메뉴 건너뛰기




Volumn 33, Issue 4, 2013, Pages 404-418

Laccase immobilization and insolubilization: From fundamentals to applications for the elimination of emerging contaminants in wastewater treatment

Author keywords

Bioreactor; Combination of cross linked enzyme aggregates; Emerging contaminants; Enzyme polymer engineered structures; Laccases; Wastewater treatment

Indexed keywords

CATALYTIC MECHANISMS; CROSS-LINKED ENZYME AGGREGATES; EMERGING CONTAMINANT; ENGINEERED STRUCTURES; ENVIRONMENTAL MATRIXES; IMMOBILIZATION TECHNIQUE; LACCASE IMMOBILIZATIONS; LACCASES;

EID: 84886769769     PISSN: 07388551     EISSN: 15497801     Source Type: Journal    
DOI: 10.3109/07388551.2012.725390     Document Type: Review
Times cited : (135)

References (148)
  • 2
    • 0036741954 scopus 로고    scopus 로고
    • Treatment of 2, 4-dichlorophenol polluted soil with free and immobilized laccase
    • Ahn MY, Dec J, Kim JE, Bollag JM. 2002. Treatment of 2, 4-dichlorophenol polluted soil with free and immobilized laccase. J Environ Qual 31: 1509-1515.
    • (2002) J Environ Qual , vol.31 , pp. 1509-1515
    • Ahn, M.Y.1    Dec, J.2    Kim, J.E.3    Bollag, J.M.4
  • 3
    • 0018786670 scopus 로고
    • The mechanism of electron transfer in laccase-catalysed reactions
    • Andréasson LE, Reinhammar B. 1979. The mechanism of electron transfer in laccase-catalysed reactions. Biochim Biophys Acta 568: 145-156.
    • (1979) Biochim Biophys Acta , vol.568 , pp. 145-156
    • Andréasson, L.E.1    Reinhammar, B.2
  • 5
    • 84869067264 scopus 로고    scopus 로고
    • Laccase-Based CLEAs: Chitosan as a Novel Cross-Linking Agent
    • Arsenault A, Cabana H, Jones JP. 2011. Laccase-Based CLEAs: Chitosan as a Novel Cross-Linking Agent. Enzyme Res 2011: 376015.
    • (2011) Enzyme Res , vol.2011 , pp. 376015
    • Arsenault, A.1    Cabana, H.2    Jones, J.P.3
  • 6
    • 33746674432 scopus 로고    scopus 로고
    • Natural and synthetic hormone removal using the horseradish peroxidase enzyme: Temperature and pH effects
    • DOI 10.1016/j.watres.2006.05.032, PII S0043135406003228
    • Auriol M, Filali-Meknassi Y, Adams CD, Tyagi RD. 2006. Natural and synthetic hormone removal using the horseradish peroxidase enzyme: temperature and pH efects. Water Res 40: 2847-2856. (Pubitemid 44164487)
    • (2006) Water Research , vol.40 , Issue.15 , pp. 2847-2856
    • Auriol, M.1    Filali-Meknassi, Y.2    Adams, C.D.3    Tyagi, R.D.4
  • 7
    • 36148946023 scopus 로고    scopus 로고
    • Removal of estrogenic activity of natural and synthetic hormones from a municipal wastewater: Efficiency of horseradish peroxidase and laccase from Trametes versicolor
    • DOI 10.1016/j.chemosphere.2007.06.064, PII S0045653507008478
    • Auriol M, Filali-Meknassi Y, Adams CD, Tyagi RD, Noguerol TN, Piña B. 2008. Removal of estrogenic activity of natural and synthetic hormones from a municipal wastewater: efciency of horseradish peroxidase and laccase from Trametes versicolor. Chemosphere 70: 445-452. (Pubitemid 350110464)
    • (2008) Chemosphere , vol.70 , Issue.3 , pp. 445-452
    • Auriol, M.1    Filali-Meknassi, Y.2    Adams, C.D.3    Tyagi, R.D.4    Noguerol, T.-N.5    Pina, B.6
  • 8
    • 34447097725 scopus 로고    scopus 로고
    • Laccase-catalyzed conversion of natural and synthetic hormones from a municipal wastewater
    • DOI 10.1016/j.watres.2007.05.008, PII S0043135407003053
    • Auriol M, Filali-Meknassi Y, Tyagi RD, Adams CD. 2007. Laccase-catalyzed conversion of natural and synthetic hormones from a municipal wastewater. Water Res 41: 3281-3288. (Pubitemid 47031276)
    • (2007) Water Research , vol.41 , Issue.15 , pp. 3281-3288
    • Auriol, M.1    Filali-Meknassi, Y.2    Tyagi, R.D.3    Adams, C.D.4
  • 9
    • 0027645602 scopus 로고
    • The fungus among us: Use of white rot fungi to biodegrade environmental pollutants
    • Aust SD, Benson JT. 1993. The fungus among us: use of white rot fungi to biodegrade environmental pollutants. Environ Health Perspect 101: 232-233.
    • (1993) Environ Health Perspect , vol.101 , pp. 232-233
    • Aust, S.D.1    Benson, J.T.2
  • 10
    • 38049085641 scopus 로고    scopus 로고
    • Preparation of cross-linked tyrosinase aggregates
    • Aytar BS, Bakir U. 2008. Preparation of cross-linked tyrosinase aggregates. Process Biochemi 43:125-131.
    • (2008) Process Biochemi , vol.43 , pp. 125-131
    • Aytar, B.S.1    Bakir, U.2
  • 11
    • 33645027271 scopus 로고    scopus 로고
    • Fungal laccases-occurrence and properties
    • Baldrian P. 2006. Fungal laccases-occurrence and properties. FEMS Microbiol Rev 30: 215-242.
    • (2006) FEMS Microbiol Rev , vol.30 , pp. 215-242
    • Baldrian, P.1
  • 12
    • 77953612325 scopus 로고    scopus 로고
    • Preparation and characterization of epoxy-functionalized magnetic chitosan beads: Laccase immobilized for degradation of reactive dyes
    • Bayramoglu G, Yilmaz M, Yakup Arica M. 2010. Preparation and characterization of epoxy-functionalized magnetic chitosan beads: laccase immobilized for degradation of reactive dyes. Bioprocess Biosyst Eng 33: 439-448.
    • (2010) Bioprocess Biosyst Eng , vol.33 , pp. 439-448
    • Bayramoglu, G.1    Yilmaz, M.2    Yakup Arica, M.3
  • 13
    • 0033015289 scopus 로고    scopus 로고
    • Analysis and occurrence of estrogenic hormones and their glucuronides in surface water and waste water in The Netherlands
    • DOI 10.1016/S0048-9697(98)00336-2, PII S0048969798003362
    • Belfroid AC, Van der Horst A, Vethaak AD, Schäfer AJ, Rijs GB, Wegener J, Cofno WP. 1999. Analysis and occurrence of estrogenic hormones and their glucuronides in surface water and waste water in The Netherlands. Sci Total Environ 225: 101-108. (Pubitemid 29148050)
    • (1999) Science of the Total Environment , vol.225 , Issue.1-2 , pp. 101-108
    • Belfroid, A.C.1    Van Der Horst, A.2    Vethaak, A.D.3    Schafer, A.J.4    Rijs, G.B.J.5    Wegener, J.6    Cofino, W.P.7
  • 14
    • 0030838432 scopus 로고    scopus 로고
    • Characterization of the gene encoding an extracellular laccase of myceliophthora thermophila and analysis of the recombinant enzyme expressed in aspergillus oryzae
    • Berka RM, Schneider P, Golightly EJ, Brown SH, Madden M, Brown KM, Halkier T, Mondorf K, Xu F. 1997. Characterization of the gene encoding an extracellular laccase of Myceliophthora thermophila and analysis of the recombinant enzyme expressed in Aspergillus oryzae. Appl Environ Microbiol 63: 3151-3157. (Pubitemid 27337808)
    • (1997) Applied and Environmental Microbiology , vol.63 , Issue.8 , pp. 3151-3157
    • Berka, R.M.1    Schneider, P.2    Golightly, E.J.3    Brown, S.H.4    Madden, M.5    Brown, K.M.6    Halkier, T.7    Mondorf, K.8    Xu, F.9
  • 15
    • 0037062591 scopus 로고    scopus 로고
    • Crystal structure of a four-copper laccase complexed with an arylamine: Insights into substrate recognition and correlation with kinetics
    • DOI 10.1021/bi0201318
    • Bertrand T, Jolivalt C, Briozzo P, Caminade E, Joly N, Madzak C, Mougin C. 2002. Crystal structure of a four-copper laccase complexed with an arylamine: insights into substrate recognition and correlation with kinetics. Biochemistry 41: 7325-7333. (Pubitemid 34602449)
    • (2002) Biochemistry , vol.41 , Issue.23 , pp. 7325-7333
    • Bertrand, T.1    Jolivalt, C.2    Briozzo, P.3    Caminade, E.4    Joly, N.5    Madzak, C.6    Mougin, C.7
  • 16
    • 70350726193 scopus 로고    scopus 로고
    • Applications of chitin-and chitosan-derivatives for the detoxifcation of water and wastewater-A short review
    • Bhatnagar A, Sillanpää M. 2009. Applications of chitin-and chitosan-derivatives for the detoxifcation of water and wastewater-a short review. Adv Colloid Interface Sci 152: 26-38.
    • (2009) Adv Colloid Interface Sci , vol.152 , pp. 26-38
    • Bhatnagar, A.1    Sillanpää, M.2
  • 18
    • 0026616392 scopus 로고
    • Decontaminating soil with enzymes
    • Bollag JM. 1992. Decontaminating soil with enzymes. Environ Sci Technol 26:1876-1881.
    • (1992) Environ Sci Technol , vol.26 , pp. 1876-1881
    • Bollag, J.M.1
  • 20
    • 59649113519 scopus 로고    scopus 로고
    • A review of the efects of emerging contaminants in wastewater and options for their removal
    • Bolong N, Ismail AF, Salim MR, Matsuura T. 2009. A review of the efects of emerging contaminants in wastewater and options for their removal. Desalination 238:229-246.
    • (2009) Desalination , vol.238 , pp. 229-246
    • Bolong, N.1    Ismail, A.F.2    Salim, M.R.3    Matsuura, T.4
  • 21
    • 3042846929 scopus 로고    scopus 로고
    • Electrochemical analysis of the interactions of laccase mediators with lignin model compounds
    • DOI 10.1016/S0304-4165(97)00117-7, PII S0304416597001177
    • Bourbonnais R, Leech D, Paice MG. 1998. Electrochemical analysis of the interactions of laccase mediators with lignin model compounds. Biochim Biophys Acta 1379: 381-390. (Pubitemid 28127880)
    • (1998) Biochimica et Biophysica Acta - General Subjects , vol.1379 , Issue.3 , pp. 381-390
    • Bourbonnais, R.1    Leech, D.2    Paice, M.G.3
  • 22
    • 0025315157 scopus 로고
    • Oxidation of non-phenolic substrates. An expended role for laccase in lignin biodegradation
    • DOI 10.1016/0014-5793(90)80298-W
    • Bourbonnais R, Paice MG. 1990. Oxidation of non-phenolic substrates. An expanded role for laccase in lignin biodegradation. FEBS Lett 267: 99-102. (Pubitemid 20211711)
    • (1990) FEBS Letters , vol.267 , Issue.1 , pp. 99-102
    • Bourbonnais, R.1    Paice, M.G.2
  • 24
    • 0141959169 scopus 로고    scopus 로고
    • Concepts of nature in organic synthesis: Cascade catalysis and multistep conversions in concert
    • DOI 10.1021/op0340311
    • Bruggink A, Schoevaart R, Kieboom T. 2003. Concepts of nature in organic synthesis: cascade catalysis and multistep conversions in concert. Org Process Res Develop 7:622-640. (Pubitemid 37229652)
    • (2003) Organic Process Research and Development , vol.7 , Issue.5 , pp. 622-640
    • Bruggink, A.1    Schoevaart, R.2    Kieboom, T.3
  • 25
    • 78650693142 scopus 로고    scopus 로고
    • Conjugation of laccase from the white rot fungus Trametes versicolor to chitosan and its utilization for the elimination of triclosan
    • Cabana H, Ahamed A, Leduc R. 2011. Conjugation of laccase from the white rot fungus Trametes versicolor to chitosan and its utilization for the elimination of triclosan. Bioresour Technol 102: 1656-1662.
    • (2011) Bioresour Technol , vol.102 , pp. 1656-1662
    • Cabana, H.1    Ahamed, A.2    Leduc, R.3
  • 26
    • 33846297346 scopus 로고    scopus 로고
    • Elimination of endocrine disrupting chemicals nonylphenol and bisphenol A and personal care product ingredient triclosan using enzyme preparation from the white rot fungus Coriolopsis polyzona
    • DOI 10.1016/j.chemosphere.2006.10.037, PII S0045653506013695
    • Cabana H, Jiwan JL, Rozenberg R, Elisashvili V, Penninckx M, Agathos SN, Jones JP. 2007a. Elimination of endocrine disrupting chemicals nonylphenol and bisphenol A and personal care product ingredient triclosan using enzyme preparation from the white rot fungus Coriolopsis polyzona. Chemosphere 67: 770-778. (Pubitemid 46116799)
    • (2007) Chemosphere , vol.67 , Issue.4 , pp. 770-778
    • Cabana, H.1    Jiwan, J.-L.H.2    Rozenberg, R.3    Elisashvili, V.4    Penninckx, M.5    Agathos, S.N.6    Jones, J.P.7
  • 27
    • 34848883383 scopus 로고    scopus 로고
    • Preparation and characterization of cross-linked laccase aggregates and their application to the elimination of endocrine disrupting chemicals
    • DOI 10.1016/j.jbiotec.2007.07.948, PII S0168165607014216
    • Cabana H, Jones JP, Agathos SN. 2007b. Preparation and characterization of cross-linked laccase aggregates and their application to the elimination of endocrine disrupting chemicals. J Biotechnol 132: 23-31. (Pubitemid 47505372)
    • (2007) Journal of Biotechnology , vol.132 , Issue.1 , pp. 23-31
    • Cabana, H.1    Jones, J.P.2    Agathos, S.N.3
  • 28
    • 64949125943 scopus 로고    scopus 로고
    • Utilization of cross-linked laccase aggregates in a perfusion basket reactor for the continuous elimination of endocrine-disrupting chemicals
    • Cabana H, Jones JP, Agathos SN. 2009a. Utilization of cross-linked laccase aggregates in a perfusion basket reactor for the continuous elimination of endocrine-disrupting chemicals. Biotechnol Bioeng 102: 1582-1592.
    • (2009) Biotechnol Bioeng , vol.102 , pp. 1582-1592
    • Cabana, H.1    Jones, J.P.2    Agathos, S.N.3
  • 29
    • 64949178553 scopus 로고    scopus 로고
    • Immobilization of laccase from the white rot fungus Coriolopsis polyzona and use of the immobilized biocatalyst for the continuous elimination of endocrine disrupting chemicals
    • Cabana H, Alexandre C, Agathos SN, Jones JP. 2009b. Immobilization of laccase from the white rot fungus Coriolopsis polyzona and use of the immobilized biocatalyst for the continuous elimination of endocrine disrupting chemicals. Bioresour Technol 100: 3447-3458.
    • (2009) Bioresour Technol , vol.100 , pp. 3447-3458
    • Cabana, H.1    Alexandre, C.2    Agathos, S.N.3    Jones, J.P.4
  • 30
    • 0025984105 scopus 로고
    • Covalent and Coordination Immobilization of Proteins
    • Taylor R F, ed New York: Marcel Dekker
    • Cabral JMS, Kennedy JF. 1991. Covalent and coordination immobilization of proteins. In: Taylor R F, ed. Protein immobilization: fundamentals and applications. New York: Marcel Dekker, pp 73-138.
    • (1991) Protein Immobilization: Fundamentals and Applications , pp. 73-138
    • Jms, C.1    Kennedy, J.F.2
  • 31
    • 4243542277 scopus 로고    scopus 로고
    • History, overview and applications of mediated lignolytic systems, especially laccase-mediator-systems (Lignozym®-process)
    • DOI 10.1016/S0168-1656(97)01683-0, PII S0168165697016830
    • Call HP, Mucke I. 1997. History, overview and applications of mediated lignolytic systems, especially laccase-mediator-systems (Lignozym(R)-process). J Biotechnol 53:163-202. (Pubitemid 27286437)
    • (1997) Journal of Biotechnology , vol.53 , Issue.2-3 , pp. 163-202
    • Call, H.P.1    Mucke, I.2
  • 33
    • 16244405562 scopus 로고    scopus 로고
    • Immobilised enzymes: Science or art?
    • DOI 10.1016/j.cbpa.2005.02.014, Bioorganic Chemistry / Biocatalysis and Biotransformation
    • Cao L. 2005. Immobilised enzymes: science or art? Curr Opin Chem Biol 9: 217-226. (Pubitemid 40462493)
    • (2005) Current Opinion in Chemical Biology , vol.9 , Issue.2 , pp. 217-226
    • Cao, L.1
  • 34
    • 0041430560 scopus 로고    scopus 로고
    • Immobilised enzymes: Carrier-bound or carrier-free?
    • DOI 10.1016/S0958-1669(03)00096-X
    • Cao L, Langen L, Sheldon RA. 2003. Immobilised enzymes: carrier-bound or carrier-free? Curr Opin Biotechnol 14: 387-394. (Pubitemid 37011318)
    • (2003) Current Opinion in Biotechnology , vol.14 , Issue.4 , pp. 387-394
    • Cao, L.1    Van Langen, L.2    Sheldon, R.A.3
  • 35
    • 0036382007 scopus 로고    scopus 로고
    • Redox-mediated decolorization of synthetic dyes by fungal laccases
    • Claus H, Faber G, König H. 2002. Redox-mediated decolorization of synthetic dyes by fungal laccases. Appl Microbiol Biotechnol 59: 672-678.
    • (2002) Appl Microbiol Biotechnol , vol.59 , pp. 672-678
    • Claus, H.1    Faber, G.2    König, H.3
  • 36
    • 33746142419 scopus 로고    scopus 로고
    • Industrial and biotechnological applications of laccases: A review
    • Couto SR, Herrera JLT. 2006. Industrial and biotechnological applications of laccases: A review. Biotechnol Adv 24:500-513.
    • (2006) Biotechnol Adv , vol.24 , pp. 500-513
    • Couto, S.R.1    Herrera, J.L.T.2
  • 37
    • 33750806309 scopus 로고    scopus 로고
    • Inhibitors of laccases: A review
    • DOI 10.2174/157340806778699262
    • Couto SR, Toca JL. 2006. Inhibitors of laccases: A review. Current Enzyme Inhibition 2:343-352. (Pubitemid 44710285)
    • (2006) Current Enzyme Inhibition , vol.2 , Issue.4 , pp. 343-352
    • Couto, S.R.1    Toca, J.L.2
  • 38
    • 33846489558 scopus 로고    scopus 로고
    • Preparation and characterization of combi-CLEAs catalyzing multiple non-cascade reactions
    • DOI 10.1016/j.molcatb.2006.10.003, PII S1381117706003043
    • Dalal S, Kapoor M, Gupta MN. 2007. Preparation and characterization of combi-CLEAs catalyzing multiple non-cascade reactions. J Mol Catal B: Enz 44:128-132. (Pubitemid 46162271)
    • (2007) Journal of Molecular Catalysis B: Enzymatic , vol.44 , Issue.3-4 , pp. 128-132
    • Dalal, S.1    Kapoor, M.2    Gupta, M.N.3
  • 39
    • 0032851992 scopus 로고    scopus 로고
    • Characterization of immobilized laccase from Lentinula edodes and its use in olive-mill wastewater treatment
    • DOI 10.1016/S0032-9592(98)00144-7, PII S0032959298001447
    • D'Annibale A, Stazi SR, Vinciguerra V, Di Mattia E, Sermanni GG. 1999. Characterization of immobilized laccase from Lentinula edodes and its use in olive-mill wastewater treatment. Process Biochem (Barking, London, England), 34:697-706. (Pubitemid 29453235)
    • (1999) Process Biochemistry , vol.34 , Issue.6-7 , pp. 697-706
    • D'Annibale, A.1    Rita Stazi, S.2    Vinciguerra, V.3    Di Mattia, E.4    Giovannozzi Sermanni, G.5
  • 40
    • 0033978162 scopus 로고    scopus 로고
    • Oxirane-immobilized Lentinula edodes laccase: Stability and phenolics removal efficiency in olive mill wastewater
    • DOI 10.1016/S0168-1656(99)00224-2, PII S0168165699002242
    • D'Annibale A, Stazi SR, Vinciguerra V, Giovannozzi Sermanni G. 2000. Oxirane-immobilized Lentinula edodes laccase: stability and phenolics removal efciency in olive mill wastewater. J Biotechnol 77: 265-273. (Pubitemid 30055341)
    • (2000) Journal of Biotechnology , vol.77 , Issue.2-3 , pp. 265-273
    • D'Annibale, A.1    Stazi, S.R.2    Vinciguerra, V.3    Giovannozzi Sermanni, G.4
  • 41
    • 6344287585 scopus 로고    scopus 로고
    • Respiratory health survey of respiratory therapists
    • DOI 10.1378/chest.126.4.1048
    • Dimich-Ward H, Wymer ML, Chan-Yeung M. 2004. Respiratory health survey of respiratory therapists. Chest 126: 1048-1053. (Pubitemid 39391230)
    • (2004) Chest , vol.126 , Issue.4 , pp. 1048-1053
    • Dimich-Ward, H.1    Wymer, M.L.2    Chan-Yeung, M.3
  • 43
    • 0037010857 scopus 로고    scopus 로고
    • Applications of laccases and tyrosinases (phenoloxidases) immobilized on different supports: A review
    • DOI 10.1016/S0141-0229(02)00214-4, PII S0141022902002144
    • Duran N, Rosa MA, D'Annibale A, Gianfreda L. 2002. Applications of laccases and tyrosinases (phenoloxidases) immobilized on diferent supports: a review. Enzyme Microb Technol 31:907-931. (Pubitemid 35375750)
    • (2002) Enzyme and Microbial Technology , vol.31 , Issue.7 , pp. 907-931
    • Duran, N.1    Rosa, M.A.2    D'Annibale, A.3    Gianfreda, L.4
  • 44
    • 14244256770 scopus 로고    scopus 로고
    • Fate of glutaraldehyde in hospital wastewater and combined effects of glutaraldehyde and surfactants on aquatic organisms
    • DOI 10.1016/j.envint.2004.08.011, PII S0160412004001497
    • Emmanuel E, Hanna K, Bazin C, Keck G, Clément B, Perrodin Y. 2005. Fate of glutaraldehyde in hospital wastewater and combined efects of glutaraldehyde and surfactants on aquatic organisms. Environ Int 31: 399-406. (Pubitemid 40289169)
    • (2005) Environment International , vol.31 , Issue.3 , pp. 399-406
    • Emmanuel, E.1    Hanna, K.2    Bazin, C.3    Keck, G.4    Clement, B.5    Perrodin, Y.6
  • 45
    • 0015087478 scopus 로고
    • Enzyme insolubilization with cross-linked polyacryloylaminoacetaldehyde dimethylacetal
    • Epton R, McLaren JV, Tomas TH. 1971. Enzyme insolubilization with cross-linked polyacryloylaminoacetaldehyde dimethylacetal. Biochem J 123: 21P-22P.
    • (1971) Biochem J , vol.123
    • Epton, R.1    McLaren, J.V.2    Tomas, T.H.3
  • 46
    • 33749545520 scopus 로고    scopus 로고
    • Glutaraldehyde cross-linking of lipases adsorbed on aminated supports in the presence of detergents leads to improved performance
    • DOI 10.1021/bm060408+
    • Fernández-Lorente G, Palomo JM, Mateo C, Munilla R, Ortiz C, Cabrera Z, Guisán JM, Fernandez-Lafuente R. 2006. Glutaraldehyde cross-linking of lipases adsorbed on aminated supports in the presence of detergents leads to improved performance. Biomacromolecules 7: 2610-2615. (Pubitemid 44530500)
    • (2006) Biomacromolecules , vol.7 , Issue.9 , pp. 2610-2615
    • Fernandez-Lorente, G.1    Palomo, J.M.2    Mateo, C.3    Munilla, R.4    Ortiz, C.5    Cabrera, Z.6    Guisan, J.M.7    Fernandez-Lafuente, R.8
  • 47
    • 35948977727 scopus 로고    scopus 로고
    • Crystal structure of a blue laccase from Lentinus tigrinus: Evidences for intermediates in the molecular oxygen reductive splitting by multicopper oxidases
    • Ferraroni M, Myasoedova NM, Schmatchenko V, Leontievsky AA, Golovleva LA, Scozzafava A, Briganti F. 2007. Crystal structure of a blue laccase from Lentinus tigrinus: evidences for intermediates in the molecular oxygen reductive splitting by multicopper oxidases. BMC Struct Biol 7: 60.
    • (2007) BMC Struct Biol , vol.7 , pp. 60
    • Ferraroni, M.1    Myasoedova, N.M.2    Schmatchenko, V.3    Leontievsky, A.A.4    Golovleva, L.A.5    Scozzafava, A.6    Briganti, F.7
  • 48
    • 0000619737 scopus 로고
    • The reaction of formaldehyde with proteins; Demonstration of intermolecular cross-linking by means of osmotic pressure measurements
    • Fraenkel-Conrat H, Mecham DK. 1949. The reaction of formaldehyde with proteins; demonstration of intermolecular cross-linking by means of osmotic pressure measurements. J Biol Chem 177: 477-486.
    • (1949) J Biol Chem , vol.177 , pp. 477-486
    • Fraenkel-Conrat, H.1    Mecham, D.K.2
  • 52
    • 4444352552 scopus 로고    scopus 로고
    • The structure of Rigidoporus lignosus laccase containing a full complement of copper ions, reveals an asymmetrical arrangement for the T3 copper pair
    • DOI 10.1016/j.jmb.2004.07.100, PII S0022283604009544
    • Garavaglia S, Cambria MT, Miglio M, Ragusa S, Iacobazzi V, Palmieri F, D'Ambrosio C, Scaloni A, Rizzi M. 2004. The structure of Rigidoporus lignosus Laccase containing a full complement of copper ions, reveals an asymmetrical arrangement for the T3 copper pair. J Mol Biol 342: 1519-1531. (Pubitemid 39208675)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.5 , pp. 1519-1531
    • Garavaglia, S.1    Teresa Cambria, M.2    Miglio, M.3    Ragusa, S.4    Iacobazzi, V.5    Palmieri, F.6    D'Ambrosio, C.7    Scaloni, A.8    Rizzi, M.9
  • 53
    • 79951578053 scopus 로고    scopus 로고
    • Laccase-catalyzed oxidation of oxybenzone in municipal wastewater primary efuent
    • Garcia HA, Hofman CM, Kinney KA, Lawler DF. 2011. Laccase-catalyzed oxidation of oxybenzone in municipal wastewater primary efuent. Water Res 45: 1921-1932.
    • (2011) Water Res , vol.45 , pp. 1921-1932
    • Garcia, H.A.1    Hofman, C.M.2    Kinney, K.A.3    Lawler, D.F.4
  • 55
    • 0009998247 scopus 로고
    • Properties of gallic acid-induced extracellular laccase of Botrytis cinerea
    • Gigi O, Marbach I, Mayer AM. 1981. Properties of gallic acid-induced extracellular laccase of Botrytis cinerea. Phytochemistry 20:1211-1213.
    • (1981) Phytochemistry , vol.20 , pp. 1211-1213
    • Gigi, O.1    Marbach, I.2    Mayer, A.M.3
  • 56
    • 0025057308 scopus 로고
    • Stability of water-soluble carbodiimides in aqueous solution
    • Gilles MA, Hudson AQ, Borders CL Jr. 1990. Stability of water-soluble carbodiimides in aqueous solution. Anal Biochem 184: 244-248. (Pubitemid 20055618)
    • (1990) Analytical Biochemistry , vol.184 , Issue.2 , pp. 244-248
    • Gilles, M.A.1    Hudson, A.Q.2    Borders Jr., C.L.3
  • 57
    • 84873513475 scopus 로고
    • Die Umsetzung des Caseins mit Formaldehyd. V. Über das verhalten der ε-aminogruppen des lysins und der peptidgruppen
    • Hadorn H, Nitschmann HH. 1944. Die Umsetzung des Caseins mit Formaldehyd. V. Über das verhalten der ε-aminogruppen des lysins und der peptidgruppen. Helvetica Chimica Acta 27:299-312.
    • (1944) Helvetica Chimica Acta , vol.27 , pp. 299-312
    • Hadorn, H.1    Nitschmann, H.H.2
  • 58
    • 0014310023 scopus 로고
    • Reaction of proteins with glutaraldehyde
    • Habeeb AJ, Hiramoto R. 1968. Reaction of proteins with glutaraldehyde. Arch Biochem Biophys 126: 16-26.
    • (1968) Arch Biochem Biophys , vol.126 , pp. 16-26
    • Habeeb, A.J.1    Hiramoto, R.2
  • 61
    • 79951852806 scopus 로고    scopus 로고
    • Untapped potential: Exploiting fungi in bioremediation of hazardous chemicals
    • Harms H, Schlosser D, Wick LY. 2011. Untapped potential: exploiting fungi in bioremediation of hazardous chemicals. Nat Rev Microbiol 9: 177-192.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 177-192
    • Harms, H.1    Schlosser, D.2    Wick, L.Y.3
  • 62
    • 58749085015 scopus 로고    scopus 로고
    • Improvement of chymotrypsin enzyme stability as single enzyme nanoparticles
    • Hegedus I, Nagy E. 2009. Improvement of chymotrypsin enzyme stability as single enzyme nanoparticles. Chem Eng Sci 64:1053-1060.
    • (2009) Chem Eng Sci , vol.64 , pp. 1053-1060
    • Hegedus, I.1    Nagy, E.2
  • 63
    • 0006021462 scopus 로고
    • The reaction of formaldehyde with proteins. V. Cross-linking between Amino and Primary Amide or Guanidyl Groups
    • Heinz Fraenkel-Conrat, Olcott HS. 1948. The reaction of formaldehyde with proteins. V. Cross-linking between Amino and Primary Amide or Guanidyl Groups. J Am Chem Soc 70:2673-2684.
    • (1948) J Am Chem Soc , vol.70 , pp. 2673-2684
    • Fraenkel-Conrat, H.1    Olcott, H.S.2
  • 65
    • 2942517661 scopus 로고    scopus 로고
    • Immobilization of cross-linked lipase aggregates within microporous polymeric membranes
    • DOI 10.1016/j.memsci.2004.04.002, PII S0376738804002303
    • Hilal N, Nigmatullin R, Alpatova A. 2004. Immobilization of cross-linked lipase aggregates within microporous polymeric membranes. J Memb Sci 238:131-141. (Pubitemid 38739506)
    • (2004) Journal of Membrane Science , vol.238 , Issue.1-2 , pp. 131-141
    • Hilal, N.1    Nigmatullin, R.2    Alpatova, A.3
  • 66
    • 33750524054 scopus 로고    scopus 로고
    • Facile preparation of an enzyme-immobilized microreactor using a cross-linking enzyme membrane on a microchannel surface
    • DOI 10.1002/adsc.200606224
    • Honda T, Miyazaki M, Nakamura H, Maeda H. 2006. Facile preparation of an enzyme-immobilized microreactor using a cross-linking enzyme membrane on a microchannel surface. Adv Synth Catal 348:2163-2171. (Pubitemid 44662644)
    • (2006) Advanced Synthesis and Catalysis , vol.348 , Issue.15 , pp. 2163-2171
    • Honda, T.1    Miyazaki, M.2    Nakamura, H.3    Maeda, H.4
  • 67
    • 27644480768 scopus 로고    scopus 로고
    • Immobilization of enzymes on a microchannel surface through cross-linking polymerization
    • DOI 10.1039/b510605b
    • Honda T, Miyazaki M, Nakamura H, Maeda H. 2005. Immobilization of enzymes on a microchannel surface through cross-linking polymerization. Chem Commun (Camb): 5062-5064. (Pubitemid 41566433)
    • (2005) Chemical Communications , Issue.40 , pp. 5062-5064
    • Honda, T.1    Miyazaki, M.2    Nakamura, H.3    Maeda, H.4
  • 68
    • 0033971693 scopus 로고    scopus 로고
    • Natural mediators in the oxidation of polycyclic aromatic hydrocarbons by laccase mediator systems
    • DOI 10.1128/AEM.66.2.524-528.2000
    • Johannes C, Majcherczyk A. 2000. Natural mediators in the oxidation of polycyclic aromatic hydrocarbons by laccase mediator systems. Appl Environ Microbiol 66: 524-528. (Pubitemid 30082736)
    • (2000) Applied and Environmental Microbiology , vol.66 , Issue.2 , pp. 524-528
    • Johannes, C.1    Majcherczyk, A.2
  • 69
    • 80255134545 scopus 로고    scopus 로고
    • Preparation of chitosan-coated magnetite nanoparticles and application for immobilization of laccase
    • Kalkan NA, Aksoy S, Aksoy EA, Hasirci N. 2012. Preparation of chitosan-coated magnetite nanoparticles and application for immobilization of laccase. J Appl Poly Sci 123:707-716.
    • (2012) J Appl Poly Sci , vol.123 , pp. 707-716
    • Kalkan, N.A.1    Aksoy, S.2    Aksoy, E.A.3    Hasirci, N.4
  • 70
    • 80051483501 scopus 로고    scopus 로고
    • Crystal structure of an ascomycete fungal laccase from Tielavia arenaria-common structural features of asco-laccases
    • Kallio JP, Gasparetti C, Andberg M, Boer H, Koivula A, Kruus K, Rouvinen J, Hakulinen N. 2011. Crystal structure of an ascomycete fungal laccase from Tielavia arenaria-common structural features of asco-laccases. FEBS J 278: 2283-2295.
    • (2011) FEBS J , vol.278 , pp. 2283-2295
    • Kallio, J.P.1    Gasparetti, C.2    Andberg, M.3    Boer, H.4    Koivula, A.5    Kruus, K.6    Rouvinen, J.7    Hakulinen, N.8
  • 71
    • 82455188098 scopus 로고    scopus 로고
    • Nano reengineering of horseradish peroxidase with dendritic macromolecules for stability enhancement
    • Khosravi A, Vossoughi M, Shahrokhian S, Alemzadeh I. 2012. Nano reengineering of horseradish peroxidase with dendritic macromolecules for stability enhancement. Enzyme Microb Technol 50: 10-16.
    • (2012) Enzyme Microb Technol , vol.50 , pp. 10-16
    • Khosravi, A.1    Vossoughi, M.2    Shahrokhian, S.3    Alemzadeh, I.4
  • 73
    • 0141684517 scopus 로고    scopus 로고
    • Single-enzyme nanoparticles armored by a nanometer-scale organic/inorganic network
    • DOI 10.1021/nl034404b
    • Kim J, Grate JW. 2003. Single-enzyme nanoparticles armored by a nanometer-scale organic/inorganic network. Nano Letters 3:1219-1222. (Pubitemid 37206066)
    • (2003) Nano Letters , vol.3 , Issue.9 , pp. 1219-1222
    • Kim, J.1    Grate, J.W.2
  • 74
    • 27844518415 scopus 로고    scopus 로고
    • Nanostructures for enzyme stabilization
    • DOI 10.1016/j.ces.2005.05.067, PII S0009250905004999, Biomolecular Engineering
    • Kim J, Grate JW, Wang P. 2006. Nanostructures for enzyme stabilization. Chem Eng Sci 61:1017-1026. (Pubitemid 41655855)
    • (2006) Chemical Engineering Science , vol.61 , Issue.3 , pp. 1017-1026
    • Kim, J.1    Grate, J.W.2    Wang, P.3
  • 75
    • 33645219681 scopus 로고    scopus 로고
    • Laccase-catalyzed oxidation of bisphenol A with the aid of additives
    • Kim YJ, Nicell JA. 2006. Laccase-catalyzed oxidation of bisphenol A with the aid of additives. Process Biochem, 41:1029-1037.
    • (2006) Process Biochem , vol.41 , pp. 1029-1037
    • Kim, Y.J.1    Nicell, J.A.2
  • 76
    • 0344825085 scopus 로고    scopus 로고
    • Rejection of organic micropollutants (disinfection by-products, endocrine disrupting compounds, and pharmaceutically active compounds) by NF/RO membranes
    • DOI 10.1016/j.memsci.2003.09.005
    • Kimura K, Amy G, Drewes JE, Heberer T, Kim T, Watanabe Y. 2003. Rejection of organic micropollutants (disinfection by-products, endocrine disrupting compounds, and pharmaceutically active compounds) by NF/RO membranes. J Memb Sci 227:113-121. (Pubitemid 37476341)
    • (2003) Journal of Membrane Science , vol.227 , Issue.1-2 , pp. 113-121
    • Kimura, K.1    Amy, G.2    Drewes, J.E.3    Heberer, T.4    Kim, T.-U.5    Watanabe, Y.6
  • 77
    • 77953335446 scopus 로고    scopus 로고
    • Efect of molecular shape on rejection of uncharged organic compounds by nanofltration membranes and on calculated pore radii
    • Kiso Y, Muroshige K, Oguchi T, Yamada T, Hirose M, Ohara T, Shintani T. 2010. Efect of molecular shape on rejection of uncharged organic compounds by nanofltration membranes and on calculated pore radii. J Memb Sci 358:101-113.
    • (2010) J Memb Sci , vol.358 , pp. 101-113
    • Kiso, Y.1    Muroshige, K.2    Oguchi, T.3    Yamada, T.4    Hirose, M.5    Ohara, T.6    Shintani, T.7
  • 78
    • 3142763845 scopus 로고    scopus 로고
    • Application of chitin- and chitosan-based materials for enzyme immobilizations: A review
    • DOI 10.1016/j.enzmictec.2003.12.013, PII S0141022904001231
    • Krajewska B. 2004. Application of chitin-and chitosan-based materials for enzyme immobilizations: a review. Enz Microbial Technol 35:126-139. (Pubitemid 38906662)
    • (2004) Enzyme and Microbial Technology , vol.35 , Issue.2-3 , pp. 126-139
    • Krajewska, B.1
  • 80
    • 0014074505 scopus 로고
    • Advances in the chemistry of carbodiimides
    • Kurzer F, Douraghi-Zadeh K. 1967. Advances in the chemistry of carbodiimides. Chem Rev 67: 107-152.
    • (1967) Chem Rev , vol.67 , pp. 107-152
    • Kurzer, F.1    Douraghi-Zadeh, K.2
  • 81
    • 0035266384 scopus 로고    scopus 로고
    • Development of self-heating microreactor for catalytic reactions
    • Kusakabe K, Miyagawa D, Gu Y, Maeda H, Morooka S. 2001. Development of self-heating microreactor for catalytic reactions. J Chem Eng Jpn 34:441-443.
    • (2001) J Chem Eng Jpn , vol.34 , pp. 441-443
    • Kusakabe, K.1    Miyagawa, D.2    Gu, Y.3    Maeda, H.4    Morooka, S.5
  • 84
    • 0035007475 scopus 로고    scopus 로고
    • Ecotoxicology of glutaraldehyde: Review of environmental fate and efects studies
    • Leung HW. 2001. Ecotoxicology of glutaraldehyde: review of environmental fate and efects studies. Ecotoxicol Environ Saf 49: 26-39.
    • (2001) Ecotoxicol Environ Saf , vol.49 , pp. 26-39
    • Leung, H.W.1
  • 85
    • 0033050135 scopus 로고    scopus 로고
    • Comparison of fungal laccases and redox mediators in oxidation of a nonphenolic lignin model compound
    • Li K, Xu F, Eriksson KE. 1999. Comparison of fungal laccases and redox mediators in oxidation of a nonphenolic lignin model compound. Appl Environ Microbiol 65: 2654-2660.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 2654-2660
    • Li, K.1    Xu, F.2    Eriksson, K.E.3
  • 87
    • 56949105543 scopus 로고    scopus 로고
    • Removal mechanisms for endocrine disrupting compounds (EDCs) in wastewater treatment-physical means, biodegradation, and chemical advanced oxidation: A review
    • Liu ZH, Kanjo Y, Mizutani S. 2009b. Removal mechanisms for endocrine disrupting compounds (EDCs) in wastewater treatment-physical means, biodegradation, and chemical advanced oxidation: a review. Sci Total Environ 407: 731-748.
    • (2009) Sci Total Environ , vol.407 , pp. 731-748
    • Zh, L.1    Kanjo, Y.2    Mizutani, S.3
  • 88
    • 0030617256 scopus 로고    scopus 로고
    • A multiphase/extractive enzyme membrane reactor for production of diltiazem chiral intermediate
    • Lopez JL, Matson SL. 1997. A multiphase/extractive enzyme membrane reactor for production of diltiazem chiral intermediate. J Memb Sci 125:189-211.
    • (1997) J Memb Sci , vol.125 , pp. 189-211
    • Lopez, J.L.1    Matson, S.L.2
  • 90
    • 77950488214 scopus 로고    scopus 로고
    • Laccase: Properties and Applications
    • Madhavi V, Lele SS. 2009. Laccase: Properties and Applications. BioResources 4:1694-1717.
    • (2009) BioResources , vol.4 , pp. 1694-1717
    • Madhavi, V.1    Lele, S.S.2
  • 91
    • 77951217331 scopus 로고    scopus 로고
    • Laccases for removal of recalcitrant and emerging pollutants
    • Majeau JA, Brar SK, Tyagi RD. 2010. Laccases for removal of recalcitrant and emerging pollutants. Bioresour Technol 101: 2331-2350.
    • (2010) Bioresour Technol , vol.101 , pp. 2331-2350
    • Majeau, J.A.1    Brar, S.K.2    Tyagi, R.D.3
  • 92
    • 0009365216 scopus 로고    scopus 로고
    • A review of chitin and chitosan applications
    • Majeti NVRK. 2000. A review of chitin and chitosan applications. React Funct Poly 46:1-27.
    • (2000) React Funct Poly , vol.46 , pp. 1-27
    • Majeti, N.V.R.K.1
  • 93
    • 0000612588 scopus 로고
    • Molecular properties of extracellular Botrytis cinerea laccase
    • Marbach I, Harel E, Mayer AM. 1984. Molecular properties of extracellular Botrytis cinerea laccase. Phytochemistry 23:2713-2717.
    • (1984) Phytochemistry , vol.23 , pp. 2713-2717
    • Marbach, I.1    Harel, E.2    Mayer, A.M.3
  • 95
    • 33947602594 scopus 로고    scopus 로고
    • Improvement of enzyme activity, stability and selectivity via immobilization techniques
    • DOI 10.1016/j.enzmictec.2007.01.018, PII S0141022907000506
    • Mateo C, Palomo JM, Fernandez-Lorente G, Guisan JM, Fernandez-Lafuente R. 2007. Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enz Microbial Technol 40:1451-1463. (Pubitemid 46482654)
    • (2007) Enzyme and Microbial Technology , vol.40 , Issue.6 , pp. 1451-1463
    • Mateo, C.1    Palomo, J.M.2    Fernandez-Lorente, G.3    Guisan, J.M.4    Fernandez-Lafuente, R.5
  • 99
    • 0025058305 scopus 로고
    • The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships
    • DOI 10.1111/j.1432-1033.1990.tb15311.x
    • Messerschmidt A, Huber R. 1990. The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships. Eur J Biochem 187: 341-352. (Pubitemid 20040393)
    • (1990) European Journal of Biochemistry , vol.187 , Issue.2 , pp. 341-352
    • Messerschmidt, A.1    Huber, R.2
  • 100
    • 8444230519 scopus 로고    scopus 로고
    • Glutaraldehyde: Behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking
    • 798
    • Migneault I, Dartiguenave C, Bertrand MJ, Waldron KC. 2004. Glutaraldehyde: behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking. BioTechniques 37: 790-6, 798.
    • (2004) BioTechniques , vol.37 , pp. 790-6
    • Migneault, I.1    Dartiguenave, C.2    Bertrand, M.J.3    Waldron, K.C.4
  • 101
    • 0018125578 scopus 로고
    • The phenoloxidases of the ascomycete Podospora anserina. Structural differences between laccases of high and low molecular weight
    • Minuth W, Klischies M, Esser K. 1978. The phenoloxidases of the ascomycete Podospora anserina. Structural diferences between laccases of high and low molecular weight. Eur J Biochem 90: 73-82. (Pubitemid 9013128)
    • (1978) European Journal of Biochemistry , vol.90 , Issue.1 , pp. 73-82
    • Minuth, W.1    Klischies, M.2    Esser, K.3
  • 103
    • 0029181831 scopus 로고
    • Mechanism of amide formation by carbodiimide for bioconjugation in aqueous media
    • Nakajima N, Ikada Y. 1995. Mechanism of amide formation by carbodiimide for bioconjugation in aqueous media. Bioconjug Chem 6: 123-130.
    • (1995) Bioconjug Chem , vol.6 , pp. 123-130
    • Nakajima, N.1    Ikada, Y.2
  • 104
    • 0036865774 scopus 로고    scopus 로고
    • Adsorption and transport of trace contaminant estrone in NF/RO membranes
    • Nghiem LD, Schäfer AI. 2002. Adsorption and transport of trace contaminant estrone in NF/RO membranes. Environ Eng Sci 19:441-451. (Pubitemid 36020037)
    • (2002) Environmental Engineering Science , vol.19 , Issue.6 , pp. 441-451
    • Nghiem, L.D.1    Schafer, A.I.2
  • 107
    • 0037082725 scopus 로고    scopus 로고
    • Characterization of porous collagen/hyaluronic acid scaffold modified by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide cross-linking
    • DOI 10.1016/S0142-9612(01)00235-6, PII S0142961201002356
    • Park SN, Park JC, Kim HO, Song MJ, Suh H. 2002. Characterization of porous collagen/hyaluronic acid scafold modifed by 1-ethyl-3-(3- dimethylaminopropyl)carbodiimide cross-linking. Biomaterials 23: 1205-1212. (Pubitemid 33109052)
    • (2002) Biomaterials , vol.23 , Issue.4 , pp. 1205-1212
    • Park, S.-N.1    Park, J.-C.2    Kim, H.O.3    Song, M.J.4    Suh, H.5
  • 108
    • 0037020063 scopus 로고    scopus 로고
    • Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers
    • Piontek K, Antorini M, Choinowski T. 2002. Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers. J Biol Chem 277: 37663-37669.
    • (2002) J Biol Chem , vol.277 , pp. 37663-37669
    • Piontek, K.1    Antorini, M.2    Choinowski, T.3
  • 109
    • 84856564571 scopus 로고    scopus 로고
    • A systematic study on triazine retention by fouled with humic substances NF/ULPRO membranes
    • Plakas KV, Karabelas AJ. 2011. A systematic study on triazine retention by fouled with humic substances NF/ULPRO membranes. Sep PurifTechnol 80:246-261.
    • (2011) Sep PurifTechnol , vol.80 , pp. 246-261
    • Plakas, K.V.1    Karabelas, A.J.2
  • 110
    • 78651149328 scopus 로고
    • Intermolecular cross linking of a protein in the crystalline state: Carboxypeptidase-A
    • Quiocho FA, Richards FM. 1964. Intermolecular cross linking of a protein in the crystalline state: carboxypeptidase-A. Proc Natl Acad Sci USA 52: 833-839.
    • (1964) Proc Natl Acad Sci USA , vol.52 , pp. 833-839
    • Quiocho, F.A.1    Richards, F.M.2
  • 111
    • 78951481967 scopus 로고    scopus 로고
    • Bacillus pumilus laccase: A heat stable enzyme with a wide substrate spectrum
    • Reiss R, Ihssen J, Töny-Meyer L. 2011. Bacillus pumilus laccase: a heat stable enzyme with a wide substrate spectrum. BMC Biotechnol 11: 9.
    • (2011) BMC Biotechnol , vol.11 , pp. 9
    • Reiss, R.1    Ihssen, J.2    Töny-Meyer, L.3
  • 113
    • 77649336425 scopus 로고    scopus 로고
    • Carrier-free immobilized enzymes for biocatalysis
    • Roessl U, Nahálka J, Nidetzky B. 2010. Carrier-free immobilized enzymes for biocatalysis. Biotechnol Lett 32: 341-350.
    • (2010) Biotechnol Lett , vol.32 , pp. 341-350
    • Roessl, U.1    Nahálka, J.2    Nidetzky, B.3
  • 114
    • 20444473057 scopus 로고    scopus 로고
    • Biosensor for the determination of phenols based on Cross-Linked Enzyme Crystals (CLEC) of laccase
    • DOI 10.1016/j.bios.2004.08.024, PII S0956566304003902
    • Roy JJ, Abraham TE, Abhijith KS, Kumar PV, Takur MS. 2005. Biosensor for the determination of phenols based on cross-linked enzyme crystals (CLEC) of laccase. Biosens Bioelectron 21: 206-211. (Pubitemid 40828294)
    • (2005) Biosensors and Bioelectronics , vol.21 , Issue.1 , pp. 206-211
    • Roy, J.J.1    Abraham, T.E.2    Abhijith, K.S.3    Kumar, P.V.S.4    Thakur, M.S.5
  • 115
    • 0026134321 scopus 로고
    • Direct dechlorination of chlorophenolic compounds by laccases from Trametes (Coriolus) versicolor
    • Roy-Arcand L, Archibald FS. 1991. Direct dechlorination of chlorophenolic compounds by laccases from Trametes (Coriolus) versicolor. Enzyme and Microbial Technology 13:194-203.
    • (1991) Enzyme and Microbial Technology , vol.13 , pp. 194-203
    • Roy-Arcand, L.1    Archibald, F.S.2
  • 116
    • 50049088751 scopus 로고    scopus 로고
    • Preparation and characterization of cross-linked enzyme aggregates (CLEA) of subtilisin for controlled release applications
    • Sangeetha K, Abraham TE. 2008. Preparation and characterization of cross-linked enzyme aggregates (CLEA) of subtilisin for controlled release applications. Int J Biol Macromol 43: 314-319.
    • (2008) Int J Biol Macromol , vol.43 , pp. 314-319
    • Sangeetha, K.1    Abraham, T.E.2
  • 117
    • 12944265071 scopus 로고    scopus 로고
    • Chronic toxicity of glutaraldehyde: Differential sensitivity of three freshwater organisms
    • DOI 10.1016/j.aquatox.2004.12.001, PII S0166445X04003340
    • Sano LL, Krueger AM, Landrum PF. 2005. Chronic toxicity of glutaraldehyde: diferential sensitivity of three freshwater organisms. Aquat Toxicol 71: 283-296. (Pubitemid 40173921)
    • (2005) Aquatic Toxicology , vol.71 , Issue.3 , pp. 283-296
    • Sano, L.L.1    Krueger, A.M.2    Landrum, P.F.3
  • 118
    • 79953750390 scopus 로고    scopus 로고
    • Micropollutant sorption to membrane polymers: A review of mechanisms for estrogens
    • Schäfer AI, Akanyeti I, Semião AJ. 2011. Micropollutant sorption to membrane polymers: a review of mechanisms for estrogens. Adv Colloid Interface Sci 164: 100-117.
    • (2011) Adv Colloid Interface Sci , vol.164 , pp. 100-117
    • Schäfer, A.I.1    Akanyeti, I.2    Semião, A.J.3
  • 119
    • 0037193160 scopus 로고    scopus 로고
    • Combined catalytic conversion involving an enzyme, a homogeneous and a heterogeneous catalyst: One-pot preparation of 4-deoxy-D-glucose derivatives from D-galactose
    • DOI 10.1016/S0040-4039(02)00479-3, PII S0040403902004793
    • Schoevaart R, Kieboom T. 2002a. Combined catalytic conversion involving an enzyme, a homogeneous and a heterogeneous catalyst: One-pot preparation of 4-deoxy-D-glucose derivatives from D-galactose. Tetrahedron Lett 43:3399-3400. (Pubitemid 34327570)
    • (2002) Tetrahedron Letters , vol.43 , Issue.18 , pp. 3399-3400
    • Schoevaart, R.1    Kieboom, T.2
  • 120
    • 0037071165 scopus 로고    scopus 로고
    • Galactose dialdehyde as potential protein cross-linker: Proof of principle
    • DOI 10.1016/S0008-6215(02)00051-4, PII S0008621502000514
    • Schoevaart R, Kieboom T. 2002b. Galactose dialdehyde as potential protein cross-linker: proof of principle. Carbohydr Res 337: 899-904. (Pubitemid 34455003)
    • (2002) Carbohydrate Research , vol.337 , Issue.10 , pp. 899-904
    • Schoevaart, R.1    Kieboom, T.2
  • 121
    • 0035800709 scopus 로고    scopus 로고
    • Galactose dialdehyde: The forgotten candidate for a protein cross-linker?
    • DOI 10.1016/S0008-6215(01)00166-5, PII S0008621501001665
    • Schoevaart R, Kieboom T. 2001. Galactose dialdehyde: the forgotten candidate for a protein cross-linker? Carbohydr Res 334: 1-6. (Pubitemid 32695362)
    • (2001) Carbohydrate Research , vol.334 , Issue.1 , pp. 1-6
    • Schoevaart, R.1    Kieboom, T.2
  • 126
    • 79251469073 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates as industrial biocatalysts
    • Sheldon RA. 2011. Cross-linked enzyme aggregates as industrial biocatalysts. Org Process Res Develop 15:213-223.
    • (2011) Org Process Res Develop , vol.15 , pp. 213-223
    • Sheldon, R.A.1
  • 127
    • 34547209337 scopus 로고    scopus 로고
    • Enzyme immobilization: The quest for optimum performance
    • Sheldon RA. 2007. Enzyme immobilization: The quest for optimum performance. Adv Syn Catal 349:1289-1307.
    • (2007) Adv Syn Catal , vol.349 , pp. 1289-1307
    • Sheldon, R.A.1
  • 129
    • 77956443206 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates in a membrane slurry reactor continuous production of 6-APA by enzymatic hydrolysis of penicillin
    • Sorgedrager MJ, Verdoes D, van der Meer H, Sheldon RA. 2008. Cross-linked enzyme aggregates in a membrane slurry reactor continuous production of 6-APA by enzymatic hydrolysis of penicillin. Chimica Oggi/Chemistry Today 24:23-25.
    • (2008) Chimica Oggi/Chemistry Today , vol.24 , pp. 23-25
    • Sorgedrager, M.J.1    Verdoes, D.2    Van Der Meer, H.3    Sheldon, R.A.4
  • 130
    • 0028829657 scopus 로고
    • Demonstration of Laccase in the White Rot Basidiomycete Phanerochaete chrysosporium BKM-F1767
    • Srinivasan C, Dsouza TM, Boominathan K, Reddy CA. 1995. Demonstration of Laccase in the White Rot Basidiomycete Phanerochaete chrysosporium BKM-F1767. Appl Environ Microbiol 61: 4274-4277.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 4274-4277
    • Srinivasan, C.1    Dsouza, T.M.2    Boominathan, K.3    Reddy, C.A.4
  • 131
    • 79551652403 scopus 로고    scopus 로고
    • Laccase: A review of its past and its future in bioremediation
    • Strong PJ, Claus H. 2011. Laccase: A review of its past and its future in bioremediation. Crit Rev Environ Sci Technol 41:373-434.
    • (2011) Crit Rev Environ Sci Technol , vol.41 , pp. 373-434
    • Strong, P.J.1    Claus, H.2
  • 132
    • 79955425303 scopus 로고    scopus 로고
    • Combined cross-linked enzyme aggregates from versatile peroxidase and glucose oxidase: Production, partial characterization and application for the elimination of endocrine disruptors
    • Taboada-Puig R, Junghanns C, Demarche P, Moreira MT, Feijoo G, Lema JM, Agathos SN. 2011. Combined cross-linked enzyme aggregates from versatile peroxidase and glucose oxidase: production, partial characterization and application for the elimination of endocrine disruptors. Bioresour Technol 102: 6593-6599.
    • (2011) Bioresour Technol , vol.102 , pp. 6593-6599
    • Taboada-Puig, R.1    Junghanns, C.2    Demarche, P.3    Moreira, M.T.4    Feijoo, G.5    Lema, J.M.6    Agathos, S.N.7
  • 133
    • 33646458829 scopus 로고    scopus 로고
    • Efects of glutaraldehyde exposure on human health
    • Takigawa T, Endo Y. 2006. Efects of glutaraldehyde exposure on human health. J Occup Health 48: 75-87.
    • (2006) J Occup Health , vol.48 , pp. 75-87
    • Takigawa, T.1    Endo, Y.2
  • 134
    • 0035168976 scopus 로고    scopus 로고
    • Treatment of model soils contaminated with phenolic endocrine-disrupting chemicals with laccase from Trametes sp. in a rotating reactor
    • DOI 10.1016/S1389-1723(01)80232-2
    • Tanaka T, Tonosaki T, Nose M, Tomidokoro N, Kadomura N, Fujii T, Taniguchi M. 2001. Treatment of model soils contaminated with phenolic endocrine-disrupting chemicals with laccase from Trametes sp. in a rotating reactor. J Biosci Bioeng 92: 312-316. (Pubitemid 33063437)
    • (2001) Journal of Bioscience and Bioengineering , vol.92 , Issue.4 , pp. 312-316
    • Tanaka, T.1    Tonosaki, T.2    Nose, M.3    Tomidokoro, N.4    Kadomura, N.5    Fujii, T.6    Taniguchi, M.7
  • 135
    • 0035498333 scopus 로고    scopus 로고
    • Oxidative mechanisms involved in lignin degradation by white-rot fungi
    • DOI 10.1021/cr000115l
    • ten Have R, Teunissen PJ. 2001. Oxidative mechanisms involved in lignin degradation by white-rot fungi. Chem Rev 101: 3397-3413. (Pubitemid 35373041)
    • (2001) Chemical Reviews , vol.101 , Issue.11 , pp. 3397-3413
    • Ten Have, R.1    Teunissen, P.J.M.2
  • 136
    • 84886785708 scopus 로고    scopus 로고
    • Enzymes: Immobilized enzymes
    • London, UK: Elsevier Science
    • Twyman RM. 2005. Enzymes: Immobilized enzymes. In: Encyclopedia of Analytical Science, 2nd edn. London, UK: Elsevier Science, pp 523-529.
    • (2005) Encyclopedia of Analytical Science 2nd Edn , pp. 523-529
    • Twyman, R.M.1
  • 137
    • 33645968409 scopus 로고    scopus 로고
    • Green oxidations with laccase-mediator systems
    • Wells A, Teria M, Eve T. 2006. Green oxidations with laccase-mediator systems. Biochem Soc Trans 34: 304-308.
    • (2006) Biochem Soc Trans , vol.34 , pp. 304-308
    • Wells, A.1    Teria, M.2    Eve, T.3
  • 138
    • 22944470620 scopus 로고
    • Carbodiimide chemistry: Recent advances
    • Williams A, Ibrahim IT. 1981. Carbodiimide chemistry: Recent advances. Chem Rev 81:589-636.
    • (1981) Chem Rev , vol.81 , pp. 589-636
    • Williams, A.1    Ibrahim, I.T.2
  • 140
    • 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
    • DOI 10.1021/bi952971a
    • 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. (Pubitemid 26189831)
    • (1996) Biochemistry , vol.35 , Issue.23 , pp. 7608-7614
    • Xu, F.1
  • 142
    • 79951987034 scopus 로고    scopus 로고
    • Enhanced carbonation reaction using chitosan-based carbonic anhydrase nanoparticles
    • Yadav R, Satyanarayanan T, Kotwal S, Rayalu S. 2011b. Enhanced carbonation reaction using chitosan-based carbonic anhydrase nanoparticles. Current Sci 100:520-524.
    • (2011) Current Sci , vol.100 , pp. 520-524
    • Yadav, R.1    Satyanarayanan, T.2    Kotwal, S.3    Rayalu, S.4
  • 143
    • 33646094220 scopus 로고    scopus 로고
    • Immobilization and characterization of laccase from Chinese Rhus vernicifera on modifed chitosan
    • Yang WY, Min DY, Wen SX, Jin L, Rong L, Tetsuo M, Bo C. 2006. Immobilization and characterization of laccase from Chinese Rhus vernicifera on modifed chitosan. Process Biochem 41:1378-1382.
    • (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    Bo, C.7
  • 145
    • 34848826800 scopus 로고
    • Chemistry of Lacquer (Urushi) part i
    • Yoshida H. 1883. Chemistry of Lacquer (Urushi) part I. Chemical Society of Tokio 43:472-486.
    • (1883) Chemical Society of Tokio , vol.43 , pp. 472-486
    • Yoshida, H.1
  • 147
    • 62849097765 scopus 로고    scopus 로고
    • Removal of 2, 4-dichlorophenol by chitosan-immobilized laccase from Coriolus versicolor
    • Zhang J, Xu Z, Chen H, Zong Y. 2009. Removal of 2, 4-dichlorophenol by chitosan-immobilized laccase from Coriolus versicolor. Biochem Eng J 45:54-59.
    • (2009) Biochem Eng J , vol.45 , pp. 54-59
    • Zhang, J.1    Xu, Z.2    Chen, H.3    Zong, Y.4
  • 148
    • 51249171014 scopus 로고
    • Purifcation and properties of two laccase isoenzymes produced by Botrytis cinerea
    • Zouari N, Romette J, Tomas D. 1987. Purifcation and properties of two laccase isoenzymes produced by Botrytis cinerea. Appl Biochem Biotechnol 15:213-225.
    • (1987) Appl Biochem Biotechnol , vol.15 , pp. 213-225
    • Zouari, N.1    Romette, J.2    Tomas, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.