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Volumn 267, Issue 1-2, 2005, Pages 2-7

Useful method for the spatial localization determination of enzyme (peroxidase) distribution on microfiltration membrane

Author keywords

DAB; Enzyme immobilization; Horseradish peroxidase (HRP); Polypropylene microfiltration membrane (PPMM)

Indexed keywords

BIOLOGICAL MEMBRANES; MICROFILTRATION; POLYPROPYLENES;

EID: 27744467373     PISSN: 03767388     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.memsci.2005.09.017     Document Type: Article
Times cited : (20)

References (27)
  • 3
    • 0025921245 scopus 로고
    • Activity of alkaline phosphatase bound to polysulfone membranes
    • J.A. Hughes, S. Zhou, D. Bhattacharyya, and M. Jay Activity of alkaline phosphatase bound to polysulfone membranes J. Membr. Sci. 60 1991 75
    • (1991) J. Membr. Sci. , vol.60 , pp. 75
    • Hughes, J.A.1    Zhou, S.2    Bhattacharyya, D.3    Jay, M.4
  • 4
    • 0031013010 scopus 로고    scopus 로고
    • Polyacrylonitrile enzyme ultrafiltration membranes prepared by adsorption, cross-linking, and covalent binding
    • M. Ulbricht, and A. Papra Polyacrylonitrile enzyme ultrafiltration membranes prepared by adsorption, cross-linking, and covalent binding Enzyme Microb. Technol. 20 1997 61
    • (1997) Enzyme Microb. Technol. , vol.20 , pp. 61
    • Ulbricht, M.1    Papra, A.2
  • 6
    • 11844276552 scopus 로고    scopus 로고
    • Enzyme multilayer-modified porous membranes as biocatalysts
    • A. Yu, Z. Liang, and F. Caruso Enzyme multilayer-modified porous membranes as biocatalysts Chem. Mater. 17 2005 171
    • (2005) Chem. Mater. , vol.17 , pp. 171
    • Yu, A.1    Liang, Z.2    Caruso, F.3
  • 7
    • 17844402960 scopus 로고    scopus 로고
    • Influence of surface properties of carbon fibres on the adsorption of catalase
    • E. Pamula, and P.G. Rouxhet Influence of surface properties of carbon fibres on the adsorption of catalase Carbon 43 7 2005 1432
    • (2005) Carbon , vol.43 , Issue.7 , pp. 1432
    • Pamula, E.1    Rouxhet, P.G.2
  • 9
    • 0011064563 scopus 로고    scopus 로고
    • Immobilization through adsorption of lusiferase on Langmuir-Blodgett films. Influence of the hydrophilicity or hydrophobicity of the surface on the enzyme kinetic behavior
    • L. Marron-Brignone, R.M. Morélis, and P.R. Coulet Immobilization through adsorption of lusiferase on Langmuir-Blodgett films. Influence of the hydrophilicity or hydrophobicity of the surface on the enzyme kinetic behavior Langmuir 12 1996 5674
    • (1996) Langmuir , vol.12 , pp. 5674
    • Marron-Brignone, L.1    Morélis, R.M.2    Coulet, P.R.3
  • 10
    • 4444280349 scopus 로고    scopus 로고
    • Covalent coupling of peroxidase to a copolymer of acrylamide (AAm)-2-hydroxyethyl methacrylate (HEMA) and its use in phenol oxidation
    • S.P. Shukla, and S. Devi Covalent coupling of peroxidase to a copolymer of acrylamide (AAm)-2-hydroxyethyl methacrylate (HEMA) and its use in phenol oxidation Prog. Biochem. 40 2005 147
    • (2005) Prog. Biochem. , vol.40 , pp. 147
    • Shukla, S.P.1    Devi, S.2
  • 11
    • 0942300986 scopus 로고    scopus 로고
    • Immobilization of horseradish peroxidase by entrapment in natural polysaccharide
    • S.P. Shukla, K. Modi, P.K. Ghosh, and S. Devi Immobilization of horseradish peroxidase by entrapment in natural polysaccharide J. Appl. Polym. Sci. 91 2004 2063
    • (2004) J. Appl. Polym. Sci. , vol.91 , pp. 2063
    • Shukla, S.P.1    Modi, K.2    Ghosh, P.K.3    Devi, S.4
  • 12
    • 0034237721 scopus 로고    scopus 로고
    • Bioencapsulation within synthetic polymers. Part 1. Sol-gel encapsulated biologicals
    • I. Gill, and A. Ballesteros Bioencapsulation within synthetic polymers. Part 1. Sol-gel encapsulated biologicals Trends Biotechnol. 18 2000 282
    • (2000) Trends Biotechnol. , vol.18 , pp. 282
    • Gill, I.1    Ballesteros, A.2
  • 14
    • 0036644239 scopus 로고    scopus 로고
    • Elaboration and chemical reactivity of enzyme modified ion exchanging textiles
    • M. Amounas, V. Magne, C. Innocent, E. Dejean, and P. Seta Elaboration and chemical reactivity of enzyme modified ion exchanging textiles Enzyme Microb. Technol. 31 2002 171
    • (2002) Enzyme Microb. Technol. , vol.31 , pp. 171
    • Amounas, M.1    Magne, V.2    Innocent, C.3    Dejean, E.4    Seta, P.5
  • 15
    • 1642453591 scopus 로고    scopus 로고
    • A recoverable enzymatic microgel based on biomolecular recognition
    • R. Cao, Z. Gu, G.D. Patterson, and B.A. Arimitage A recoverable enzymatic microgel based on biomolecular recognition J. Am. Chem. Soc. 126 2004 726
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 726
    • Cao, R.1    Gu, Z.2    Patterson, G.D.3    Arimitage, B.A.4
  • 16
    • 0023385298 scopus 로고
    • Polymerization of phenols catalyzed by peroxidase in non-aqueous media
    • S. Dordick, M.A. Marletta, and A.M. Klibanov Polymerization of phenols catalyzed by peroxidase in non-aqueous media Biotechnol. Bioeng. 30 1987 31
    • (1987) Biotechnol. Bioeng. , vol.30 , pp. 31
    • Dordick, S.1    Marletta, M.A.2    Klibanov, A.M.3
  • 17
    • 0028006782 scopus 로고
    • Phenol conversion and dimeric intermediates in horseradish peroxidase-catalyzed phenol removal from water
    • J. Yu, K.E. Taylor, H. Zou, N. Biswas, and J.K. Bewtra Phenol conversion and dimeric intermediates in horseradish peroxidase-catalyzed phenol removal from water Environ. Sci. Technol. 28 1994 2154
    • (1994) Environ. Sci. Technol. , vol.28 , pp. 2154
    • Yu, J.1    Taylor, K.E.2    Zou, H.3    Biswas, N.4    Bewtra, J.K.5
  • 19
    • 0042805245 scopus 로고    scopus 로고
    • Quantitative analysis of catalysis and inhibition at horseradish peroxidase monolayers immobilized on an electrode surface
    • B. Limoges, J.-M. Savéant, and D. Yazidi Quantitative analysis of catalysis and inhibition at horseradish peroxidase monolayers immobilized on an electrode surface J. Am. Chem. Soc. 125 2003 9192
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 9192
    • Limoges, B.1    Savéant, J.-M.2    Yazidi, D.3
  • 20
    • 0013895415 scopus 로고
    • The early stages of absorption of injected horseradish peroxidase in the proximal tubules of mouse kidney: Ultrastructural cytochemistry by a new technique
    • R.C. Graham, and M.J. Karnovsky The early stages of absorption of injected horseradish peroxidase in the proximal tubules of mouse kidney: ultrastructural cytochemistry by a new technique J. Histochem. Cytochem. 14 1966 291
    • (1966) J. Histochem. Cytochem. , vol.14 , pp. 291
    • Graham, R.C.1    Karnovsky, M.J.2
  • 21
  • 22
  • 24
    • 0015787876 scopus 로고
    • A colorimetric method for measurement of the (peroxidase-mediated) oxidation of 3,3′-diaminobenzidine
    • H.D. Fahimi, and V. Herzog A colorimetric method for measurement of the (peroxidase-mediated) oxidation of 3,3′-diaminobenzidine J. Histochem. Cytochem. 21 1973 499
    • (1973) J. Histochem. Cytochem. , vol.21 , pp. 499
    • Fahimi, H.D.1    Herzog, V.2
  • 25
    • 20544448219 scopus 로고    scopus 로고
    • Surface modification of polypropylene microporous membranes with a novel glycopolymer
    • Q. Yang, Z.-K. Xu, Z.-W. Dai, J.-L. Wang, and M. Ulbricht Surface modification of polypropylene microporous membranes with a novel glycopolymer Chem. Mater. 17 2005 3050
    • (2005) Chem. Mater. , vol.17 , pp. 3050
    • Yang, Q.1    Xu, Z.-K.2    Dai, Z.-W.3    Wang, J.-L.4    Ulbricht, M.5
  • 26
    • 0028858510 scopus 로고
    • Spectroscopic studies on calcium depleted horseradish peroxidase: Observation of tryptophan sensitized bound terbium (III) fluorescence
    • D. Pahari, A.B. Patel, and D.V. Behere Spectroscopic studies on calcium depleted horseradish peroxidase: observation of tryptophan sensitized bound terbium (III) fluorescence J. Inorg. Biochem. 60 1995 245
    • (1995) J. Inorg. Biochem. , vol.60 , pp. 245
    • Pahari, D.1    Patel, A.B.2    Behere, D.V.3
  • 27
    • 0031239477 scopus 로고    scopus 로고
    • A model of peroxidase activity with inhibition by hydrogen peroxide
    • J.A. Nicell, and H. Wright A model of peroxidase activity with inhibition by hydrogen peroxide Enzyme Microb. Technol. 21 1997 302
    • (1997) Enzyme Microb. Technol. , vol.21 , pp. 302
    • Nicell, J.A.1    Wright, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.