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Volumn 30, Issue 1, 2012, Pages 86-95

Enzymatic cross-linking of gelatine with laccase and tyrosinase

Author keywords

Gelatine; Laccase; Tyrosinase

Indexed keywords

AGARICUS BISPORUS; ENZYMATIC OXIDATIONS; GELATINE; LACCASES; MODEL SUBSTRATES; OXYGEN CONSUMPTION; RP-HPLC; SDS-PAGE; SOLUBLE MATERIALS; T. VERSICOLOR; TOXIC CHEMICALS; TRAMETES HIRSUTA; TYROSINASE; TYROSINE RESIDUES;

EID: 84856498760     PISSN: 10242422     EISSN: 10292446     Source Type: Journal    
DOI: 10.3109/10242422.2012.646036     Document Type: Conference Paper
Times cited : (40)

References (69)
  • 2
    • 0035021486 scopus 로고    scopus 로고
    • Infl uence of transglutaminase treat- ment on the thermoreversible gelation of gelatine
    • Babin H, Dickinson E. 2001. Infl uence of transglutaminase treat- ment on the thermoreversible gelation of gelatine. Food Hydrocoll 15:271-276.
    • (2001) Food Hydrocoll , vol.15 , pp. 271-276
    • Babin, H.1    Dickinson, E.2
  • 3
    • 0029437855 scopus 로고
    • Bioartificial materials based on collagen .1. Collagen cross- linking with gaseous glutaraldehyde
    • Barbani N, Giusti P, Lazzeri L, Polacco G, Pizzirani G. 1995. Bioartificial materials based on collagen .1. Collagen cross- linking with gaseous glutaraldehyde. J Biomater Sci Polymer Ed 7:461-469.
    • (1995) J Biomater Sci Polymer Ed , vol.7 , pp. 461-469
    • Barbani, N.1    Giusti, P.2    Lazzeri, L.3    Polacco, G.4    Pizzirani, G.5
  • 4
    • 0015516321 scopus 로고
    • The peroxidase- catalyzed oxidation of tyrosine
    • Bayse GS, Michaels AW, Morrison M. 1972. The peroxidase- catalyzed oxidation of tyrosine. BBA 284:34
    • (1972) BBA , vol.284 , pp. 34
    • Bayse, G.S.1    Michaels, A.W.2    Morrison, M.3
  • 6
    • 33745564300 scopus 로고    scopus 로고
    • Transglutaminase reactivity with gelatine: Perspective applications in tissue engineering
    • DOI 10.1007/s10529-006-9046-2
    • Bertoni F, Barbani N, Giusti P, Ciardelli G. 2006. Transglutaminase reactivity with gelatine: perspective applications in tissue engineering. Biotechnol Lett 28:697-702. (Pubitemid 43978874)
    • (2006) Biotechnology Letters , vol.28 , Issue.10 , pp. 697-702
    • Bertoni, F.1    Barbani, N.2    Giusti, P.3    Ciardelli, G.4
  • 8
    • 0017647916 scopus 로고
    • Some mechanical property considerations of reconstituted collagen for drug release supports
    • Bradley WG, Wilkes GL. 1977 Some mechanical property considerations of reconstituted collagen for drug release supports. Biomat Med Dev Artific Org 5:159-175. (Pubitemid 8146042)
    • (1977) Biomaterials Medical Devices and Artificial Organs , vol.5 , Issue.2 , pp. 159-175
    • Bradley, W.G.1    Wilkes, G.L.2
  • 11
    • 84856504518 scopus 로고    scopus 로고
    • Enzymatic food structure engineering
    • Buchert J. 2007. Enzymatic food structure engineering. Ann Nutr Metabol 51:9.
    • (2007) Ann Nutr Metabol , vol.51 , pp. 9
    • Buchert, J.1
  • 13
    • 0036346623 scopus 로고    scopus 로고
    • In vitro protein- polysaccharide conjugation: Tyrosinase-catalyzed conjugation of gelatin and chitosan
    • Chen TH, Embree HD, Wu LQ, Payne GF. 2002. In vitro protein- polysaccharide conjugation: tyrosinase-catalyzed conjugation of gelatin and chitosan. Biopolym 64:U292-U302.
    • (2002) Biopolym , vol.64
    • Chen, T.H.1    Embree, H.D.2    Wu, L.Q.3    Payne, G.F.4
  • 15
    • 0034883923 scopus 로고    scopus 로고
    • Combinatorial screening for enzyme-mediated coupling. Tyrosinase-catalyzed coupling to create protein-chitosan conjugates
    • DOI 10.1021/bm000125w
    • Chen TH, Vazquez-Duhalt R, Wu CF, Bentley WE, Payne GF. 2001. Combinatorial screening for enzyme-mediated coupling. Tyrosinase-catalyzed coupling to create protein-chitosan conjugates. Biomacromol 2:456-462. (Pubitemid 32707525)
    • (2001) Biomacromolecules , vol.2 , Issue.2 , pp. 456-462
    • Chen, T.1    Vazquez-Duhalt, R.2    Wu, C.-F.3    Bentley, W.E.4    Payne, G.F.5
  • 16
    • 0345526456 scopus 로고    scopus 로고
    • Enzymatic synthesis and antioxidant property of gelatin-catechin conjugates
    • DOI 10.1023/B:BILE.0000004391.27564.8e
    • Chung JE, Kurisawa M, Uyama H, Kobayashi S. 2003. Enzymatic synthesis and antioxidant property of gelatin-catechin conjugates. Biotechnol Lett 25:1993-1997. (Pubitemid 37502440)
    • (2003) Biotechnology Letters , vol.25 , Issue.23 , pp. 1993-1997
    • Chung, J.E.1    Kurisawa, M.2    Uyama, H.3    Kobayashi, S.4
  • 17
    • 0030722720 scopus 로고    scopus 로고
    • Evidence of the indirect formation of the catecholic intermediate substrate responsible for the autoactivation kinetics of tyrosinase
    • DOI 10.1074/jbc.272.42.26226
    • Cooksey CJ, Garratt PJ, Land EJ, Pavel S, Ramsden CA, Riley PA, Smit NP. 1997. Evidence of the indirect formation of the catecholic intermediate substrate responsible for the autoactiva- tion kinetics of tyrosinase. J Biol Chem 272:26226-26235. (Pubitemid 27458833)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.42 , pp. 26226-26235
    • Cooksey, C.J.1    Garratt, P.J.2    Land, E.J.3    Pavel, S.4    Ramsden, C.A.5    Riley, P.A.6    Smit, N.P.M.7
  • 18
    • 26944434828 scopus 로고    scopus 로고
    • Antimicrobial activity of fl avo- noids
    • Cushnie TPT, Lamb AJ. 2005. Antimicrobial activity of fl avo- noids. Int J Antimicrob Agents 26:343-356.
    • (2005) Int J Antimicrob Agents , vol.26 , pp. 343-356
    • Tpt, C.1    Lamb, A.J.2
  • 19
    • 0042061223 scopus 로고    scopus 로고
    • Hydrogels for tissue engineering: Scaffold design variables and applications
    • DOI 10.1016/S0142-9612(03)00340-5
    • Drury JL, Mooney DJ. 2003. Hydrogels for tissue engineering: scaf- fold design variables and applications. Biomat 24:4337-4351. (Pubitemid 36960132)
    • (2003) Biomaterials , vol.24 , Issue.24 , pp. 4337-4351
    • Drury, J.L.1    Mooney, D.J.2
  • 20
    • 0014939358 scopus 로고
    • Physicochemical and kinetic properties of mushroom tyrosinase
    • Duckwort HW, Coleman JE. 1970. Physicochemical and kinetic properties of mushroom tyrosinase. J Biol Chem 245: 1613-1625.
    • (1970) J Biol Chem , vol.245 , pp. 1613-1625
    • Duckwort, H.W.1    Coleman, J.E.2
  • 21
    • 0001505441 scopus 로고
    • Amino acid composition of mammalian collagen and gelatin
    • Eastoe JE. 1955. Amino acid composition of mammalian collagen and gelatin. Biochem J 61:589-600.
    • (1955) Biochem J , vol.61 , pp. 589-600
    • Eastoe, J.E.1
  • 22
    • 77951220642 scopus 로고    scopus 로고
    • Role of the C-terminal extension in a bacterial tyrosinase
    • Fairhead M, Thony-Meyer L. 2010a. Role of the C-terminal extension in a bacterial tyrosinase. Febs J 277:2083-2095.
    • (2010) Febs J , vol.277 , pp. 2083-2095
    • Fairhead, M.1    Thony-Meyer, L.2
  • 23
    • 78649451634 scopus 로고    scopus 로고
    • Cross-linking and immobi- lisation of different proteins with recombinant Verrucomicro- bium spinosum tyrosinase
    • Fairhead M, Thony-Meyer L. 2010b. Cross-linking and immobi- lisation of different proteins with recombinant Verrucomicro- bium spinosum tyrosinase. J Biotechnol 150:546-551.
    • (2010) J Biotechnol , vol.150 , pp. 546-551
    • Fairhead, M.1    Thony-Meyer, L.2
  • 24
    • 55449136448 scopus 로고    scopus 로고
    • Evaluation of the antioxidant activity of different fl avonoids by the chemiluminescence method
    • Georgetti, SR, Casagrande R, Di Mambro,VM, Azzolini AECS, Fonseca MJV. 2003. Evaluation of the antioxidant activity of different fl avonoids by the chemiluminescence method. AAPS PharmSci 5.
    • (2003) AAPS PharmSci , vol.5
    • Georgetti, S.R.1    Casagrande, R.2    Mambrovm, D.3    Aecs, A.4    Fonseca, M.J.V.5
  • 25
    • 0036980061 scopus 로고    scopus 로고
    • Protein-protein crosslinking in food: Methods, consequences, applications
    • Gerrard JA. 2002. Protein-protein crosslinking in food: methods, consequences, applications. Trends Food Sci Technol 13: 391-399.
    • (2002) Trends Food Sci Technol , vol.13 , pp. 391-399
    • Gerrard, J.A.1
  • 26
    • 0037122675 scopus 로고    scopus 로고
    • Hydrogels for biomedical applications
    • DOI 10.1016/S0169-409X(01)00239-3, PII S0169409X01002393
    • Hoffman AS. 2002. Hydrogels for biomedical applications. Adv Drug Del Rev 54:3-12. (Pubitemid 34081178)
    • (2002) Advanced Drug Delivery Reviews , vol.54 , Issue.1 , pp. 3-12
    • Hoffman, A.S.1
  • 27
    • 0028940012 scopus 로고
    • Strand scission in DNA induced by -DOPA in the presence of Cu(II)
    • Husain S, Hadi SM. 1995. Strand scission in DNA induced by -DOPA in the presence of Cu(II). FEBS Lett 364:75-78.
    • (1995) FEBS Lett , vol.364 , pp. 75-78
    • Husain, S.1    Hadi, S.M.2
  • 28
    • 0021213448 scopus 로고
    • Oxidation of tyrosine residues in proteins by tyrosinase. Formation of protein-bonded 3,4-dihydroxyphenylalanine and 5-S-cysteinyl-3,4- dihydroxyphenylalanine
    • Ito S, Kato T, Shinpo K, Fujita K. 1984. Oxidation of Tyrosine Residues in Proteins by Tyrosinase-formation of protein- bonded 3,4- Dihydroxyphenylalanine and 5-S-Cysteinyl-3,4- Dihydroxyphenylalanine. Biochem J 222:407-411. (Pubitemid 14004920)
    • (1984) Biochemical Journal , vol.222 , Issue.2 , pp. 407-411
    • Ito, S.1    Kato, T.2    Shinpo, K.3    Fujita, K.4
  • 29
    • 0021213448 scopus 로고
    • Oxidation of tyrosine residues in proteins by tyrosinase. Formation of protein-bonded 3,4-dihydroxyphenylalanine and 5-S-cysteinyl-3,4- dihydroxyphenylalanine
    • Ito S, Kato T, Shinpo K, Fujita K. 1984. Oxidation of tyrosine residues in proteins by tyrosinase-formation of protein-bonded 3,4-Dihydroxyphenylalanine and 5-S-Cysteinyl-3,4-Dihydrox- yphenylalanine. Biochem J 222:407-411. (Pubitemid 14004920)
    • (1984) Biochemical Journal , vol.222 , Issue.2 , pp. 407-411
    • Ito, S.1    Kato, T.2    Shinpo, K.3    Fujita, K.4
  • 30
    • 0021892899 scopus 로고
    • Tyrosinase-cytalyzed conjugation of dopa with glutathione
    • DOI 10.1007/BF01970033
    • Ito S, Palumbo A, Prota G. 1985. Tyrosinase-catalyzed conjuga- tion of dopa with glutathione. Experientia 41:960-961. (Pubitemid 15037180)
    • (1985) Experientia , vol.41 , Issue.7 , pp. 960-961
    • Ito, S.1    Palumbo, A.2    Prota, G.3
  • 31
    • 42549092546 scopus 로고    scopus 로고
    • Chemistry of mixed melanogenesis - Pivotal roles of dopaquinone
    • DOI 10.1111/j.1751-1097.2007.00238.x
    • Ito S, Wakamatsu K. 2008. Chemistry of mixed melanogenesis- Pivotal roles of dopaquinone. Photochem Photobiol 84: 582-592. (Pubitemid 351589353)
    • (2008) Photochemistry and Photobiology , vol.84 , Issue.3 , pp. 582-592
    • Ito, S.1    Wakamatsu, K.2
  • 32
    • 0033856899 scopus 로고    scopus 로고
    • Tyrosinase-induced cross-linking of tyrosine-containing peptides investigated by matrix-assisted laser desorption/ionization time-of-fl ight mass spectrometry
    • Jee JG, Park SJ, Kim HJ. 2000. Tyrosinase-induced cross-linking of tyrosine-containing peptides investigated by matrix-assisted laser desorption/ionization time-of-fl ight mass spectrometry. Rapid Commun Mass Spectrom 14:1563-1567.
    • (2000) Rapid Commun Mass Spectrom , vol.14 , pp. 1563-1567
    • Jee, J.G.1    Park, S.J.2    Kim, H.J.3
  • 33
    • 42749085115 scopus 로고    scopus 로고
    • Tyrosinase-catalysed coupling of functional molecules onto protein fibres
    • Jus S, Kokol V, Guebitz GM. 2008. Tyrosinase-catalysed coupling of functional molecules onto protein fibres. Enz Microb Technol 42:535-542.
    • (2008) Enz Microb Technol , vol.42 , pp. 535-542
    • Jus, S.1    Kokol, V.2    Guebitz, G.M.3
  • 35
    • 1642525701 scopus 로고    scopus 로고
    • Quinone cross-linked polysaccharide hybrid fiber
    • DOI 10.1021/bm034363d
    • Kuboe Y Tonegawa H, Ohkawa K, Yamamoto H. 2004. Quinone cross-linked polysaccharide hybrid fiber. Biomacromol 5:348-357. (Pubitemid 38404470)
    • (2004) Biomacromolecules , vol.5 , Issue.2 , pp. 348-357
    • Kuboe, Y.1    Tonegawa, H.2    Ohkawa, K.3    Yamamoto, H.4
  • 36
    • 0033981947 scopus 로고    scopus 로고
    • Enzymatic gelation of the natural polymer chitosan
    • DOI 10.1016/S0032-3861(99)00360-2, PII S0032386199003602
    • Kumar G, Bristow JF, Smith PJ, Payne GF. 2000. Enzymatic gelation of the natural polymer chitosan. Polym 41:2157-2168. (Pubitemid 30025579)
    • (2000) Polymer , vol.41 , Issue.6 , pp. 2157-2168
    • Kumar, G.1    Bristow, J.F.2    Smith, P.J.3    Payne, G.F.4
  • 37
    • 34249853658 scopus 로고    scopus 로고
    • Tyrosinase-aided protein cross-linking: Effects on gel formation of chicken breast myofibrils and texture and water-holding of chicken breast meat homogenate gels
    • Lantto R, Puolanne E, Kruus K, Buchert J, Autio K. 2007. Tyrosinase-aided protein cross-linking: effects on gel formation of chicken breast myofibrils and texture and water-holding of chicken breast meat homogenate gels. J Agric Food Chem 55:1248-1255.
    • (2007) J Agric Food Chem , vol.55 , pp. 1248-1255
    • Lantto, R.1    Puolanne, E.2    Kruus, K.3    Buchert, J.4    Autio, K.5
  • 38
  • 39
    • 0020688520 scopus 로고
    • Neurospora tyrosinase-structural, spectroscopic and catalytic properties
    • Lerch K. 1983 Neurospora tyrosinase-structural, spectroscopic and catalytic properties. Mol Cell Biochem 52:125-138.
    • (1983) Mol Cell Biochem , vol.52 , pp. 125-138
    • Lerch, K.1
  • 41
    • 84986520447 scopus 로고
    • Modification of proteins by polyphenol oxidase and peroxidase and their products
    • Matheis G, Whitaker JR. 1984. Modification of proteins by polyphenol oxidase and peroxidase and their products. J Food Biochem 8:137-162.
    • (1984) J Food Biochem , vol.8 , pp. 137-162
    • Matheis, G.1    Whitaker, J.R.2
  • 42
    • 0033119824 scopus 로고    scopus 로고
    • Bioadhesion of gelatin films crosslinked with glutaraldehyde
    • DOI 10.1002/(SICI)1097-4636(199904)45:1<20::AID-JBM3>3.0.CO;2-6
    • Matsuda S, Iwata H, Se N, Ikada Y. 1999. Bioadhesion of gelatin films crosslinked with glutaraldehyde. J Biomed Mat Res 45:20-27. (Pubitemid 29068434)
    • (1999) Journal of Biomedical Materials Research , vol.45 , Issue.1 , pp. 20-27
    • Matsuda, S.1    Iwata, H.2    Se, N.3    Ikada, Y.4
  • 45
    • 0034772876 scopus 로고    scopus 로고
    • Caffeic acid, chlorogenic acid, and dihydrocaffeic acid metabolism: Glutathione conjugate formation
    • Moridani MY, Scobie H, Jamshidzadeh A, Salehi P, O'Brien PJ. 2001. Caffeic acid, chlorogenic acid, and dihydrocaffeic acid metabolism: glutathione conjugate formation. Drug Metabol Dispos 29:1432-1439. (Pubitemid 33000689)
    • (2001) Drug Metabolism and Disposition , vol.29 , Issue.11 , pp. 1432-1439
    • Moridani, M.Y.1    Scobie, H.2    Jamshidzadeh, A.3    Salehi, P.4    O'Brien, P.J.5
  • 46
    • 0024288734 scopus 로고
    • Ligninolytic enzymes of the white-rot fungus phlebia radiata
    • Niku-Paavola ML, Karhunen E, Salola P, Raunio V. 1988. Ligninolytic enzymes of the white-rot fungus phlebia radiata. Biochem J 254:877-883.
    • (1988) Biochem J , vol.254 , pp. 877-883
    • Niku-Paavola, M.L.1    Karhunen, E.2    Salola, P.3    Raunio, V.4
  • 51
    • 55049131330 scopus 로고    scopus 로고
    • Release properties of chemical and enzymatic crosslinked gelatine-gum Arabic microparticles containing a fl uorescent probe plus vetiver essential oil
    • Prata AS, Zanin MHA, Re MI, Grosso CRF. 2008. Release properties of chemical and enzymatic crosslinked gelatine-gum Arabic microparticles containing a fl uorescent probe plus vetiver essential oil. Coll Surf B Biointerf 67:171-178.
    • (2008) Coll Surf B Biointerf , vol.67 , pp. 171-178
    • Prata, A.S.1    Mha, Z.2    Re, M.I.3    Grosso, C.R.F.4
  • 52
    • 0029434529 scopus 로고
    • Recent developments of collagen-based materials for medical applications and drug delivery systems
    • Rao KP. 1995. Recent developments of collagen-based materials for medical applications and drug delivery systems. J Biomat Sci Polym Ed 7:623-645.
    • (1995) J Biomat Sci Polym Ed , vol.7 , pp. 623-645
    • Rao, K.P.1
  • 53
    • 33745600868 scopus 로고    scopus 로고
    • Role of antioxidants in prophylaxis and therapy: A pharmaceutical perspective
    • DOI 10.1016/j.jconrel.2006.04.015, PII S0168365906002057
    • Ratnam DV, Ankola DD, Bhardwaj V Sahana DK, Kumar MNVR. 2006. Role of antioxidants in prophylaxis and therapy: a phar- maceutical perspective. J Contr Rel 113:189-207. (Pubitemid 43983041)
    • (2006) Journal of Controlled Release , vol.113 , Issue.3 , pp. 189-207
    • Ratnam, D.V.1    Ankola, D.D.2    Bhardwaj, V.3    Sahana, D.K.4    Kumar, M.N.V.R.5
  • 54
    • 84989656707 scopus 로고
    • Prolonged resorption of collagen sponges-vapor-phase treatment with formaldehyde
    • Ruderman RJ, Wade CWR, Shepard WD Leonard F 1973. Prolonged resorption of collagen sponges-vapor-phase treatment with formaldehyde. J Biomed Mat Res 7:263-265.
    • (1973) J Biomed Mat Res , vol.7 , pp. 263-265
    • Ruderman, R.J.1    Cwr, W.2    Shepard Leonard, W.D.F.3
  • 56
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schagger H. 2006. Tricine-SDS-PAGE. Nat Protocols 1:16-22.
    • (2006) Nat Protocols , vol.1 , pp. 16-22
    • Schagger, H.1
  • 59
    • 33748327047 scopus 로고    scopus 로고
    • Production and characterization of a secreted, C-terminally processed tyrosinase from the filamentous fungus Trichoderma reesei
    • DOI 10.1111/j.1742-4658.2006.05429.x
    • Selinheimo E, Saloheimo M, Ahola E, Westerholm-Parvinen A, Kalkkinen N, Buchert J, Kruus K. 2006. Production and char- acterization of a secreted, C-terminally processed tyrosinase from the filamentous fungus Trichoderma reesei. Febs J 273:4322-4335. (Pubitemid 44326511)
    • (2006) FEBS Journal , vol.273 , Issue.18 , pp. 4322-4335
    • Selinheimo, E.1    Saloheimo, M.2    Ahola, E.3    Westerholm-Parvinen, A.4    Kalkkinen, N.5    Buchert, J.6    Kruus, K.7
  • 62
    • 84856450342 scopus 로고
    • The action of tyrosinase on certain proteins and products of their autolysis
    • Sizer IW. 1947. The action of tyrosinase on certain proteins and products of their autolysis. J Biol Chem 169:303-311.
    • (1947) J Biol Chem , vol.169 , pp. 303-311
    • Sizer, I.W.1
  • 63
    • 0344013443 scopus 로고    scopus 로고
    • Plant phenolics as cross-linkers of gelatine gels and gelatine-based coacervates for use as food ingredients
    • Strauss G, Gibson SA. 2004. Plant phenolics as cross-linkers of gelatine gels and gelatine-based coacervates for use as food ingredients. Food Hydrocoll 18:81-89.
    • (2004) Food Hydrocoll , vol.18 , pp. 81-89
    • Strauss, G.1    Gibson, S.A.2
  • 65
    • 13244252815 scopus 로고    scopus 로고
    • Enzymatic cross-linking of proteins with tyrosinase
    • Thalmann C, Lötzbeyer T. 2002. Enzymatic cross-linking of proteins with tyrosinase. Eur Food Res Technol 214: 276-281.
    • (2002) Eur Food Res Technol , vol.214 , pp. 276-281
    • Thalmann, C.1    Lötzbeyer, T.2
  • 66
    • 0028013536 scopus 로고
    • The structure and function of fungal laccases
    • Thurston CF. 1994. The structure and function of fungal laccases. Microbiol-Sgm 140, 19-26. (Pubitemid 24067305)
    • (1994) Microbiology , vol.140 , Issue.1 , pp. 19-26
    • Thurston, C.F.1
  • 69
    • 28544444138 scopus 로고    scopus 로고
    • Coating proteins: Structure and cross-linking in fp-1 from the green shell mussel Perna canaliculus
    • DOI 10.1021/bi051530g
    • Zhao H, Waite JH. 2005. Coating proteins: structure and cross- linking in fp-1 from the green shell mussel Perna canaliculus. Biochem 44:15915-15923. (Pubitemid 41746922)
    • (2005) Biochemistry , vol.44 , Issue.48 , pp. 15915-15923
    • Zhao, H.1    Waite, J.H.2


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