메뉴 건너뛰기




Volumn 40, Issue 1, 2005, Pages 147-154

Covalent coupling of peroxidase to a copolymer of acrylamide (AAm)-2-hydroxyethyl methaacrylate (HEMA) and its use in phenol oxidation

Author keywords

AAm HEMA; Covalent coupling; Horseradish peroxidase; Oxidation; Phenol

Indexed keywords

CONFORMATIONS; COPOLYMERS; ENZYMES; OXIDATION; PHENOLS;

EID: 4444280349     PISSN: 00329592     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2003.11.051     Document Type: Article
Times cited : (25)

References (19)
  • 2
    • 33845280481 scopus 로고
    • Protease catalyzed regioselective esterification of sugar and related compounds in anhydrous dimethyl formamide
    • Riva S., Chopineau J., Kieboom A.P.G., Klibanov A.M. Protease catalyzed regioselective esterification of sugar and related compounds in anhydrous dimethyl formamide. J. Am. Chem. Soc. 110:1988;584-589
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 584-589
    • Riva, S.1    Chopineau, J.2    Kieboom, A.P.G.3    Klibanov, A.M.4
  • 3
    • 4444244413 scopus 로고
    • Enzymes that work in organic solvents
    • Therisod M., Klibanov A.M. Enzymes that work in organic solvents. J. Am. Chem. Soc. 108:1986;5684-5686
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 5684-5686
    • Therisod, M.1    Klibanov, A.M.2
  • 4
    • 0027909874 scopus 로고
    • Lipase-catalysed acylation of sugars solubilized in hydrophobic solvents by complexation
    • Ikeda I., Klibanov A.M. Lipase-catalysed acylation of sugars solubilized in hydrophobic solvents by complexation. Biotechnol. Bioeng. 42:1993;788-791
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 788-791
    • Ikeda, I.1    Klibanov, A.M.2
  • 5
    • 84963333732 scopus 로고
    • β-Galactosidase technology - A solution to the lactose problem
    • Shukla T.P. β-Galactosidase technology - a solution to the lactose problem. CRC Crit. Rev. Food Technol. 5:1975;325
    • (1975) CRC Crit. Rev. Food Technol. , vol.5 , pp. 325
    • Shukla, T.P.1
  • 6
    • 0018518563 scopus 로고
    • Preparation and magnetic filtration of polyacrlyamide gels containing covalently immobilized proteins and a ferro fluid
    • Adalsteinsson O., Lamotte A., Baddour R.F., Cotton C.K., Pollak A., White side G.M. Preparation and magnetic filtration of polyacrlyamide gels containing covalently immobilized proteins and a ferro fluid. J. Mol. Catal. 6:1979;199-225
    • (1979) J. Mol. Catal. , vol.6 , pp. 199-225
    • Adalsteinsson, O.1    Lamotte, A.2    Baddour, R.F.3    Cotton, C.K.4    Pollak, A.5    White Side, G.M.6
  • 7
    • 0020720473 scopus 로고
    • Kinetic and thermal characteristics of enzyme-graft copolymer
    • Cremonsi P., D'Anguiro S. Kinetic and thermal characteristics of enzyme-graft copolymer. Biotechnol. Bioeng. 25:1983;735-744
    • (1983) Biotechnol. Bioeng. , vol.25 , pp. 735-744
    • Cremonsi, P.1    D'Anguiro, S.2
  • 8
    • 0022714379 scopus 로고
    • Optimization of enzyme immobilization of keratin or polyamide-coated bead shaped
    • Lobarzewskhi W.A., Wolski T., Fiedurek J. Optimization of enzyme immobilization of keratin or polyamide-coated bead shaped. Biotechnol. Bioeng. 28:1986;747-750
    • (1986) Biotechnol. Bioeng. , vol.28 , pp. 747-750
    • Lobarzewskhi, W.A.1    Wolski, T.2    Fiedurek, J.3
  • 9
    • 0345491416 scopus 로고    scopus 로고
    • Hydrazide-functionalized poly(2-hydroxyethyl methaacrylate) microspheres for immobilization of horseradish peroxidase
    • Horak D., Darpisek M., Turkova J., Benes M. Hydrazide-functionalized poly(2-hydroxyethyl methaacrylate) microspheres for immobilization of horseradish peroxidase. Biotechnol. Prog. 15:1999;208-215
    • (1999) Biotechnol. Prog. , vol.15 , pp. 208-215
    • Horak, D.1    Darpisek, M.2    Turkova, J.3    Benes, M.4
  • 10
    • 0034274982 scopus 로고    scopus 로고
    • In situ entrapment of α-Chymotrpsin in network of acrylamide and 2-hydroxyethyl methaacrylate copolymer
    • Soni S., Desai J.D., Devi S. In situ entrapment of α-Chymotrpsin in network of acrylamide and 2-hydroxyethyl methaacrylate copolymer. J. Appl. Polym. Sci. 77:2000;2996-3002
    • (2000) J. Appl. Polym. Sci. , vol.77 , pp. 2996-3002
    • Soni, S.1    Desai, J.D.2    Devi, S.3
  • 11
    • 84985668701 scopus 로고
    • Immobilization of β-galactosidase onto polymer materials
    • Reijikumar S., Devi S. Immobilization of β-galactosidase onto polymer materials. J. Appl. Polym. Sci. 55:1995;871-878
    • (1995) J. Appl. Polym. Sci. , vol.55 , pp. 871-878
    • Reijikumar, S.1    Devi, S.2
  • 12
    • 0019087738 scopus 로고
    • P-Toluene sulphonyl chloride as an activating agent of agarose for the preparation of immobilized affinity ligand and proteins. Optimization of condition for activation and coupling
    • Nilsson K., Norlow O., Mossback K. p-Toluene sulphonyl chloride as an activating agent of agarose for the preparation of immobilized affinity ligand and proteins. Optimization of condition for activation and coupling. Eur. J. Biochem. 112:1980;397-402
    • (1980) Eur. J. Biochem. , vol.112 , pp. 397-402
    • Nilsson, K.1    Norlow, O.2    Mossback, K.3
  • 13
    • 0016636495 scopus 로고
    • Covalent attachment of proteins to polysaccharide carriers by means of benzoquinone
    • Brandt J., Anderson L.O., Porath J. Covalent attachment of proteins to polysaccharide carriers by means of benzoquinone. Biochem. Biophys. Acta. 386:1975;196-202
    • (1975) Biochem. Biophys. Acta , vol.386 , pp. 196-202
    • Brandt, J.1    Anderson, L.O.2    Porath, J.3
  • 14
    • 0942300986 scopus 로고    scopus 로고
    • Immobilization of horseradish peroxidase by entrapment in natural polysaccharide
    • in press.
    • Shukla SP, Modi K, Devi S. Immobilization of horseradish peroxidase by entrapment in natural polysaccharide. J. Appl. Polym. Sci., in press.
    • J. Appl. Polym. Sci.
    • Shukla, S.P.1    Modi, K.2    Devi, S.3
  • 15
    • 0031973583 scopus 로고    scopus 로고
    • Effluent treatment of pulp and paper and textile industries using immobilized horseradish peroxidase
    • Zamora P.P., Esposito E., Pelegrini R., Groto R., Reyes J., Duran N. Effluent treatment of pulp and paper and textile industries using immobilized horseradish peroxidase. Env. Technol. 19(1):1998;55-63
    • (1998) Env. Technol. , vol.19 , Issue.1 , pp. 55-63
    • Zamora, P.P.1    Esposito, E.2    Pelegrini, R.3    Groto, R.4    Reyes, J.5    Duran, N.6
  • 16
    • 0030570418 scopus 로고    scopus 로고
    • Tyrosinase containing chitosan gels: A combined catalyst and sorbent for selective phenol removal
    • Sun W.Q., Payne G.F. Tyrosinase containing chitosan gels: a combined catalyst and sorbent for selective phenol removal. Biotechnol. Bioeng. 51:1996;79-86
    • (1996) Biotechnol. Bioeng. , vol.51 , pp. 79-86
    • Sun, W.Q.1    Payne, G.F.2
  • 17
    • 0032964543 scopus 로고    scopus 로고
    • Development and demonstration of an immobilized polyphenol oxidase bioprobe for the detection of phenolic pollutants in water
    • Barton S., Russell I.M. Development and demonstration of an immobilized polyphenol oxidase bioprobe for the detection of phenolic pollutants in water. Anal Chim. Acta. 389:1999;161-170
    • (1999) Anal Chim. Acta , vol.389 , pp. 161-170
    • Barton, S.1    Russell, I.M.2
  • 18
    • 0017540326 scopus 로고
    • Preparation and properties of horseradish peroxidase bound covalently to polystyrene beads. Application in the semi-automatic determination of hydrogen peroxide with homovanillic acid as substrate
    • Miller J.N., Rocks B.F., Burns D.T. Preparation and properties of horseradish peroxidase bound covalently to polystyrene beads. Application in the semi-automatic determination of hydrogen peroxide with homovanillic acid as substrate. Anal. Chim. Acta. 93:1977;353-356
    • (1977) Anal. Chim. Acta , vol.93 , pp. 353-356
    • Miller, J.N.1    Rocks, B.F.2    Burns, D.T.3
  • 19
    • 0942271110 scopus 로고
    • Preparations and properties of covalently bound peroxide on cyanogen bromide-activated cellulose
    • Schell H.D., Turcu A., Pele M. Preparations and properties of covalently bound peroxide on cyanogen bromide-activated cellulose. Cellul. Chem. Technol. 9:1975;205
    • (1975) Cellul. Chem. Technol. , vol.9 , pp. 205
    • Schell, H.D.1    Turcu, A.2    Pele, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.