메뉴 건너뛰기




Volumn 272, Issue 14, 2005, Pages 3640-3650

Laccase-catalyzed polymerization of tyrosine-containing peptides

Author keywords

Cross linking; Ferulic acid; Laccase; Peptide; Tyrosine

Indexed keywords

ETHER; FERULIC ACID; GLYCINE; LACCASE; LEUCINE; PEPTIDE; POLYMER; TYROSINE;

EID: 22544447653     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04786.x     Document Type: Article
Times cited : (123)

References (47)
  • 1
    • 0032817983 scopus 로고    scopus 로고
    • Studies with plant laccases. I. Comparison of plant and fungal laccases
    • Harvey BM & Walker JRK (1999) Studies with plant laccases. I. Comparison of plant and fungal laccases. Biochem Mol Biol Biophys 3, 45-51.
    • (1999) Biochem Mol Biol Biophys , vol.3 , pp. 45-51
    • Harvey, B.M.1    Walker, J.R.K.2
  • 3
    • 49249153466 scopus 로고
    • Polyphenol oxidases in plants
    • Mayer AM & Harel E (1979) Polyphenol oxidases in plants. Phytochemistry 18, 193-215.
    • (1979) Phytochemistry , vol.18 , pp. 193-215
    • Mayer, A.M.1    Harel, E.2
  • 4
    • 0035006855 scopus 로고    scopus 로고
    • Modification of lignin for the production of new compounded materials
    • Huttermann A, Mai C & Kharazipour A (2001) Modification of lignin for the production of new compounded materials. Appl Microbiol Biotechnol 55, 387-394.
    • (2001) Appl Microbiol Biotechnol , vol.55 , pp. 387-394
    • Huttermann, A.1    Mai, C.2    Kharazipour, A.3
  • 5
    • 0035535560 scopus 로고    scopus 로고
    • Molecular cloning and expression of eight cDNAs in loblolly pine (Pinus taeda)
    • Sato Y, Wuli B, Sederoff R & Whetten R (2001) Molecular cloning and expression of eight cDNAs in loblolly pine (Pinus taeda). J Plant Res 114, 147-155.
    • (2001) J Plant Res , vol.114 , pp. 147-155
    • Sato, Y.1    Wuli, B.2    Sederoff, R.3    Whetten, R.4
  • 6
    • 0030750335 scopus 로고    scopus 로고
    • The evidence for a laccase-like enzyme activity in a Bacillus sphaericus strain
    • Claus H & Filip Z (1997) The evidence for a laccase-like enzyme activity in a Bacillus sphaericus strain. Microbiol Res 152, 209-216.
    • (1997) Microbiol Res , vol.152 , pp. 209-216
    • Claus, H.1    Filip, Z.2
  • 7
    • 0027417556 scopus 로고
    • Polyphenol oxidase in Azospirillum lipoferum isolated from rice rhizosphere: Evidence for laccase activity in non-motile strains of Azospirillum lipoferum
    • Givaudan A, Effosse A, Faure D, Potier P, Bouillant ML & Bally R (1993) Polyphenol oxidase in Azospirillum lipoferum isolated from rice rhizosphere: evidence for laccase activity in non-motile strains of Azospirillum lipoferum. FEMS Microbiol Lett 108, 205-210.
    • (1993) FEMS Microbiol Lett , vol.108 , pp. 205-210
    • Givaudan, A.1    Effosse, A.2    Faure, D.3    Potier, P.4    Bouillant, M.L.5    Bally, R.6
  • 8
    • 0033920889 scopus 로고    scopus 로고
    • Purification and characterization of the first bacterial laccase in the rhizospheric bacterium Azospirillum lipoferum
    • Diamantidis G, Effosse A, Potier P & Bally R (2001) Purification and characterization of the first bacterial laccase in the rhizospheric bacterium Azospirillum lipoferum. Soil Biol Biochem 32, 919-927.
    • (2001) Soil Biol Biochem , vol.32 , pp. 919-927
    • Diamantidis, G.1    Effosse, A.2    Potier, P.3    Bally, R.4
  • 11
    • 0029937108 scopus 로고    scopus 로고
    • Oxidation of phenols, anilines, and benzenethiols by fungal laccases: Correlation between activity and redox potentials as well as halide inhibition
    • Xu F (1996) Oxidation of phenols, anilines, and benzenethiols by fungal laccases: correlation between activity and redox potentials as well as halide inhibition. Biochemistry 35, 7608-7614.
    • (1996) Biochemistry , vol.35 , pp. 7608-7614
    • Xu, F.1
  • 12
    • 0030379974 scopus 로고    scopus 로고
    • Enzymatic oxidative polymerization of 2,6-dimethylphenol
    • Ikeda R, Sugihara J, Uyama H & Kobayashi S (1996) Enzymatic oxidative polymerization of 2,6-dimethylphenol. Macromolecules 29, 8702-8705.
    • (1996) Macromolecules , vol.29 , pp. 8702-8705
    • Ikeda, R.1    Sugihara, J.2    Uyama, H.3    Kobayashi, S.4
  • 13
    • 0028013536 scopus 로고
    • The structure and function of fungal laccases
    • Thurston CF (1994) The structure and function of fungal laccases. Microbiology 140, 19-26.
    • (1994) Microbiology , vol.140 , pp. 19-26
    • Thurston, C.F.1
  • 14
    • 0030574980 scopus 로고    scopus 로고
    • Novel synthetic pathway to a poly(phenylene oxide). Laccase-catalyzed oxidative polymerization of syringic acid
    • Ikeda R, Uyama H & Kobayashi S (1996) Novel synthetic pathway to a poly(phenylene oxide). Laccase-catalyzed oxidative polymerization of syringic acid. Macromolecules 29, 3053-3054.
    • (1996) Macromolecules , vol.29 , pp. 3053-3054
    • Ikeda, R.1    Uyama, H.2    Kobayashi, S.3
  • 15
    • 0030025889 scopus 로고    scopus 로고
    • A study of a series of recombinant fungal laccases and bilirubin oxidase that exhibit significant differences in redox potential, substrate specificity, and stability
    • Xu F, Shin W, Brown SH, Wahleithner JA, Sundaram UM & Solomon EI (1996) A study of a series of recombinant fungal laccases and bilirubin oxidase that exhibit significant differences in redox potential, substrate specificity, and stability. Biochim Biophys Acta 1292, 303-311.
    • (1996) Biochim Biophys Acta , vol.1292 , pp. 303-311
    • Xu, F.1    Shin, W.2    Brown, S.H.3    Wahleithner, J.A.4    Sundaram, U.M.5    Solomon, E.I.6
  • 16
    • 0017671516 scopus 로고
    • Polymerization of phenolic intermediates of pesticides by a fungal enzyme
    • Bollag JM, Sjoblad RD & Minard RD (1977) Polymerization of phenolic intermediates of pesticides by a fungal enzyme. Experientia 33, 1564-1566.
    • (1977) Experientia , vol.33 , pp. 1564-1566
    • Bollag, J.M.1    Sjoblad, R.D.2    Minard, R.D.3
  • 17
    • 0020705587 scopus 로고
    • Cross-linkage between anilines and phenolic humus constituents
    • Bollag JM, Minard RD & Liu SY (1983) Cross-linkage between anilines and phenolic humus constituents. Environ Sci Technol 17, 72-80.
    • (1983) Environ Sci Technol , vol.17 , pp. 72-80
    • Bollag, J.M.1    Minard, R.D.2    Liu, S.Y.3
  • 19
    • 0001220893 scopus 로고    scopus 로고
    • Fermentation, biocatalysis and bioseparation
    • (Flickinger MC & Drew SW, eds). John Wiley & Sons, New York
    • Xu F (1999) Fermentation, biocatalysis and bioseparation. In The Encyclopedia of Bioprocessing Technology (Flickinger MC & Drew SW, eds), pp. 1545-1554. John Wiley & Sons, New York.
    • (1999) The Encyclopedia of Bioprocessing Technology , pp. 1545-1554
    • Xu, F.1
  • 20
    • 0000326191 scopus 로고    scopus 로고
    • Laccases: A useful group of oxidoreductive enzymes
    • Gianfreda L, Xu F & Bollag J-M (1999) Laccases: a useful group of oxidoreductive enzymes. Biorem J 3, 1-26.
    • (1999) Biorem J , vol.3 , pp. 1-26
    • Gianfreda, L.1    Xu, F.2    Bollag, J.-M.3
  • 22
    • 0035113941 scopus 로고    scopus 로고
    • Effect of laccase and manganese peroxidase on wheat gluten and pentosans during mixing
    • Labat E, Morel MH & Rouau X (2001) Effect of laccase and manganese peroxidase on wheat gluten and pentosans during mixing. Food Hydrocoll 15, 47-52.
    • (2001) Food Hydrocoll , vol.15 , pp. 47-52
    • Labat, E.1    Morel, M.H.2    Rouau, X.3
  • 23
    • 0032648735 scopus 로고    scopus 로고
    • Oxidative gelation of sugar-beet pectins: Use of laccases and hydration properties of the cross-linked pectins
    • Micard V & Thibault J-F (1999) Oxidative gelation of sugar-beet pectins: use of laccases and hydration properties of the cross-linked pectins. Carbohydrate Polymers 39, 265-273.
    • (1999) Carbohydrate Polymers , vol.39 , pp. 265-273
    • Micard, V.1    Thibault, J.-F.2
  • 24
    • 33044495813 scopus 로고    scopus 로고
    • (1994) Use of Laccases in Baking. Patent No. WO94/28728
    • Si JQ (1994) Use of Laccases in Baking. Patent No. WO94/28728.
    • Si, J.Q.1
  • 25
    • 0031805157 scopus 로고    scopus 로고
    • Oxidative cross-linking of pentosans by a fungal laccase and horseradish peroxidase: Mechanism of linkage between feruloylated arabinoxylans
    • Figueroa-Espinoza MC & Rouau X (1998) Oxidative cross-linking of pentosans by a fungal laccase and horseradish peroxidase: mechanism of linkage between feruloylated arabinoxylans. Cereal Chem 75, 259-265.
    • (1998) Cereal Chem , vol.75 , pp. 259-265
    • Figueroa-Espinoza, M.C.1    Rouau, X.2
  • 26
    • 0033020839 scopus 로고    scopus 로고
    • Oxidative cross-linking of wheat arabinoxylans by manganese peroxidase. Comparison with laccase and horseradish peroxidase. Effect of cysteine and tyrosine on gelation
    • Figueroa-Espinoza MC, Morel MH, Surget A & Rouau X (1999) Oxidative cross-linking of wheat arabinoxylans by manganese peroxidase. Comparison with laccase and horseradish peroxidase. Effect of cysteine and tyrosine on gelation. J Sci Food Agric 79, 460-463.
    • (1999) J Sci Food Agric , vol.79 , pp. 460-463
    • Figueroa-Espinoza, M.C.1    Morel, M.H.2    Surget, A.3    Rouau, X.4
  • 27
    • 0000038841 scopus 로고    scopus 로고
    • Cross-linking of whey proteins by enzymatic oxidation
    • Faergemand M, Otte J & Qvist KB (1998) Cross-linking of whey proteins by enzymatic oxidation. J Agric Food Chem 46, 1326-1333.
    • (1998) J Agric Food Chem , vol.46 , pp. 1326-1333
    • Faergemand, M.1    Otte, J.2    Qvist, K.B.3
  • 29
    • 33044508044 scopus 로고    scopus 로고
    • (1999) Method for Cross-linking Protein by Using Enzyme. US Patent 6,121,013
    • Shotaro Y (1999) Method for Cross-linking Protein by Using Enzyme. US Patent 6,121,013.
    • Shotaro, Y.1
  • 30
    • 0000712707 scopus 로고    scopus 로고
    • Effect of lysine, tyrosine, cysteine, and glutathione on the oxidative cross-linking of feruloylated arabinoxylans by a fungal laccase
    • Figueroa-Espinoza M-C, Morel M-H & Rouau X (1998) Effect of lysine, tyrosine, cysteine, and glutathione on the oxidative cross-linking of feruloylated arabinoxylans by a fungal laccase. J Agric Food Chem 46, 2583-2589.
    • (1998) J Agric Food Chem , vol.46 , pp. 2583-2589
    • Figueroa-Espinoza, M.-C.1    Morel, M.-H.2    Rouau, X.3
  • 31
    • 0033748390 scopus 로고    scopus 로고
    • Effects of laccase and ferulic acid on wheat flour doughs
    • Labat E, Morel MH & Rouau X (2000) Effects of laccase and ferulic acid on wheat flour doughs. Cereal Chem 77, 823-828.
    • (2000) Cereal Chem , vol.77 , pp. 823-828
    • Labat, E.1    Morel, M.H.2    Rouau, X.3
  • 32
    • 0030662180 scopus 로고    scopus 로고
    • Identification and quantification of radical reaction intermediates by electron spin resonance spectrometry of laccase-catalysed oxidation of wood fibres from beech
    • Felby C, Nielsen BR, Olesen PO & Skibsted LH (1997) Identification and quantification of radical reaction intermediates by electron spin resonance spectrometry of laccase-catalysed oxidation of wood fibres from beech. Appl Microbiol Biotechnol 48, 459-464.
    • (1997) Appl Microbiol Biotechnol , vol.48 , pp. 459-464
    • Felby, C.1    Nielsen, B.R.2    Olesen, P.O.3    Skibsted, L.H.4
  • 33
    • 0030880690 scopus 로고    scopus 로고
    • Tyrosinase-catecholic substrates in vitro model: Kinetic studies on the o-quinone/o-semiquinone radical formation
    • Ferrari RP, Laurenti E, Ghibaudi EM & Casella L (1997) Tyrosinase-catecholic substrates in vitro model: kinetic studies on the o-quinone/o-semiquinone radical formation. J Inorg Biochem 68, 61-69.
    • (1997) J Inorg Biochem , vol.68 , pp. 61-69
    • Ferrari, R.P.1    Laurenti, E.2    Ghibaudi, E.M.3    Casella, L.4
  • 34
    • 0035006855 scopus 로고    scopus 로고
    • Modification of lignin for the production of new compounded materials
    • Hüttermann A, Mai C & Kharazipour A (2001) Modification of lignin for the production of new compounded materials. Appl Microbiol Biotechnol 55, 387-394.
    • (2001) Appl Microbiol Biotechnol , vol.55 , pp. 387-394
    • Hüttermann, A.1    Mai, C.2    Kharazipour, A.3
  • 35
    • 0035800642 scopus 로고    scopus 로고
    • Oxidation of ferulic acid by laccase: Identification of the products and inhibitory effects of some dipeptides
    • Carunchio F, Crescenzi C, Girelli AM, Messina A & Tarola AM (2001) Oxidation of ferulic acid by laccase: identification of the products and inhibitory effects of some dipeptides. Talanta 55, 189-200.
    • (2001) Talanta , vol.55 , pp. 189-200
    • Carunchio, F.1    Crescenzi, C.2    Girelli, A.M.3    Messina, A.4    Tarola, A.M.5
  • 36
    • 0001325401 scopus 로고
    • The reduction of nitroso-spin traps in chemical and biological systems. A cautionary note
    • Kalyanaraman B, Perez-Reyes E & Mason RP (1979) The reduction of nitroso-spin traps in chemical and biological systems. A cautionary note. Tetrahedron Lett 50, 4809-4812.
    • (1979) Tetrahedron Lett , vol.50 , pp. 4809-4812
    • Kalyanaraman, B.1    Perez-Reyes, E.2    Mason, R.P.3
  • 37
    • 0024510080 scopus 로고
    • Problems associated with spin trapping oxygen-centered free radicals in biological systems
    • Pou S, Hassett DJ, Britigan BE, Cohen MS & Rosen GM (1989) Problems associated with spin trapping oxygen-centered free radicals in biological systems. Anal Biochem 177, 1-6.
    • (1989) Anal Biochem , vol.177 , pp. 1-6
    • Pou, S.1    Hassett, D.J.2    Britigan, B.E.3    Cohen, M.S.4    Rosen, G.M.5
  • 38
    • 0021742265 scopus 로고
    • An electron spin resonance study of o-semiquinones formed during the enzymatic and autoxidation of catechol estrogens
    • Kalyanaraman B, Sealy RC & Sivarajah K (1984) An electron spin resonance study of o-semiquinones formed during the enzymatic and autoxidation of catechol estrogens. J Biol Chem 259, 14018-14022.
    • (1984) J Biol Chem , vol.259 , pp. 14018-14022
    • Kalyanaraman, B.1    Sealy, R.C.2    Sivarajah, K.3
  • 39
    • 4344659042 scopus 로고    scopus 로고
    • Effects of laccase-mediator combinations on wool
    • Lantto R, Schönberg C & Buchert J (2004) Effects of laccase-mediator combinations on wool. Textile Res J 74, 713-717.
    • (2004) Textile Res J , vol.74 , pp. 713-717
    • Lantto, R.1    Schönberg, C.2    Buchert, J.3
  • 40
  • 43
    • 0037009169 scopus 로고    scopus 로고
    • Investigations on the laccase-catalyzed polymerization of lignin model compounds using size-exclusion HPLC
    • Rittstieg K, Suurnäkki A, Suortti T, Kruus K, Guebitz G & Buchert J (2002) Investigations on the laccase-catalyzed polymerization of lignin model compounds using size-exclusion HPLC. Enzyme Microb Technol 31, 403-410.
    • (2002) Enzyme Microb Technol , vol.31 , pp. 403-410
    • Rittstieg, K.1    Suurnäkki, A.2    Suortti, T.3    Kruus, K.4    Guebitz, G.5    Buchert, J.6
  • 44
    • 0024288734 scopus 로고
    • Ligninolytic enzymes of the white-rot-fungus Phlebia radiata
    • Niku-Paavola M-L, Karhunen E, Salola P & Raunio V (1988) Ligninolytic enzymes of the white-rot-fungus Phlebia radiata. Biochem J 254, 877-884.
    • (1988) Biochem J , vol.254 , pp. 877-884
    • Niku-Paavola, M.-L.1    Karhunen, E.2    Salola, P.3    Raunio, V.4
  • 45
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.