메뉴 건너뛰기




Volumn 67, Issue , 2012, Pages 28-34

Immobilization of soybean peroxidase on aminopropyl glass beads: Structural and kinetic studies

Author keywords

Enzyme activity; Heterogenous biocatalysis; Immobilization; Immobilized enzymes; Peroxidase; Soybean

Indexed keywords

AMINOPROPYL; BIOCATALYSIS; CATALYTIC SITES; CONSECUTIVE REACTION; DEGRADATION OF POLLUTANTS; EXPERIMENTAL TECHNIQUES; GLASS BEAD; HIGH RESISTANCE; IMMOBILIZATION PROCESS; IMMOBILIZED ENZYME; INITIAL ACTIVITY; KINETIC MEASUREMENT; KINETIC STUDY; OXIDATIVE REACTION; PEROXIDASE; SOYBEAN; SOYBEAN PEROXIDASE; SPECIFIC ACTIVITY; STABILITY PROPERTIES; THERMAL DENATURATIONS; UV VISIBLE SPECTROSCOPY;

EID: 84861908080     PISSN: 1369703X     EISSN: 1873295X     Source Type: Journal    
DOI: 10.1016/j.bej.2012.05.002     Document Type: Article
Times cited : (18)

References (42)
  • 1
    • 84864741204 scopus 로고    scopus 로고
    • Enzymes, Industrial (overview)
    • Academic Press, Oxford, S. Moselio (Ed.)
    • Saha B.C., Jordan D.B., Bothast R.J. Enzymes, Industrial (overview). Encyclopedia of Microbiology 2009, 281-294. Academic Press, Oxford. third ed. S. Moselio (Ed.).
    • (2009) Encyclopedia of Microbiology , pp. 281-294
    • Saha, B.C.1    Jordan, D.B.2    Bothast, R.J.3
  • 3
    • 0035826279 scopus 로고    scopus 로고
    • Modulation of lipase properties in macro-aqueous systems by controlled enzyme immobilization: enantioselective hydrolysis of a chiral ester by immobilized Pseudomonas lipase
    • Fernandez-Lorente G., Terreni M., Mateo C., Bastida A., Fernandez-Lafuente R., Dalmases P., Huguet J., Guisan J.M. Modulation of lipase properties in macro-aqueous systems by controlled enzyme immobilization: enantioselective hydrolysis of a chiral ester by immobilized Pseudomonas lipase. Enzyme Microb. Technol. 2001, 28:389-396.
    • (2001) Enzyme Microb. Technol. , vol.28 , pp. 389-396
    • Fernandez-Lorente, G.1    Terreni, M.2    Mateo, C.3    Bastida, A.4    Fernandez-Lafuente, R.5    Dalmases, P.6    Huguet, J.7    Guisan, J.M.8
  • 4
    • 9644262749 scopus 로고    scopus 로고
    • Application of immobilized horseradish peroxidase for the removal of p-chlorophenol from aqueous solution
    • Lai Y.-C., Lin S.-C. Application of immobilized horseradish peroxidase for the removal of p-chlorophenol from aqueous solution. Process Biochem. 2005, 40:1167-1174.
    • (2005) Process Biochem. , vol.40 , pp. 1167-1174
    • Lai, Y.-C.1    Lin, S.-C.2
  • 6
    • 67649780829 scopus 로고    scopus 로고
    • Comparison of alternative treatments for 4-chlorophenol removal from aqueous solutions: use of free and immobilized soybean peroxidase and KrCl excilamp
    • Gómez M., Matafonova G., Gómez J.L., Batoev V., Christofi N. Comparison of alternative treatments for 4-chlorophenol removal from aqueous solutions: use of free and immobilized soybean peroxidase and KrCl excilamp. J. Hazard. Mater. 2009, 169:46-51.
    • (2009) J. Hazard. Mater. , vol.169 , pp. 46-51
    • Gómez, M.1    Matafonova, G.2    Gómez, J.L.3    Batoev, V.4    Christofi, N.5
  • 7
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases
    • Welinder K.G. Superfamily of plant, fungal and bacterial peroxidases. Curr. Opin. Struct. Biol. 1992, 2:388-393.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 388-393
    • Welinder, K.G.1
  • 8
    • 0035100890 scopus 로고    scopus 로고
    • Structure of soybean seed coat peroxidase: a plant peroxidase with unusual stability and haem-apoprotein interactions
    • Henriksen A., Mirza O., Indiani C., Teilum K., Smulevich G., Welinder K.G., Gajhede M. Structure of soybean seed coat peroxidase: a plant peroxidase with unusual stability and haem-apoprotein interactions. Protein Sci. 2001, 10:108-115.
    • (2001) Protein Sci. , vol.10 , pp. 108-115
    • Henriksen, A.1    Mirza, O.2    Indiani, C.3    Teilum, K.4    Smulevich, G.5    Welinder, K.G.6    Gajhede, M.7
  • 10
    • 0035830761 scopus 로고    scopus 로고
    • Reactions of soybean peroxidase and hydrogen peroxide pH 2. 4-12.0, and veratryl alcohol at pH 2.4
    • Nissum M., Schiødt C.B., Welinder K.G. Reactions of soybean peroxidase and hydrogen peroxide pH 2. 4-12.0, and veratryl alcohol at pH 2.4. Biochim. Biophys. Acta 2001, 1545:339-348.
    • (2001) Biochim. Biophys. Acta , vol.1545 , pp. 339-348
    • Nissum, M.1    Schiødt, C.B.2    Welinder, K.G.3
  • 11
    • 0029842169 scopus 로고    scopus 로고
    • Unusual thermal stability of soybean peroxidase
    • McEldoon J.P., Dordick J.S. Unusual thermal stability of soybean peroxidase. Biotechnol. Prog. 1996, 12:555-558.
    • (1996) Biotechnol. Prog. , vol.12 , pp. 555-558
    • McEldoon, J.P.1    Dordick, J.S.2
  • 12
    • 0037162406 scopus 로고    scopus 로고
    • Thermal and conformational stability of seed coat soybean peroxidase
    • Kamal J.K.A., Behere D.V. Thermal and conformational stability of seed coat soybean peroxidase. Biochemistry 2002, 41:9034-9042.
    • (2002) Biochemistry , vol.41 , pp. 9034-9042
    • Kamal, J.K.A.1    Behere, D.V.2
  • 13
    • 33751301244 scopus 로고    scopus 로고
    • ESR spectroscopy investigation of the denaturation process of soybean peroxidase induced by guanidine hydrochloride, DMSO or heat
    • Boscolo B., Laurenti E., Ghibaudi E. ESR spectroscopy investigation of the denaturation process of soybean peroxidase induced by guanidine hydrochloride, DMSO or heat. Protein J. 2006, 25:379-390.
    • (2006) Protein J. , vol.25 , pp. 379-390
    • Boscolo, B.1    Laurenti, E.2    Ghibaudi, E.3
  • 14
    • 0032843986 scopus 로고    scopus 로고
    • Removal of phenolic compounds from synthetic wastewater using soybean peroxidase
    • Caza N., Bewtra J.K., Biswas N., Taylor K.E. Removal of phenolic compounds from synthetic wastewater using soybean peroxidase. Water Res. 1999, 33:3012-3018.
    • (1999) Water Res. , vol.33 , pp. 3012-3018
    • Caza, N.1    Bewtra, J.K.2    Biswas, N.3    Taylor, K.E.4
  • 15
    • 33645735766 scopus 로고    scopus 로고
    • Comparison of commercial peroxidases for removing phenol from water solutions
    • Bódalo A., Gómez J.L., Gómez E., Bastida J., Máximo M.F. Comparison of commercial peroxidases for removing phenol from water solutions. Chemosphere 2006, 63:626-632.
    • (2006) Chemosphere , vol.63 , pp. 626-632
    • Bódalo, A.1    Gómez, J.L.2    Gómez, E.3    Bastida, J.4    Máximo, M.F.5
  • 16
    • 55949132665 scopus 로고    scopus 로고
    • A comparative study of free and immobilized soybean and horseradish peroxidases for 4-chlorophenol removal: protective effects of immobilization
    • Bódalo A., Bastida J., Máximo M., Montiel M., Gómez M., Murcia M. A comparative study of free and immobilized soybean and horseradish peroxidases for 4-chlorophenol removal: protective effects of immobilization. Bioprocess Biosyst. Eng. 2008, 31:587-593.
    • (2008) Bioprocess Biosyst. Eng. , vol.31 , pp. 587-593
    • Bódalo, A.1    Bastida, J.2    Máximo, M.3    Montiel, M.4    Gómez, M.5    Murcia, M.6
  • 17
    • 67449132600 scopus 로고    scopus 로고
    • Comparison of soybean peroxidase with laccase in the removal of phenol from synthetic and refinery wastewater samples
    • Steevensz A., Al-Ansari M.M., Taylor K.E., Bewtra J.K., Biswas N. Comparison of soybean peroxidase with laccase in the removal of phenol from synthetic and refinery wastewater samples. J. Chem. Technol. Biotechnol. 2009, 84:761-769.
    • (2009) J. Chem. Technol. Biotechnol. , vol.84 , pp. 761-769
    • Steevensz, A.1    Al-Ansari, M.M.2    Taylor, K.E.3    Bewtra, J.K.4    Biswas, N.5
  • 18
    • 23944514507 scopus 로고    scopus 로고
    • Enzymatic biobleaching of two recalcitrant paper dyes with horseradish and soybean peroxidase
    • Knutson K., Kirzan S., Ragauskas A. Enzymatic biobleaching of two recalcitrant paper dyes with horseradish and soybean peroxidase. Biotechnol. Lett. 2005, 27:753-758.
    • (2005) Biotechnol. Lett. , vol.27 , pp. 753-758
    • Knutson, K.1    Kirzan, S.2    Ragauskas, A.3
  • 20
    • 0031973583 scopus 로고    scopus 로고
    • Effluent treatment of pulp and paper, and textile industries using immobilised horseradish peroxidase
    • Peralta-Zamora P., Esposito E., Pelegrini R., Groto R., Reyes J., Durán N. Effluent treatment of pulp and paper, and textile industries using immobilised horseradish peroxidase. Environ. Technol. 1998, 19:55-63.
    • (1998) Environ. Technol. , vol.19 , pp. 55-63
    • Peralta-Zamora, P.1    Esposito, E.2    Pelegrini, R.3    Groto, R.4    Reyes, J.5    Durán, N.6
  • 21
    • 1942456730 scopus 로고    scopus 로고
    • Properties of horseradish peroxidase immobilised onto polyaniline
    • Fernandes K.F., Lima C.S., Lopes F.M., Collins C.H. Properties of horseradish peroxidase immobilised onto polyaniline. Process Biochem. 2004, 39:957-962.
    • (2004) Process Biochem. , vol.39 , pp. 957-962
    • Fernandes, K.F.1    Lima, C.S.2    Lopes, F.M.3    Collins, C.H.4
  • 22
    • 77549088939 scopus 로고    scopus 로고
    • Immobilization of horseradish peroxidase on modified chitosan beads
    • Monier M., Ayad D.M., Wei Y., Sarhan A.A. Immobilization of horseradish peroxidase on modified chitosan beads. Int. J. Biol. Macromol. 2010, 46:324-330.
    • (2010) Int. J. Biol. Macromol. , vol.46 , pp. 324-330
    • Monier, M.1    Ayad, D.M.2    Wei, Y.3    Sarhan, A.A.4
  • 23
    • 0037334650 scopus 로고    scopus 로고
    • Activity, stability and conformational flexibility of seed coat soybean peroxidase
    • Kamal J.K.A., Behere D.V. Activity, stability and conformational flexibility of seed coat soybean peroxidase. J. Inorg. Biochem. 2003, 94:236-242.
    • (2003) J. Inorg. Biochem. , vol.94 , pp. 236-242
    • Kamal, J.K.A.1    Behere, D.V.2
  • 24
  • 25
    • 0342445773 scopus 로고
    • The determination of pore volume and area distributions in porous substances. I. Computations from nitrogen isotherms
    • Barrett E.P., Joyner L.G., Halenda P.P. The determination of pore volume and area distributions in porous substances. I. Computations from nitrogen isotherms. J. Am. Chem. Soc. 1951, 73:373-380.
    • (1951) J. Am. Chem. Soc. , vol.73 , pp. 373-380
    • Barrett, E.P.1    Joyner, L.G.2    Halenda, P.P.3
  • 26
    • 0020199907 scopus 로고
    • Observations on the use of guaiacol and 2,2'-azino-di(3-ethylbenzthiazoline-6-sulfonic acid) as peroxidase substrates
    • Mäkinen K.K., Tenovuo J. Observations on the use of guaiacol and 2,2'-azino-di(3-ethylbenzthiazoline-6-sulfonic acid) as peroxidase substrates. Anal. Biochem. 1982, 126:100-108.
    • (1982) Anal. Biochem. , vol.126 , pp. 100-108
    • Mäkinen, K.K.1    Tenovuo, J.2
  • 27
    • 49149140663 scopus 로고
    • A sensitive and versatile chromogenic assay for peroxidase and peroxidase-coupled reactions
    • Ngo T.T., Lenhoff H.M. A sensitive and versatile chromogenic assay for peroxidase and peroxidase-coupled reactions. Anal. Biochem. 1980, 105:389-397.
    • (1980) Anal. Biochem. , vol.105 , pp. 389-397
    • Ngo, T.T.1    Lenhoff, H.M.2
  • 33
    • 84939775172 scopus 로고
    • Reporting physisorption data for gas/solid systems with special reference to the determination of surface area and porosity
    • (Recommendations 1984)
    • Sing K.S.W. Reporting physisorption data for gas/solid systems with special reference to the determination of surface area and porosity. Pure Appl. Chem. 1985, 57:603-619. (Recommendations 1984).
    • (1985) Pure Appl. Chem. , vol.57 , pp. 603-619
    • Sing, K.S.W.1
  • 34
    • 0034732640 scopus 로고    scopus 로고
    • Effect of low temperature on soybean peroxidase: spectroscopic characterization of the quantum-mechanically admixed spin state
    • Indiani C., Feis A., Howes B.D., Marzocchi M.P., Smulevich G. Effect of low temperature on soybean peroxidase: spectroscopic characterization of the quantum-mechanically admixed spin state. J. Inorg. Biochem. 2000, 79:269-274.
    • (2000) J. Inorg. Biochem. , vol.79 , pp. 269-274
    • Indiani, C.1    Feis, A.2    Howes, B.D.3    Marzocchi, M.P.4    Smulevich, G.5
  • 35
    • 0002791918 scopus 로고
    • Electron paramagnetic resonance of hemoproteins
    • Wesley Publishing Company, Reading, A.B.P. Lever, H.B. Gray (Eds.)
    • Palmer G. Electron paramagnetic resonance of hemoproteins. Iron Porphyrins, Part 2, Addison 1983, 45-88. Wesley Publishing Company, Reading. A.B.P. Lever, H.B. Gray (Eds.).
    • (1983) Iron Porphyrins, Part 2, Addison , pp. 45-88
    • Palmer, G.1
  • 37
    • 0034307247 scopus 로고    scopus 로고
    • Ionic strength and pH effect on the Fe(III)-imidazolate bond in the heme pocket of horseradish peroxidase: an EPR and UV-visible combined approach
    • Laurenti E., Suriano G., Ghibaudi E.M., Ferrari R.P. Ionic strength and pH effect on the Fe(III)-imidazolate bond in the heme pocket of horseradish peroxidase: an EPR and UV-visible combined approach. J. Inorg. Biochem. 2000, 81:259-266.
    • (2000) J. Inorg. Biochem. , vol.81 , pp. 259-266
    • Laurenti, E.1    Suriano, G.2    Ghibaudi, E.M.3    Ferrari, R.P.4
  • 38
    • 0030939023 scopus 로고    scopus 로고
    • Kinetic studies on the oxidation of phenols by the horseradish peroxidase compound II
    • Patel P.K., Mondal M.S., Modi S., Behere D.V. Kinetic studies on the oxidation of phenols by the horseradish peroxidase compound II. Biochim. Biophys. Acta 1997, 1339:79-87.
    • (1997) Biochim. Biophys. Acta , vol.1339 , pp. 79-87
    • Patel, P.K.1    Mondal, M.S.2    Modi, S.3    Behere, D.V.4
  • 39
    • 0037900138 scopus 로고    scopus 로고
    • Oxidation of 2,4-dichlorophenol catalyzed by horseradish peroxidase: characterization of the reaction mechanism by UV-visible spectroscopy and mass spectrometry
    • Laurenti E., Ghibaudi E., Ardissone S., Ferrari R.P. Oxidation of 2,4-dichlorophenol catalyzed by horseradish peroxidase: characterization of the reaction mechanism by UV-visible spectroscopy and mass spectrometry. J. Inorg. Biochem. 2003, 95:171-176.
    • (2003) J. Inorg. Biochem. , vol.95 , pp. 171-176
    • Laurenti, E.1    Ghibaudi, E.2    Ardissone, S.3    Ferrari, R.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.