메뉴 건너뛰기




Volumn 27, Issue 5, 2011, Pages 1433-1441

Assembly of horseradish peroxidase within supported cationic bilayers

Author keywords

Catalytic activity; Dioctadecyldimethylammonium bromide; Horseradish peroxidase; Particles; Supported cationic bilayers

Indexed keywords

BI-LAYER; BIOTECHNOLOGICAL APPLICATIONS; DEPOSITED LAYER; DIOCTADECYL DIMETHYLAMMONIUM BROMIDES; HORSE-RADISH PEROXIDASE; IMMOBILIZED ENZYME; IN-SITU ELLIPSOMETRY; MEAN DIAMETER; ON-WAFER; POLYSTYRENE MICRO-SPHERE; PRODUCT APPEARANCE; SPECTROPHOTOMETRIC DETERMINATION; SUPERNATANTS;

EID: 80053900096     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.640     Document Type: Article
Times cited : (4)

References (42)
  • 2
    • 0034826741 scopus 로고    scopus 로고
    • Enzymes inside lipid vesicles: preparation, reactivity and applications
    • Walde P, Ichikawa S. Enzymes inside lipid vesicles: preparation, reactivity and applications. Biomol Eng. 2001; 18: 143-77.
    • (2001) Biomol Eng , vol.18 , pp. 143-177
    • Walde, P.1    Ichikawa, S.2
  • 3
    • 70349929705 scopus 로고    scopus 로고
    • Vesicles as soft templates for the enzymatic polymerization of aniline
    • Guo Z, Ruegger H, Kissner R, Ishikawa T, Willeke M, Walde P. Vesicles as soft templates for the enzymatic polymerization of aniline. Langmuir. 2009; 25: 11390-11405.
    • (2009) Langmuir , vol.25 , pp. 11390-11405
    • Guo, Z.1    Ruegger, H.2    Kissner, R.3    Ishikawa, T.4    Willeke, M.5    Walde, P.6
  • 4
    • 45149113100 scopus 로고    scopus 로고
    • Liposomal encapsulation of yeast alcohol dehydrogenase with cofactor for stabilization of the enzyme structure and activity
    • Yoshimoto M, Sato M, Yoshimoto N, Nakao K. Liposomal encapsulation of yeast alcohol dehydrogenase with cofactor for stabilization of the enzyme structure and activity. Biotechnol Prog. 2008; 24: 576-582.
    • (2008) Biotechnol Prog , vol.24 , pp. 576-582
    • Yoshimoto, M.1    Sato, M.2    Yoshimoto, N.3    Nakao, K.4
  • 5
    • 27144462716 scopus 로고    scopus 로고
    • pH-dependent interaction of cytochrome c with mitochondrial mimetic membranes: the role of an array of positively charged amino acids
    • Kawai C, Prado, FM, Nunes GLC, DiMascio P, Carmona-Ribeiro AM, Nantes IL. pH-dependent interaction of cytochrome c with mitochondrial mimetic membranes: the role of an array of positively charged amino acids. J Biol Chem. 2005; 280: 34709-34717.
    • (2005) J Biol Chem , vol.280 , pp. 34709-34717
    • Kawai, C.1    Prado, F.M.2    Nunes, G.L.C.3    DiMascio, P.4    Carmona-Ribeiro, A.M.5    Nantes, I.L.6
  • 6
    • 21544475262 scopus 로고    scopus 로고
    • Involvement of phospholipid, biomembrane integrity, and NO peroxidase activity in the NO catabolism by cytochrome c oxidase
    • Chen YR, Chen CL, Liu X, He G, Zweier JL. Involvement of phospholipid, biomembrane integrity, and NO peroxidase activity in the NO catabolism by cytochrome c oxidase. Arch Biochem Biophys. 2005; 439: 200-210.
    • (2005) Arch Biochem Biophys , vol.439 , pp. 200-210
    • Chen, Y.R.1    Chen, C.L.2    Liu, X.3    He, G.4    Zweier, J.L.5
  • 7
    • 79952197831 scopus 로고    scopus 로고
    • Stabilization of enzymes through encapsulation in liposomes
    • Yoshimoto M. Stabilization of enzymes through encapsulation in liposomes. Methods Mol Biol. 2011; 679: 9-18.
    • (2011) Methods Mol Biol , vol.679 , pp. 9-18
    • Yoshimoto, M.1
  • 8
    • 33745932472 scopus 로고    scopus 로고
    • Horseradish and soybean peroxidases: comparable tools for alternative niches?
    • Ryan BJ, Carolan N, O'Fagain, C. Horseradish and soybean peroxidases: comparable tools for alternative niches? Trends Biotechnol. 2006; 24: 355-363.
    • (2006) Trends Biotechnol , vol.24 , pp. 355-363
    • Ryan, B.J.1    Carolan, N.2    O'Fagain, C.3
  • 9
    • 0033192422 scopus 로고    scopus 로고
    • Identification of polar toxicants in industrial wastewaters using toxicity-based fractionation with liquid chromatography/mass spectrometry
    • Castillo M, Barcelo D. Identification of polar toxicants in industrial wastewaters using toxicity-based fractionation with liquid chromatography/mass spectrometry. Anal Chem. 1999; 71: 3769-3776.
    • (1999) Anal Chem , vol.71 , pp. 3769-3776
    • Castillo, M.1    Barcelo, D.2
  • 10
    • 33947144753 scopus 로고    scopus 로고
    • Immobilized horseradish peroxidase as a reusable catalyst for emulsion polymerization
    • Naves AF, Carmona-Ribeiro AM, Petri DFS. Immobilized horseradish peroxidase as a reusable catalyst for emulsion polymerization. Langmuir. 2007; 23: 1981-1987.
    • (2007) Langmuir , vol.23 , pp. 1981-1987
    • Naves, A.F.1    Carmona-Ribeiro, A.M.2    Petri, D.F.S.3
  • 12
    • 0033230735 scopus 로고    scopus 로고
    • Evaluation of 4-nitrophenol ELISA kit for assessing the origin of organic pollution in wastewater treatment works
    • Farrea M, Oubina A, Marco MP, Ginebreda A, Tirapu L, Barcelo D. Evaluation of 4-nitrophenol ELISA kit for assessing the origin of organic pollution in wastewater treatment works. Environ Sci Technol. 1999; 33: 3898-3904.
    • (1999) Environ Sci Technol , vol.33 , pp. 3898-3904
    • Farrea, M.1    Oubina, A.2    Marco, M.P.3    Ginebreda, A.4    Tirapu, L.5    Barcelo, D.6
  • 13
    • 22544476518 scopus 로고    scopus 로고
    • Soybean peroxidase-catalyzed oxidation of luminol by hydrogen peroxide
    • Alpeeva IS, Sakharov IY. Soybean peroxidase-catalyzed oxidation of luminol by hydrogen peroxide. J Agric Food Chem. 2005; 53: 5784-5788.
    • (2005) J Agric Food Chem , vol.53 , pp. 5784-5788
    • Alpeeva, I.S.1    Sakharov, I.Y.2
  • 16
    • 77951173603 scopus 로고    scopus 로고
    • Biomimetic Nanoparticles: preparation, characterization and biomedical Applications
    • Carmona-Ribeiro AM. Biomimetic Nanoparticles: preparation, characterization and biomedical Applications. Int J Nanomed. 2010; 5: 249-259.
    • (2010) Int J Nanomed , vol.5 , pp. 249-259
    • Carmona-Ribeiro, A.M.1
  • 17
  • 18
    • 0026831273 scopus 로고
    • Synthetic bilayer adsorption onto polystyrene microspheres
    • Carmona-Ribeiro AM, Midmore BR. Synthetic bilayer adsorption onto polystyrene microspheres. Langmuir. 1992; 8: 801-806.
    • (1992) Langmuir , vol.8 , pp. 801-806
    • Carmona-Ribeiro, A.M.1    Midmore, B.R.2
  • 19
    • 0037326367 scopus 로고    scopus 로고
    • The effect of synthetic lipids on solubilization and colloid stability of hydrophobic drugs
    • Pacheco LF, Carmona-Ribeiro AM. The effect of synthetic lipids on solubilization and colloid stability of hydrophobic drugs. J Colloid Interface Sci. 2003; 258: 146-154.
    • (2003) J Colloid Interface Sci , vol.258 , pp. 146-154
    • Pacheco, L.F.1    Carmona-Ribeiro, A.M.2
  • 20
    • 4143112271 scopus 로고    scopus 로고
    • Cationic bilayers on polymeric particles: effect of low NaCl concentration on surface coverage
    • Pereira EMA, Vieira DB, Carmona-Ribeiro AM. Cationic bilayers on polymeric particles: effect of low NaCl concentration on surface coverage. J Phys Chem B. 2004; 108: 11490-11495.
    • (2004) J Phys Chem B , vol.108 , pp. 11490-11495
    • Pereira, E.M.A.1    Vieira, D.B.2    Carmona-Ribeiro, A.M.3
  • 21
    • 33745798227 scopus 로고    scopus 로고
    • Adsorption of cationic lipid bilayer onto flat silicon wafers: the effect of ion nature and concentration
    • Pereira EMA, Petri DFS, Carmona-Ribeiro AM. Adsorption of cationic lipid bilayer onto flat silicon wafers: the effect of ion nature and concentration. J Phys Chem B. 2006; 110: 10070-10074.
    • (2006) J Phys Chem B , vol.110 , pp. 10070-10074
    • Pereira, E.M.A.1    Petri, D.F.S.2    Carmona-Ribeiro, A.M.3
  • 23
    • 0034635116 scopus 로고    scopus 로고
    • Structural and conformational stability of horseradish peroxidase: effect of temperature and pH
    • Chattopadhyay K, Mazumdar S. Structural and conformational stability of horseradish peroxidase: effect of temperature and pH. Biochemistry. 2000; 39: 263-270.
    • (2000) Biochemistry , vol.39 , pp. 263-270
    • Chattopadhyay, K.1    Mazumdar, S.2
  • 24
    • 0037072992 scopus 로고    scopus 로고
    • Oxidation of ABTS by hydrogen peroxide catalyzed by horseradish peroxidase encapsulated into sol-gel glass. Effects of glass matrix on reactivity
    • Kadnikova EN, Kostic NM. Oxidation of ABTS by hydrogen peroxide catalyzed by horseradish peroxidase encapsulated into sol-gel glass. Effects of glass matrix on reactivity. J Mol Catal B- Enzym. 2002; 18: 39-48.
    • (2002) J Mol Catal B- Enzym , vol.18 , pp. 39-48
    • Kadnikova, E.N.1    Kostic, N.M.2
  • 26
    • 0000091363 scopus 로고
    • A simple and accurate method for determination of chloride in biological fluids
    • Schales O, Schales SS. A simple and accurate method for determination of chloride in biological fluids. J Biol Chem. 1941; 140: 879-884.
    • (1941) J Biol Chem , vol.140 , pp. 879-884
    • Schales, O.1    Schales, S.S.2
  • 29
    • 0016425962 scopus 로고
    • The steady state kinetics of peroxidase with 2,2' azino-di(3 ethylbenzthiazoline-6-sulphonic acid) as chromogen
    • Childs RE, Bardsley WG. The steady state kinetics of peroxidase with 2, 2' azino-di(3 ethylbenzthiazoline-6-sulphonic acid) as chromogen. Biochem. J. 1975; 145: 93-103.
    • (1975) Biochem. J , vol.145 , pp. 93-103
    • Childs, R.E.1    Bardsley, W.G.2
  • 31
    • 68949190997 scopus 로고    scopus 로고
    • Adsorption and inactivation behavior of horseradish peroxidase on cellulosic fiber surfaces
    • Di Risio S, Yan N. Adsorption and inactivation behavior of horseradish peroxidase on cellulosic fiber surfaces. J Colloid Interface Sci. 2009; 338: 410-419.
    • (2009) J Colloid Interface Sci , vol.338 , pp. 410-419
    • Di Risio, S.1    Yan, N.2
  • 32
    • 0035893794 scopus 로고    scopus 로고
    • Synthetic bilayer fragments for solubilization of amphotericin B
    • Vieira DB, Carmona-Ribeiro AM. Synthetic bilayer fragments for solubilization of amphotericin B. J Colloid Interface Sci. 2001; 244: 427-431.
    • (2001) J Colloid Interface Sci , vol.244 , pp. 427-431
    • Vieira, D.B.1    Carmona-Ribeiro, A.M.2
  • 33
    • 0141741201 scopus 로고    scopus 로고
    • In vivo activity of a novel amphotericin B formulation with cationic bilayer fragments
    • Lincopan N, Mamizuka EM, Carmona-Ribeiro AM. In vivo activity of a novel amphotericin B formulation with cationic bilayer fragments. J Antimicrobial Chemother. 2003; 52: 412-418.
    • (2003) J Antimicrobial Chemother , vol.52 , pp. 412-418
    • Lincopan, N.1    Mamizuka, E.M.2    Carmona-Ribeiro, A.M.3
  • 34
    • 52149087451 scopus 로고    scopus 로고
    • Enhanced activity of horseradish peroxidase in Langmuir-Blodgett films of phospholipids
    • Schmidt TF, Caseli L, Vitala T, Oliveira ON Jr. Enhanced activity of horseradish peroxidase in Langmuir-Blodgett films of phospholipids. Biochim Biophys Acta. 2008; 1778: 2291-2297.
    • (2008) Biochim Biophys Acta , pp. 2291-2297
    • Schmidt, T.F.1    Caseli, L.2    Vitala, T.3    Oliveira Jr, O.N.4
  • 35
    • 67651174321 scopus 로고    scopus 로고
    • Enzyme activity of horseradish peroxidase immobilized in chitosan matrices in alternated layers
    • Schmidt TF, Caseli L, Santos DS, Oliveira ON Jr. Enzyme activity of horseradish peroxidase immobilized in chitosan matrices in alternated layers. Mat Sci Eng C Biomim. 2009; 29: 1889-1892.
    • (2009) Mat Sci Eng C Biomim , vol.29 , pp. 1889-1892
    • Schmidt, T.F.1    Caseli, L.2    Santos, D.S.3    Oliveira Jr, O.N.4
  • 36
    • 0030714961 scopus 로고    scopus 로고
    • Formation and properties of dimeric recombinant horseradish peroxidase in a system of reversed micelles
    • Gazaryan IG, Klyacho NL, Dulkis YK, Ouporov IV, Levashov AV. Formation and properties of dimeric recombinant horseradish peroxidase in a system of reversed micelles. Biochem J. 1997; 328: 643-647.
    • (1997) Biochem J , vol.328 , pp. 643-647
    • Gazaryan, I.G.1    Klyacho, N.L.2    Dulkis, Y.K.3    Ouporov, I.V.4    Levashov, A.V.5
  • 38
    • 11544329249 scopus 로고    scopus 로고
    • Study of horseradish peroxidase activity in alternate-layer Langmuir-Blodgett films
    • Berzina TS, Piras L, Troitsky VI. Study of horseradish peroxidase activity in alternate-layer Langmuir-Blodgett films. Thin Solid Films. 1998; 327: 621-626.
    • (1998) Thin Solid Films , vol.327 , pp. 621-626
    • Berzina, T.S.1    Piras, L.2    Troitsky, V.I.3
  • 39
    • 9244256789 scopus 로고    scopus 로고
    • Synthesis of stable polystyrene and poly(methyl methacrylate) particles in the presence of carboxymethyl cellulose
    • Castro LBR, Soares KV, Naves AF, Carmona-Ribeiro AM, Petri DFS. Synthesis of stable polystyrene and poly(methyl methacrylate) particles in the presence of carboxymethyl cellulose. Ind Eng Chem Res. 2004; 43: 7774-7779.
    • (2004) Ind Eng Chem Res , vol.43 , pp. 7774-7779
    • Castro, L.B.R.1    Soares, K.V.2    Naves, A.F.3    Carmona-Ribeiro, A.M.4    Petri, D.F.S.5
  • 40
    • 34548289415 scopus 로고    scopus 로고
    • Adsorption behavior and activity of horseradish peroxidase onto polysaccharide-decorated particles
    • Silva RA, Carmona-Ribeiro AM, Petri DFS. Adsorption behavior and activity of horseradish peroxidase onto polysaccharide-decorated particles. Int J Biol Macromol. 2007; 41: 404-409.
    • (2007) Int J Biol Macromol , vol.41 , pp. 404-409
    • Silva, R.A.1    Carmona-Ribeiro, A.M.2    Petri, D.F.S.3
  • 41
    • 77957965368 scopus 로고    scopus 로고
    • Protein adsorption onto polyelectrolyte layers: effects of protein hydrophobicity and charge anisotropy
    • Silva RA, Urzua MD, Petri DFS, Dubin PL. Protein adsorption onto polyelectrolyte layers: effects of protein hydrophobicity and charge anisotropy. Langmuir. 2010; 26: 14032-14038.
    • (2010) Langmuir , vol.26 , pp. 14032-14038
    • Silva, R.A.1    Urzua, M.D.2    Petri, D.F.S.3    Dubin, P.L.4
  • 42
    • 77952833325 scopus 로고    scopus 로고
    • What Governs Protein Adsorption and Immobilization at a Charged Solid Surface?
    • Kubiak-Ossowska K, Mulheran P. What Governs Protein Adsorption and Immobilization at a Charged Solid Surface? Langmuir. 2010; 26: 7690-7694.
    • (2010) Langmuir , vol.26 , pp. 7690-7694
    • Kubiak-Ossowska, K.1    Mulheran, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.