메뉴 건너뛰기




Volumn 44, Issue 4, 2009, Pages 440-445

Semi-interpenetrating polymer networks (semi-IPNs) for entrapment of laccase and their use in Acid Orange 52 decolorization

Author keywords

Acid Orange 52; Decolorization; Entrapment; Enzyme immobilization; Laccase; Semi interpenetrating polymer networks

Indexed keywords

ACIDS; ACRYLIC MONOMERS; AMIDES; ENZYME IMMOBILIZATION; ENZYMES; HYDROGELS; POLYMERS;

EID: 62049083367     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2008.12.008     Document Type: Article
Times cited : (54)

References (51)
  • 3
    • 0026451060 scopus 로고
    • A comparative study of the performance of solid supported and soluble urease for the enzymatic hydrolysis of urea
    • Demirel G., Akovali G., Tanyolac A., and Hasirci N. A comparative study of the performance of solid supported and soluble urease for the enzymatic hydrolysis of urea. J Chem Technol Biot 55 (1992) 319-323
    • (1992) J Chem Technol Biot , vol.55 , pp. 319-323
    • Demirel, G.1    Akovali, G.2    Tanyolac, A.3    Hasirci, N.4
  • 4
    • 0028671152 scopus 로고
    • Immobilization of urease and estimation of effective diffusion coefficients of urea in HEMA and VP copolymer matrices
    • Demircioglu H., Beyenal H., Tanyolac A., and Hasirci N. Immobilization of urease and estimation of effective diffusion coefficients of urea in HEMA and VP copolymer matrices. Polym Int 35 (1994) 321-327
    • (1994) Polym Int , vol.35 , pp. 321-327
    • Demircioglu, H.1    Beyenal, H.2    Tanyolac, A.3    Hasirci, N.4
  • 6
    • 33947159656 scopus 로고    scopus 로고
    • Covalent immobilization of invertase on chemically activated poly(2-hydroxyl methacrylate) microbeads
    • Altinok H., Aksoy S., Tümtürk H., and Hasirci N. Covalent immobilization of invertase on chemically activated poly(2-hydroxyl methacrylate) microbeads. Russ Chem B+ 55 (2006) 1860-1864
    • (2006) Russ Chem B+ , vol.55 , pp. 1860-1864
    • Altinok, H.1    Aksoy, S.2    Tümtürk, H.3    Hasirci, N.4
  • 7
    • 44349182547 scopus 로고    scopus 로고
    • Covalent immobilization of invertase on chemically activated poly(styrene-2-hydroxyethyl methacrylate) microbeads
    • Altinok H., Aksoy S., Tümtürk H., and Hasirci N. Covalent immobilization of invertase on chemically activated poly(styrene-2-hydroxyethyl methacrylate) microbeads. J Food Biochem 32 (2008) 299-315
    • (2008) J Food Biochem , vol.32 , pp. 299-315
    • Altinok, H.1    Aksoy, S.2    Tümtürk, H.3    Hasirci, N.4
  • 8
    • 0029041172 scopus 로고
    • Production of cephalosporin C by immobilized Cephalosporium acremonium in polyethyleneimine-modified barium alginate
    • Park J.H., and Khang Y.H. Production of cephalosporin C by immobilized Cephalosporium acremonium in polyethyleneimine-modified barium alginate. Enzyme Microb Tech 17 (1995) 408-412
    • (1995) Enzyme Microb Tech , vol.17 , pp. 408-412
    • Park, J.H.1    Khang, Y.H.2
  • 9
    • 41249099405 scopus 로고    scopus 로고
    • Immobilization of glucose isomerase in surface modified alginate gel beads
    • Tümtürk H., Demirel G., Altinok H., Aksoy S., and Hasirci N. Immobilization of glucose isomerase in surface modified alginate gel beads. J Food Biochem 32 (2008) 234-246
    • (2008) J Food Biochem , vol.32 , pp. 234-246
    • Tümtürk, H.1    Demirel, G.2    Altinok, H.3    Aksoy, S.4    Hasirci, N.5
  • 10
    • 33645027361 scopus 로고    scopus 로고
    • Semi-interpenetrating polymer networks (IPNs) for entrapment of glucose isomerase
    • Demirel G., Ozcetin G., Sahin F., Tumturk H., Aksoy S., and Hasirci N. Semi-interpenetrating polymer networks (IPNs) for entrapment of glucose isomerase. React Funct Polym 66 (2006) 389-394
    • (2006) React Funct Polym , vol.66 , pp. 389-394
    • Demirel, G.1    Ozcetin, G.2    Sahin, F.3    Tumturk, H.4    Aksoy, S.5    Hasirci, N.6
  • 11
    • 0028013536 scopus 로고
    • The structure and function of fungal laccases
    • Thurston C.F. The structure and function of fungal laccases. Microbiology 140 (1994) 19-26
    • (1994) Microbiology , vol.140 , pp. 19-26
    • Thurston, C.F.1
  • 12
    • 0033974765 scopus 로고    scopus 로고
    • Laccases are widespread in bacteria
    • Alexandre G., and Zhulin I.B. Laccases are widespread in bacteria. Tibtech 18 (2000) 41-42
    • (2000) Tibtech , vol.18 , pp. 41-42
    • Alexandre, G.1    Zhulin, I.B.2
  • 13
    • 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. Oxidation of phenols, anilines, and benzenethiols by fungal laccases: correlation between activity and redox potentials as well as halide inhibition. Biochemistry 35 (1996) 7608-7614
    • (1996) Biochemistry , vol.35 , pp. 7608-7614
    • Xu, F.1
  • 14
    • 0035983821 scopus 로고    scopus 로고
    • Laccase: new functions for an old enzyme
    • Mayer A.M., and Staples R.C. Laccase: new functions for an old enzyme. Phytochemistry 60 (2002) 551-565
    • (2002) Phytochemistry , vol.60 , pp. 551-565
    • Mayer, A.M.1    Staples, R.C.2
  • 15
    • 0036382007 scopus 로고    scopus 로고
    • Redox-mediated decolorization of synthetic dyes by fungal laccases
    • Claus H., Faber G., and König H. Redox-mediated decolorization of synthetic dyes by fungal laccases. Appl Microbiol Biotechnol 59 (2002) 672-678
    • (2002) Appl Microbiol Biotechnol , vol.59 , pp. 672-678
    • Claus, H.1    Faber, G.2    König, H.3
  • 17
    • 0346665884 scopus 로고    scopus 로고
    • Enzymatic oxidative transformation of chlorophenol mixtures
    • Bollag J.-M., Horng-Lun Chu, Rao M.A., and Gianfreda L. Enzymatic oxidative transformation of chlorophenol mixtures. J Environ Qual 32 (2003) 63-69
    • (2003) J Environ Qual , vol.32 , pp. 63-69
    • Bollag, J.-M.1    Horng-Lun Chu2    Rao, M.A.3    Gianfreda, L.4
  • 18
    • 38049007776 scopus 로고    scopus 로고
    • Immobilization of Pycnoporus coccineus laccase on Eupergit C: stabilization and treatment of olive oil mill wastewaters
    • Berrio J., Plou F.J., Ballesteros A., Martínez ÁT, and Martínez M.J. Immobilization of Pycnoporus coccineus laccase on Eupergit C: stabilization and treatment of olive oil mill wastewaters. Biocatal Biotransform 25 (2007) 130-134
    • (2007) Biocatal Biotransform , vol.25 , pp. 130-134
    • Berrio, J.1    Plou, F.J.2    Ballesteros, A.3    Martínez ÁT4    Martínez, M.J.5
  • 20
    • 33846443681 scopus 로고    scopus 로고
    • Immobilization of laccase by alginate-chitosan microcapsules and its use in dye decolorization
    • Lu L., Zhao M., and Wang Y. Immobilization of laccase by alginate-chitosan microcapsules and its use in dye decolorization. World J Microb Biot 23 (2007) 159-166
    • (2007) World J Microb Biot , vol.23 , pp. 159-166
    • Lu, L.1    Zhao, M.2    Wang, Y.3
  • 21
    • 0035160019 scopus 로고    scopus 로고
    • Decolourization of textile effluent
    • Sharma J.K., and Arora M.K. Decolourization of textile effluent. Pollution Res 20 (2001) 453-457
    • (2001) Pollution Res , vol.20 , pp. 453-457
    • Sharma, J.K.1    Arora, M.K.2
  • 22
    • 0033668965 scopus 로고    scopus 로고
    • Enzyme applications in the textile industry
    • Durán N., and Durán M. Enzyme applications in the textile industry. Rev Progress Coloration 30 (2000) 41-44
    • (2000) Rev Progress Coloration , vol.30 , pp. 41-44
    • Durán, N.1    Durán, M.2
  • 24
    • 4344672369 scopus 로고    scopus 로고
    • Study of dye decolorization in an immobilized laccase enzyme-reactor using online spectroscopy
    • Kandelbauer A., Maute O., Kessler R.W., Erlacher A., and Gübitz G.M. Study of dye decolorization in an immobilized laccase enzyme-reactor using online spectroscopy. Biotechnol Bioeng 87 (2004) 552-563
    • (2004) Biotechnol Bioeng , vol.87 , pp. 552-563
    • Kandelbauer, A.1    Maute, O.2    Kessler, R.W.3    Erlacher, A.4    Gübitz, G.M.5
  • 25
    • 0033788757 scopus 로고    scopus 로고
    • The role of (auto)catalysis in the mechanism of an anaerobic azo reduction
    • Van der Zee F.P., Lettinga G., and Field J.A. The role of (auto)catalysis in the mechanism of an anaerobic azo reduction. Water Sci Technol 42 (2000) 301-308
    • (2000) Water Sci Technol , vol.42 , pp. 301-308
    • Van der Zee, F.P.1    Lettinga, G.2    Field, J.A.3
  • 26
    • 0036220801 scopus 로고    scopus 로고
    • Biodegradation of a polymeric dye in a pulsed bed bioreactor by immobilised Phanerochaete chrysosporium
    • Mielgo I., Moreira M.T., Feijoo G., and Lema J.M. Biodegradation of a polymeric dye in a pulsed bed bioreactor by immobilised Phanerochaete chrysosporium. Water Res 36 (2002) 1896-1901
    • (2002) Water Res , vol.36 , pp. 1896-1901
    • Mielgo, I.1    Moreira, M.T.2    Feijoo, G.3    Lema, J.M.4
  • 27
    • 0032975903 scopus 로고    scopus 로고
    • Production of laccase by immobilized cells of Agaricus sp.: induction effect of xylan and lignin derivatives
    • Kaluskar V.M., Kapadnis B.P., Jaspers C.H., and Penninckx M.J. Production of laccase by immobilized cells of Agaricus sp.: induction effect of xylan and lignin derivatives. Appl Biochem Biotechnol 76 (1999) 161-170
    • (1999) Appl Biochem Biotechnol , vol.76 , pp. 161-170
    • Kaluskar, V.M.1    Kapadnis, B.P.2    Jaspers, C.H.3    Penninckx, M.J.4
  • 28
    • 0033796345 scopus 로고    scopus 로고
    • Ligninolytic enzyme production and the ability of decolourisation of Poly R-478 in packed-bed bioreactors by Phanerochaete chrysosporium
    • Rodríguez Couto S., Rivela I., Muňoz M.R., and Sanromán A. Ligninolytic enzyme production and the ability of decolourisation of Poly R-478 in packed-bed bioreactors by Phanerochaete chrysosporium. Bioprocess Eng 23 (2000) 287-293
    • (2000) Bioprocess Eng , vol.23 , pp. 287-293
    • Rodríguez Couto, S.1    Rivela, I.2    Muňoz, M.R.3    Sanromán, A.4
  • 29
    • 4344686054 scopus 로고    scopus 로고
    • Purification and partial characterization of manganese peroxidase from immobilized Phanerochaete chrysosporium
    • Öztürk Ürek R., and Kaşikara Pazarlioǧlu N. Purification and partial characterization of manganese peroxidase from immobilized Phanerochaete chrysosporium. Process Biochem 39 (2004) 2061-2068
    • (2004) Process Biochem , vol.39 , pp. 2061-2068
    • Öztürk Ürek, R.1    Kaşikara Pazarlioǧlu, N.2
  • 30
    • 2942735047 scopus 로고    scopus 로고
    • Stainless steel sponge: a novel carrier for the immobilisation of the white-rot fungus Trametes hirsuta for decolourization of textile dyes
    • Rodríguez Couto S., Sanromán M.A., Hofer D., and Gübitz G.M. Stainless steel sponge: a novel carrier for the immobilisation of the white-rot fungus Trametes hirsuta for decolourization of textile dyes. Bioresource Technol 95 (2004) 67-72
    • (2004) Bioresource Technol , vol.95 , pp. 67-72
    • Rodríguez Couto, S.1    Sanromán, M.A.2    Hofer, D.3    Gübitz, G.M.4
  • 31
    • 22944453326 scopus 로고    scopus 로고
    • Dye decolorization by Trametes hirsuta immobilized into alginate beads
    • Domínguez A., Rodríguez Couto S., and Sanromán M.A. Dye decolorization by Trametes hirsuta immobilized into alginate beads. World J Microb Biot 21 (2005) 405-409
    • (2005) World J Microb Biot , vol.21 , pp. 405-409
    • Domínguez, A.1    Rodríguez Couto, S.2    Sanromán, M.A.3
  • 32
    • 36348935593 scopus 로고    scopus 로고
    • Reactive blue 19 decolourization by laccase immobilized on silica beads
    • Champagne P.-P., and Ramsay J.A. Reactive blue 19 decolourization by laccase immobilized on silica beads. Appl Microbiol Biotechnol 77 (2007) 819-823
    • (2007) Appl Microbiol Biotechnol , vol.77 , pp. 819-823
    • Champagne, P.-P.1    Ramsay, J.A.2
  • 34
    • 0019366638 scopus 로고
    • Quantitative estimation of laccase forms in some white-rot fungi using syringaldazine as a substrate
    • Leonowicz A., and Grzywnowicz K. Quantitative estimation of laccase forms in some white-rot fungi using syringaldazine as a substrate. Enzyme Microb Tech 3 (1981) 55-58
    • (1981) Enzyme Microb Tech , vol.3 , pp. 55-58
    • Leonowicz, A.1    Grzywnowicz, K.2
  • 35
    • 0017184389 scopus 로고
    • Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 36
    • 0033813302 scopus 로고    scopus 로고
    • Biodegradation of phenols by laccase immobilised in a membrane reactor
    • Lante A., Crapisi A., Krastanov A., and Spettoli P. Biodegradation of phenols by laccase immobilised in a membrane reactor. Process Biochem 36 (2000) 51-58
    • (2000) Process Biochem , vol.36 , pp. 51-58
    • Lante, A.1    Crapisi, A.2    Krastanov, A.3    Spettoli, P.4
  • 37
    • 0036660926 scopus 로고    scopus 로고
    • Immobilization of wood-rotting fungi laccases on modified cellulose and acrylic carriers
    • Al-Adhami A.J.H., Bryjak J., Markiewicz B.G., and Chozch W.P. Immobilization of wood-rotting fungi laccases on modified cellulose and acrylic carriers. Process Biochem 37 (2002) 1387-1394
    • (2002) Process Biochem , vol.37 , pp. 1387-1394
    • Al-Adhami, A.J.H.1    Bryjak, J.2    Markiewicz, B.G.3    Chozch, W.P.4
  • 38
    • 0035972773 scopus 로고    scopus 로고
    • Effects of fungal laccase immobilization procedures for the development of a biosensor for phenol compounds
    • Freire R.S., Durán N., and Kubota L.T. Effects of fungal laccase immobilization procedures for the development of a biosensor for phenol compounds. Talanta 54 (2001) 681-686
    • (2001) Talanta , vol.54 , pp. 681-686
    • Freire, R.S.1    Durán, N.2    Kubota, L.T.3
  • 39
    • 33845226423 scopus 로고    scopus 로고
    • Comparative study of immobilized Trametes versicolor laccase on nanoparticles and kaolinite
    • Hu X., Zhau X., and Hwang H. Comparative study of immobilized Trametes versicolor laccase on nanoparticles and kaolinite. Chemosphere 66 (2007) 1618-1626
    • (2007) Chemosphere , vol.66 , pp. 1618-1626
    • Hu, X.1    Zhau, X.2    Hwang, H.3
  • 40
    • 3142640533 scopus 로고    scopus 로고
    • Oxidation of anthracene and benzo[a]pyrene by immobilized laccase from Trametes versicolor
    • Dodor D.E., Hwang H., and Ekunwe S.I.N. Oxidation of anthracene and benzo[a]pyrene by immobilized laccase from Trametes versicolor. Enzyme Microb Tech 35 (2004) 210-217
    • (2004) Enzyme Microb Tech , vol.35 , pp. 210-217
    • Dodor, D.E.1    Hwang, H.2    Ekunwe, S.I.N.3
  • 41
    • 0034255734 scopus 로고    scopus 로고
    • Characterization and immobilization of the laccase from Pleurotus ostreatus and its use for the continuous elimination of phenolic pollutants
    • Hublik G., and Schinner F. Characterization and immobilization of the laccase from Pleurotus ostreatus and its use for the continuous elimination of phenolic pollutants. Enzyme Microb Tech 27 (2000) 330-336
    • (2000) Enzyme Microb Tech , vol.27 , pp. 330-336
    • Hublik, G.1    Schinner, F.2
  • 42
    • 0034736404 scopus 로고    scopus 로고
    • Kinetics of glucose isomerization to fructose by immobilized glucose isomerase: anomeric reactivity of d-glucose in kinetic model
    • Han S.L., and Juan H. Kinetics of glucose isomerization to fructose by immobilized glucose isomerase: anomeric reactivity of d-glucose in kinetic model. J Biotechnol 84 (2000) 145-153
    • (2000) J Biotechnol , vol.84 , pp. 145-153
    • Han, S.L.1    Juan, H.2
  • 43
    • 0031825756 scopus 로고    scopus 로고
    • Immobilization of glucose isomerase and its application in continuous production of high fructose syrup
    • Ge Y.B., Zhou H., Kong W., Tong Y., Wang S.Y., and Li W. Immobilization of glucose isomerase and its application in continuous production of high fructose syrup. Appl Biochem Biotech 69 (1998) 203-215
    • (1998) Appl Biochem Biotech , vol.69 , pp. 203-215
    • Ge, Y.B.1    Zhou, H.2    Kong, W.3    Tong, Y.4    Wang, S.Y.5    Li, W.6
  • 44
    • 33646094220 scopus 로고    scopus 로고
    • Immobilization and characterization of laccase from Chinese Rhus vernicifera on modified chitosan
    • Yang W.Y., Min D.Y., Wen S.X., Jin L., Rong L., Tetsuo M., et al. Immobilization and characterization of laccase from Chinese Rhus vernicifera on modified chitosan. Process Biochem 41 (2006) 1378-1382
    • (2006) Process Biochem , vol.41 , pp. 1378-1382
    • Yang, W.Y.1    Min, D.Y.2    Wen, S.X.3    Jin, L.4    Rong, L.5    Tetsuo, M.6
  • 45
    • 0033978162 scopus 로고    scopus 로고
    • Oxirane-immobilized Lentinus edodes laccase: stability and phenolics removal efficiency in olive mill wastewater
    • D'Annibale A., Stazi S.R., Vinciguerra V., and Sermanni G.G. Oxirane-immobilized Lentinus edodes laccase: stability and phenolics removal efficiency in olive mill wastewater. J Biotechnol 77 (2000) 265-273
    • (2000) J Biotechnol , vol.77 , pp. 265-273
    • D'Annibale, A.1    Stazi, S.R.2    Vinciguerra, V.3    Sermanni, G.G.4
  • 46
    • 0036362884 scopus 로고    scopus 로고
    • Laccase stabilization by covalent binding immobilization on activated polyvinyl alcohol carrier
    • Yinghui D., Qiuling W., and Shiyu F. Laccase stabilization by covalent binding immobilization on activated polyvinyl alcohol carrier. Lett Appl Microbiol 35 (2002) 451-456
    • (2002) Lett Appl Microbiol , vol.35 , pp. 451-456
    • Yinghui, D.1    Qiuling, W.2    Shiyu, F.3
  • 47
    • 33746837687 scopus 로고    scopus 로고
    • Immobilization of laccase on amine-terminated magnetic nano-composite by glutaraldehyde crosslinking method
    • Xiao H., Huang J., Liu C., and Jiang D. Immobilization of laccase on amine-terminated magnetic nano-composite by glutaraldehyde crosslinking method. T Nonferr Metal Soc 16 (2006) 414-418
    • (2006) T Nonferr Metal Soc , vol.16 , pp. 414-418
    • Xiao, H.1    Huang, J.2    Liu, C.3    Jiang, D.4
  • 48
    • 0032840163 scopus 로고    scopus 로고
    • Laccase-catalyzed decolorization of synthetic dyes
    • Wong Y., and Yu J. Laccase-catalyzed decolorization of synthetic dyes. Water Res 33 (1999) 3512-3520
    • (1999) Water Res , vol.33 , pp. 3512-3520
    • Wong, Y.1    Yu, J.2
  • 49
    • 0242585298 scopus 로고    scopus 로고
    • Grape seeds: the best lignocellulosic waste to produce laccase by solid state cultures of Trametes hirsuta
    • Moldes D., Gallego P.P., Rodríguez Couto S., and Sanromán A. Grape seeds: the best lignocellulosic waste to produce laccase by solid state cultures of Trametes hirsuta. Biotechnol Lett 25 (2003) 491-495
    • (2003) Biotechnol Lett , vol.25 , pp. 491-495
    • Moldes, D.1    Gallego, P.P.2    Rodríguez Couto, S.3    Sanromán, A.4
  • 50
    • 10644225079 scopus 로고    scopus 로고
    • Chestnut shell and barley bran as potential substrates for laccase production by Coriolopsis rigida under solid-state conditions
    • Gomez J., Pazos M., Rodríguez Couto S., and Sanromán M.A. Chestnut shell and barley bran as potential substrates for laccase production by Coriolopsis rigida under solid-state conditions. J Food Eng 68 (2005) 315-319
    • (2005) J Food Eng , vol.68 , pp. 315-319
    • Gomez, J.1    Pazos, M.2    Rodríguez Couto, S.3    Sanromán, M.A.4
  • 51
    • 0042694643 scopus 로고    scopus 로고
    • Immobilized laccase for decolourization of Reactive Black 5 dyeing effluent
    • Zille A., Tzanov T., Gübitz G.M., and Cavaco-Paulo A. Immobilized laccase for decolourization of Reactive Black 5 dyeing effluent. Biotechnol Lett 25 (2003) 1473-1477
    • (2003) Biotechnol Lett , vol.25 , pp. 1473-1477
    • Zille, A.1    Tzanov, T.2    Gübitz, G.M.3    Cavaco-Paulo, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.