. 2001, 57, 85-91.
    • Leontievsky, A., Myasoedova, N., Baskunov, B., Golovleva, L. et al., Transformation of 2, 4, 6-trichlorophenol by free and immobilized fungal laccase, Appl. Microb. Biotechnol. 2001, 57, 85-91.
  • 13
    • 0037381637 scopus 로고    scopus 로고
    • Immobilization of invertase on Celite and on polyacrylamide by an adsorption procedure
    • Mansour, E. H., Dawoud, F. M., Immobilization of invertase on Celite and on polyacrylamide by an adsorption procedure. J. Sci. Food Agri. 2003, 83, 446-450.
    • (2003) J. Sci. Food Agri , vol.83 , pp. 446-450
    • Mansour, E.H.1    Dawoud, F.M.2
  • 14
    • 33646144862 scopus 로고    scopus 로고
    • Direct immobilization of polyphenol oxidases on Celite 545 from ammonium sulphate fractionated proteins of potato (Solanum tuberosum)
    • Khan, A. A., Akhtar, S., Husain, Q., Direct immobilization of polyphenol oxidases on Celite 545 from ammonium sulphate fractionated proteins of potato (Solanum tuberosum). J. Mol. Catal. B: Enzym. 2006, 40, 58-63.
    • (2006) J. Mol. Catal. B: Enzym , vol.40 , pp. 58-63
    • Khan, A.A.1    Akhtar, S.2    Husain, Q.3
  • 15
    • 39249085619 scopus 로고    scopus 로고
    • Enzyme-catalyzed conversion of phenol by using immobilized horseradish peroxidase (HRP) in a membrane less electrochemical reactor
    • Cho, S. H., Shim, J., Yun, S. H., Moon, S. H., Enzyme-catalyzed conversion of phenol by using immobilized horseradish peroxidase (HRP) in a membrane less electrochemical reactor. Appl. Catal. A: General 2008, 337, 66-72.
    • (2008) Appl. Catal. A: General , vol.337 , pp. 66-72
    • Cho, S.H.1    Shim, J.2    Yun, S.H.3    Moon, S.H.4
  • 16
    • 0037010857 scopus 로고    scopus 로고
    • Applications of laccase and tyrosinases (phenoloxidases) immobilized on different supports: A review
    • Duran, N., Rosa, M. A., D'Annibale, A., Gianfreda, L., Applications of laccase and tyrosinases (phenoloxidases) immobilized on different supports: A review. Enzyme Microb. Technol. 2002, 31, 907-931.
    • (2002) Enzyme Microb. Technol , vol.31 , pp. 907-931
    • Duran, N.1    Rosa, M.A.2    D'Annibale, A.3    Gianfreda, L.4
  • 17
    • 34249824600 scopus 로고    scopus 로고
    • Fungal laccase: Copper induction, semi-purification, immobilization, phenolic effluent treatment and electrochemical measurement
    • Cordi, L., Minussi, R. C., Freire, R. S., Duran, N., Fungal laccase: Copper induction, semi-purification, immobilization, phenolic effluent treatment and electrochemical measurement. Afr. J. Biotechnol. 2007, 6, 1255-1259.
    • (2007) Afr. J. Biotechnol , vol.6 , pp. 1255-1259
    • Cordi, L.1    Minussi, R.C.2    Freire, R.S.3    Duran, N.4
  • 18
    • 34347357384 scopus 로고    scopus 로고
    • Electron transfer reactivity and catalytic activity of structurally rigidized hemoglobin
    • Wang, J., Liang, Z., Wang, L., Fan, C., Li, G., Electron transfer reactivity and catalytic activity of structurally rigidized hemoglobin. Sens. Act. B 2007, 125, 17-21.
    • (2007) Sens. Act. B , vol.125 , pp. 17-21
    • Wang, J.1    Liang, Z.2    Wang, L.3    Fan, C.4    Li, G.5
  • 19
    • 0034333634 scopus 로고    scopus 로고
    • Lipase-catalyzed reaction in the packed-bed reactor with continuous extraction column to overcome a product inhibition
    • Jeong, S., Hwang, B.Y., Kim, J., Kim, B. G., Lipase-catalyzed reaction in the packed-bed reactor with continuous extraction column to overcome a product inhibition. J. Mol. Catal. B: Enzym. 2000, 10, 597-604.
    • (2000) J. Mol. Catal. B: Enzym , vol.10 , pp. 597-604
    • Jeong, S.1    Hwang, B.Y.2    Kim, J.3    Kim, B.G.4
  • 20
    • 34250695597 scopus 로고    scopus 로고
    • Degradation of azo dye by an electroenzymatic method using horseradish peroxidase immobilized on porous support
    • Shim, J., Kim, G.Y., Yeon, K. H., Cho, S. H. et al., Degradation of azo dye by an electroenzymatic method using horseradish peroxidase immobilized on porous support. Korean J. Chem. Eng. 2007, 24, 72-78.
    • (2007) Korean J. Chem. Eng , vol.24 , pp. 72-78
    • Shim, J.1    Kim, G.Y.2    Yeon, K.H.3    Cho, S.H.4
  • 22
    • 17744405761 scopus 로고    scopus 로고
    • Immobilization and characterization of ficin
    • Fadyloglu, S., Immobilization and characterization of ficin. Nahrung/ Food 2001, 45, 143-146.
    • (2001) Nahrung/ Food , vol.45 , pp. 143-146
    • Fadyloglu, S.1
  • 23
    • 12944275401 scopus 로고    scopus 로고
    • Lipase-catalyzed naproxen methyl ester hydrolysis in water saturated ionic liquid: Significantly enhanced enatioselectivity and stability
    • Xin, J.Y., Zhao, Y. J., Shi, Y. G., Xia, C. G., Li, S. B., Lipase-catalyzed naproxen methyl ester hydrolysis in water saturated ionic liquid: Significantly enhanced enatioselectivity and stability. World J. Microb. Biotechnol. 2005, 21, 193-199.
    • (2005) World J. Microb. Biotechnol , vol.21 , pp. 193-199
    • Xin, J.Y.1    Zhao, Y.J.2    Shi, Y.G.3    Xia, C.G.4    Li, S.B.5
  • 24
    • 0026591370 scopus 로고
    • How do organic solvents affect peroxidase structure and function
    • Ryu, K., Dorick, J., How do organic solvents affect peroxidase structure and function. Biochemistry 1992, 31, 2588-2598.
    • (1992) Biochemistry , vol.31 , pp. 2588-2598
    • Ryu, K.1    Dorick, J.2
  • 25
    • 0024297764 scopus 로고
    • Mechanism-based inactivation of horseradish peroxidase by sodium azide: Formation of meso-azidoprotoporphyrin IX
    • Ortiz de Montellano, P. R., David, S. K., Ator, M. A., Tew, D., Mechanism-based inactivation of horseradish peroxidase by sodium azide: Formation of meso-azidoprotoporphyrin IX. Biochemistry 1988, 27, 5470-5476.
    • (1988) Biochemistry , vol.27 , pp. 5470-5476
    • Ortiz de Montellano, P.R.1    David, S.K.2    Ator, M.A.3    Tew, D.4
  • 26
    • 0031200793 scopus 로고    scopus 로고
    • Purification and characterization of a novel class III peroxidase isoenzyme from tea leaves
    • Kvaratskhelia, M., Winkel, C., Thorneley, R. N. F., Purification and characterization of a novel class III peroxidase isoenzyme from tea leaves. Plant Physiol. 1997, 114, 1237-1245.
    • (1997) Plant Physiol , vol.114 , pp. 1237-1245
    • Kvaratskhelia, M.1    Winkel, C.2    Thorneley, R.N.F.3
  • 27
    • 0031105669 scopus 로고    scopus 로고
    • Further studies on the inactivation by sodium azide of lignin peroxidase from Phanerochaete chrysosporium
    • Tatarko, M. Bumpus, J. A., Further studies on the inactivation by sodium azide of lignin peroxidase from Phanerochaete chrysosporium. Arch. Biochem. Biophys. 1997, 339, 200-209.
    • (1997) Arch. Biochem. Biophys , vol.339 , pp. 200-209
    • Tatarko, M.1    Bumpus, J.A.2
  • 28
    • 21344447936 scopus 로고    scopus 로고
    • Inhibition of laccase activity from Trametes versicolor by heavy metals and organic compounds
    • Lorenzo, M., Moldes, D., Rodriguez, C. S., Sanroma, M.A., Inhibition of laccase activity from Trametes versicolor by heavy metals and organic compounds. Chemosphere 2005, 60, 1124-1128.
    • (2005) Chemosphere , vol.60 , pp. 1124-1128
    • Lorenzo, M.1    Moldes, D.2    Rodriguez, C.S.3    Sanroma, M.A.4
  • 30
    • 33745902785 scopus 로고    scopus 로고
    • Effect of mercuric chloride on kinetic properties of horseradish peroxidase
    • Einollahi, N., Abbasi, S., Dashti, N., Vaezzadeh, F., Effect of mercuric chloride on kinetic properties of horseradish peroxidase. Iran. J. Public Health 2006, 35, 49-56.
    • (2006) Iran. J. Public Health , vol.35 , pp. 49-56
    • Einollahi, N.1    Abbasi, S.2    Dashti, N.3    Vaezzadeh, F.4
  • 31
    • 0034351361 scopus 로고    scopus 로고
    • Inhibitive determination of mercury and other metal ions by potentiometric urea biosensor
    • vel Krawczyk, T. K., Moszczynska, M., Trojanowicz, M., Inhibitive determination of mercury and other metal ions by potentiometric urea biosensor. Biosens. Bioelectron. 2000, 15, 681-691.
    • (2000) Biosens. Bioelectron , vol.15 , pp. 681-691
    • vel Krawczyk, T.K.1    Moszczynska, M.2    Trojanowicz, M.3
  • 32
    • 33644985358 scopus 로고    scopus 로고
    • Effect of mercury (II) traces on catalytic activity of peanut and horseradish peroxidases
    • Bagirova, N. A., Muginova, S. V., Shekhovtsova, T. N., Gazaryan, I. G., Van Huystee, R. B., Effect of mercury (II) traces on catalytic activity of peanut and horseradish peroxidases. Anal. Lett. 2006, 39, 521-541.
    • (2006) Anal. Lett , vol.39 , pp. 521-541
    • Bagirova, N.A.1    Muginova, S.V.2    Shekhovtsova, T.N.3    Gazaryan, I.G.4    Van Huystee, R.B.5
  • 33
    • 0032472347 scopus 로고    scopus 로고
    • Preparation and characterization of urease bound on crosslinked poly (vinyl alcohol)
    • Rejikumar, S., Devi, S., Preparation and characterization of urease bound on crosslinked poly (vinyl alcohol). J. Mol. Catal. B: Enzym. 1998, 4, 61-66.
    • (1998) J. Mol. Catal. B: Enzym , vol.4 , pp. 61-66
    • Rejikumar, S.1    Devi, S.2
  • 34
    • 1942440453 scopus 로고    scopus 로고
    • Preparation of a highly stable, very active and high-yield multilayered assembly of glucose oxidase using carbohydrate-specific polyclonal antibodies
    • Jan, U., Husain, Q., Preparation of a highly stable, very active and high-yield multilayered assembly of glucose oxidase using carbohydrate-specific polyclonal antibodies. Biotechnol. Appl. Biochem. 2004, 39, 233-239.
    • (2004) Biotechnol. Appl. Biochem , vol.39 , pp. 233-239
    • Jan, U.1    Husain, Q.2
  • 35
    • 33644614404 scopus 로고    scopus 로고
    • Enzyme immobilization: The state of art in biotechnology
    • Norouzian, D., Enzyme immobilization: The state of art in biotechnology. Iran. J. Biotechnol. 2003, 1, 197-206.
    • (2003) Iran. J. Biotechnol , vol.1 , pp. 197-206
    • Norouzian, D.1
  • 36
    • 0011040481 scopus 로고    scopus 로고
    • Microcapsules of alginate-chitosan. II: A study of capsule stability and permeability
    • Gaserod, O., Sannes, A., Skjak-BraeK, G., Microcapsules of alginate-chitosan. II: A study of capsule stability and permeability. Biomaterials 1999, 20, 773-783.
    • (1999) Biomaterials , vol.20 , pp. 773-783
    • Gaserod, O.1    Sannes, A.2    Skjak-BraeK, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.