Industrial and biotechnological applications of ligninolytic enzymes of the basidiomycota: A review
Márcia Jaqueline Mendonça Maciel1 · Ademir Castro e Silva1 · Helena Camarão Telles Ribeiro1*
1Programa de Pós-Graduação em Biotecnologia e Recursos Naturais da Amazônia, Universidade do Estado do Amazonas, Amazonas, Brasil
*Corresponding author: firstname.lastname@example.org
Financial support: Fundação de Amparo à Pesquisa do Estado do Amazonas (FAPEAM), Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) e Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES), Universidade do Estado do Amazonas (UEA) Amazonas - Brasil.
Keywords: laccase, lignin peroxidase, manganese peroxidase, white-rot fungi.
Ligninolytic enzymes of the basidiomycetes play a crucial role in the global carbon cycle. The demand for application of ligninolytic enzymes complexes of white-rot fungi in industry and biotechnology is ever increasing due to their use in a variety of processes. Ligninolytic enzymes have potential applications in a large number of fields, including the chemical, fuel, food, agricultural, paper, textile, cosmetic industrial sectors and more. This ligninolytic system of white-rot fungi is also directly involved in the degradation of various xenobiotic compounds and dyes. Their capacities to remove xenobiotic substances and produce polymeric products make them a useful tool for bioremediation purposes. This paper reviews the applications of ligninolytic enzymes of basidiomycetes within different industrial and biotechnological area.
Basidiomycetes species are considered to be a very interesting group of fungi given their exceptional adjustment abilities to accommodate detrimental conditions of the environment where they continue to act as natural lignocellulose destroyers and include very different ecological groups such as white rot, brown rot, and leaf litter fungi (Cho et al. 2009). Lignin is the most abundant natural aromatic polymer on earth and degradation of this recalcitrant aromatic polymer is caused in nature by white rot fungi through a process that was defined as an enzymatic combustion (Kirk and Farrell, 1987). The ligninolytic system is an extracellular enzymatic complex that includes peroxidases, laccases and oxidases responsible for the production of extracellular hydrogen peroxide (H2O2) (Ruiz-Dueñas and Martinez, 2009). Those enzyme systems exhibit differential characteristics depending on the species, strains and culture conditions (Kirk and Farrell, 1987). The fungi absorb nutrients available in the ambient when the molecules are small, and when they are bigger the fungi uses their enzymes (Esposito and de Azevedo, 2004). The enzymes responsible for lignin degradation are mainly: lignin peroxidase (LiP), manganese peroxidase (MnP) and a copper containing phenoloxidase, known as laccase (Table 1). The potential application of ligninolytic enzymes in biotechnology has stimuled their investigation (Vikineswary et al. 2006) and the understanding of physiological mechanisms regulating enzyme synthesis in lignocellulose bioconversion could be useful for improving the technological process of edible and medicinal mushroom production (Songulashvili et al. 2007). Ligninolytic enzymes have a potential in several industrial and biotechnological processes (Figure 1) within a wide variety of organic and inorganic specific substrates (Esposito and de Azevedo, 2004; Rodríguez and Toca, 2006). Consequently, the aim of this review is to highlight the potential industrial and biotechnological applications of ligninolytic enzymes.
Laccases (benzenediol: oxygen oxidoreductase EC 220.127.116.11) belong to multicopper oxidase family (Hoegger et al. 2006; Alcalde, 2007). These copper-containing enzymes catalyze the oxidation of various substrates with the simultaneous reduction of molecular oxygen to water (Yaropolov et al. 1994). Yoshida first discovered laccases in 1883 after observing that latex from the Japanese lacquer tree (Rhus vernicifera) hardened in the presence of air (Call and Mücke, 1997; Gianfreda et al. 1999). Since then, laccase activity has been found in other plants, some insects, and few bacteria (Kramer et al. 2001; Claus, 2003; Claus, 2004; Dittmer et al. 2004). However, most laccases were reported from fungal organisms and most biotechnologically useful laccases are also of fungi origin (Kalmiş et al. 2008). Probably the first report on the presence of laccase in fungi was from Laborde in 1897 (Mayer and Harel, 1979). Over 60 fungal strains belonging to the phyla Ascomycota, Zygomycota and especially Basidiomycota show laccase activities (Kiiskinen et al. 2004; Baldrian, 2006). The catalytic site of laccase is quite conserved among different species of fungi, but the rest of the enzyme structure shows high diversity (Gochev and Krastanov, 2007). Fungal laccases are mostly inducible, extracellular, monomeric glycoproteins with carbohydrate contents of 10-20% which may contribute to the high stability of laccases (Mayer and Staples, 2002). The amino acid chain contains about 520-550 aminoacids including a N-terminal secretion peptide (Gianfreda et al. 1999). Laccases are multinuclear enzymes (Gayazov and Rodakiewicz-Nowak, 1996; Heinzkill et al. 1998; Bertrand et al. 2002; Piontek et al. 2002). The active site of laccase comprises four copper atoms in three groups, referred to as T1, T2 and T3 (Yaropolov et al. 1994; Solomon et al. 1996). Copper atoms differ from each other in their paramagnetic resonance (EPR) signals (Gianfreda et al. 1999). The T1 copper is responsible for the blue colour of the enzyme and has a characteristic absorbance around 610 nm. The T2 copper is colourless and cannot be detected spectrophotometrically, but EPR detectable (Solomon et al. 1996; Leontievsky et al. 1997; Koroljova-Skorobogat’ko et al. 1998). The bi-nuclear T3 copper is diamagnetic. It displays a spectral absorbance shoulder in the region of 330 nm and also displays a characteristic fluorescence spectrum (Shin and Lee, 2000). The yellow laccase had no blue maxima in the absorption spectrum. The yellow laccase was suggested to be formed as a result of blue laccase modification by products of lignin degradation, which might play a role as natural electron-transfer mediators for the oxidation of non-phenolic substances (Higuchi, 2004). Almost all fungi that have been examined produce more than one isoform of laccase (Hoshida et al. 2001). Laccases are usually the first ligninolytic enzymes secreted to the surrounding media by the fungus that normally oxidizes only those lignin model compounds with a free phenolic group, forming phenoxy radicals as the mediators that are a group of low molecular-weight organic compounds. Many artificial mediators have been studied, being ABTS [2.2-azino-bis-(3-ethylbenzothiazoline-6-sulphonic acid)] the first described laccase mediator (Bourbonnais and Paice, 1990; Call and Mücke, 1997). There are natural compounds acting as mediator in laccase oxidation such p-hydroxycinnamic acids (Gianfreda et al. 1999; Moreira Neto, 2006; Gochev and Krastanov, 2007; Camarero et al. 2008).
Lignin peroxidases (EC 18.104.22.168) belong to the family of oxidoreductases (Higuchi, 2004; Martínez et al. 2005; Hammel and Cullen, 2008). Lignin peroxidases (LiPs) were first described in the basidiomycete Phanerochaete chrysosporium Burdsall (order Corticiales) in 1983 (Glenn et al. 1983; Tien and Kirk, 1988). This enzyme has been recorded for several species of white-rot basidiomycetes (Buswell et al. 1987; Kirk and Farrell, 1987; Pointing et al. 2005) and in actinomycetes (Périé and Gold, 1991; Périé et al. 1996; Niladevi and Prema, 2005). LiP is an extracellular hemeprotein, dependent of H2O2, with an unusually high redox potential and low optimum pH (Gold and Alic, 1993; Haglund, 1999; Piontek et al. 2001; Erden et al. 2009). LiP is capable of oxidizing a variety of reducing substrates including polymeric substrates (Oyadomari et al. 2003). Due to their high redox potentials and their enlarged substrate range LiPs have great potential for application in various industrial processes (Erden et al. 2009). LiP shows little substrate specificity, reacting with a wide variety of lignin model compounds and even unrelated molecules (Barr and Aust, 1994). It has the distinction of being able to oxidise methoxylated aromatic rings without a free phenolic group, generating cation radicals that can react further by a variety of pathways, including ring opening, demethylation, and phenol dimerisation (Haglund, 1999). LiP in contrast with laccases does not require mediators to degrade high redox-potencial compounds but it needs hydrogen peroxide to initiate the catalysis.
Manganese peroxidases (EC 22.214.171.124) belong to the family of oxidoreductases (Higuchi, 2004; Martínez et al. 2005; Hammel and Cullen, 2008). Following the discovery of LiP in Phanerochaete chrysosporium, Manganese peroxidase (MnP) secreted from the same fungus was found as another lignin degrading enzyme (Glenn and Gold, 1985; Paszczyński et al. 1985), and subsequent investigations have shown that MnP is distributed in almost all white-rot fungi (Hofrichter, 2002). Manganese peroxidases (MnP) seem to be more widespread among white rot fungi than lignin peroxidase (Hammel and Cullen, 2008). Manganese peroxidase (MnP) oxides Mn2+ to Mn3+, which oxides phenolic structures to phenoxyl radicals (Hofrichter, 2002). The product Mn3+ is highly reactive and complex with chelating organic acid, as oxalate or malate, which are produced by the fungus (Kishi et al. 1994; Galkin et al. 1998; Mäkëla et al. 2002). The redox potential of the Mn peroxidase system is lower than that of lignin peroxidase and it has shown capacity for preferable oxidize in vitro phenolic substrates. On the other hand, studies indicate that contrary to LiP, MnP may oxidize Mn(II) without H2O2 with decomposition of acids, and concomitant production of peroxyl radicals that may affect lignin structure (Hofrichter et al. 1999). Due to their Mn-oxidizing activity, the Pleurotus Versatile peroxidase (VP) enzymes were first described as MnP enzymes, but they were later recognized as representing a new peroxidase type. VP is also able to efficiently oxidize phenolic compounds and dyes that are the substrates of generic peroxidases and related peroxidases, or the well-known horse-radish peroxidase (HRP). Versatile Peroxidase (EC 126.96.36.199) oxidizes Mn2+, as MnP does, and also high redox potential aromatic compounds, as LiP does. The interest on VP has increased during the last years, both as a model enzyme and as a source of industrial/environmental biocatalysts (Martínez et al. 2005; Martínez et al. 2009; Ruiz-Dueñas et al. 2009).
The enzymes are used for the degradation of many compounds, and it’s used for biological functions too, having many functions in the fungi organism, as shown in Table 2.
Laccases can be applied to certain processes that enhance or modify the colour appearance of food or beverage for the elimination of undesirable phenolics, responsible for the browning, haze formation and turbidity in clear fruit juice, beer and wine (Rodríguez and Toca, 2006). Laccase is also employed to ascorbic acid determination, sugar beet pectin gelation, baking and in the treatment of olive mill wastewater (Ghindilis, 2000; Minussi et al. 2002; Rodríguez and Toca, 2006; Selinheimo et al. 2006; Minussi et al. 2007). And lignin peroxidase (LiP) and manganese peroxidase (MnP) have potential to produce natural aromatic flavours (Lesage-Meessen et al. 1996; Lomascolo et al. 1999; Zorn et al. 2003; Barbosa et al. 2008).
Pulp and paper industry
Laccases are able to depolymerize lignin and delignify wood pulps, kraft pulp fibers and chlorine-free in the biopolpation process (Bourbonnais et al. 1997; Lund and Ragauskas, 2001; Chandra and Ragauskas, 2002; Camarero et al. 2004; Rodríguez and Toca, 2006; Vikineswary et al. 2006). One of the most studied applications in the industry is the laccases-mediator bleaching of kraft pulp and the efficiency of which has been proven in mill-scale trials (Strebotnik and Hammel, 2000). This ability could be used in the future to attach chemically versatile compounds in the fiber surfaces and let recycled pulp for new use (Rodríguez and Toca, 2006; Mocchiutti et al. 2005; Saparrat et al. 2008; Widsten and Kandelbauer, 2008). Lignin peroxidases (LiP) compared with laccase, are the biocatalysts of choice for bleaching (Bajpai, 2004; Sigoillot et al. 2005). LiP and MnP were reported to be effective in decolourizing kraft pulp mill effluents (Ferrer et al. 1991; Michel et al. 1991; Moreira et al. 2003). In laboratory scale the consumption of refining energy in mechanical pulping was reduced with MnP pretreatment with a slight improvement in pulp properties (Kurek et al. 2001; Wasenberg et al. 2003; Maijala et al. 2007).
Laccases-mediator system finds potential application in enzymatic modification of dye bleaching in the textile and dyes industries (Abadulla et al. 2000; Kunamneni et al. 2008). Most currently existing processes to treat dye wastewater are ineffective and not economical (Mc Kay, 1979; Cooper, 1993; Riu et al. 1998; Rodríguez and Toca, 2006). Therefore, the development of processes based on laccases seems an atractive solution due their potential in degrading dyes of diverse chemical structure (Abadulla et al. 2000; Blanquez et al. 2004; Hou et al. 2004; Rodríguez and Toca, 2006) including synthetic dyes currently employed in the industry (Wong and Yu, 1999; Rodríguez et al. 2005; Rodríguez and Toca, 2006; Kunamneni et al. 2008). Lignin peroxidases (LiP) were evaluated by decolorizing different synthetic dyes too (Cripps et al. 1990; Pointing, 2001; Robles-Hernández et al. 2008; Gomes et al. 2009). And MnP can biodegrade dyes, as well as decolorize various types of synthetic dyes in aqueous cultures and packed-bed bioreactors (Kasinath et al. 2003; Shin, 2004; Champagne and Ramsay, 2005).
Laccases are involved in green biodegradation due its catalytic properties. The xenobiotic compound is a major source of contamination in soil and laccase degrade it (Rodríguez and Toca, 2006). Moreover, polycyclic aromatic hydrocarbons (PAHs), which arise from natural oil deposits and utilisation of fossil fuels, are also degraded by laccases (Pointing, 2001; Anastasi et al. 2009). Many PAHs have been found in exhibit cytotoxic, mutagenic and carcinogenic properties that represents serious risk to human health (Bamforth and Singleton, 2005). Lignin peroxidases (LiP) present a non specific biocatalyst mechanism. MnP showed that mineralization of many environmental contaminants are used for bioremediation process. Due to their ability to degrade azo, heterocyclic, reactive and polymeric dyes, it degrades 1.1.1-trichloro-2.2-bis-(4-chlorophenyl) ethane (DDT), 2.4.6-trinitrotoluene (TNT) and polycyclic aromatic hydrocarbons (PAH’s) too (Köller et al. 2000; Abraham et al. 2002; Ohtsubo et al. 2004; Robles-Hernández et al. 2008; Gomes et al. 2009; Wen et al. 2009). LiP from P. chrysosporium was one of the first enzymes of basidiomycete capable for PAH degradation (Bumpus and Aust, 1987).
Organic, medical, pharmaceutical, cosmetic and nanotechnology applications
Recently, increasing interest has been focused on the application of laccase as a new biocatalyst in organic synthesis (Milstein et al. 1989; Mayer and Staples, 2002) (Table 3). Enzymatic polymerization using laccase has drawn considerable attention since laccase or laccase-mediator system (LMS) are capable of generating straightforwardly polymers that are impossible to produce through conventional chemical synthesis (Akta and Tanyolac, 2003). Laccases have been employed for several applications in organic synthesis as the oxidation of functional groups, the coupling of phenols and steroids, medical agents (anesthetics, anti-inflammatory, antibiotics and sedatives), the construction of carbon-nitrogen bonds and in synthesis of complex natural products and industries of cosmetics (Baminger et al. 2001; Fabbrini et al. 2001; D’Acunzo et al. 2002; Mikolasch et al. 2002; Baiocco et al. 2003; Barilli et al. 2004; Nicotra et al. 2004; Xu, 2005; Rodríguez and Toca, 2006; Ponzoni et al. 2007; Mikolasch and Schauer, 2009).
A new enzymatic method based on laccase was developed to distinguish simultaneously morphine and codeine in drug samples injected into a flow detection system (Bauer et al. 1999). Laccases also can be applied as biosensors or bioreporters (Bauer et al. 1999; Xu, 1999; Durán and Esposito, 2000; Ghindilis, 2000; D’Souza, 2001; Kuznetsov et al. 2001; Kunamneni et al. 2008; Szamocki, et al. 2009). Laccases still could be immobilized on the cathode of biofuel cells that could provide for small transmitter systems (Ghindilis, 2000) and laccase-based miniature biological fuel cell is of particular interest for many medical applications calling for a power source implanted in a human body (Rodríguez and Toca, 2006; Heller, 2004).
Lignin peroxidase (LiP) exhibit highest bioelectro-catalytic activity at atomic resolution and this makes available for commercial development of biosensors for polymeric phenol or lignin (Christenson et al. 2004) (Table 3). In the future LiP may be of great interest in synthetic chemistry, where they have been proposed to be applicable for production of cosmetic and dermatological preparations for skin (Belinky et al. 2005).
Manganese peroxidase (MnP) produced by the basidiomycete Bjerkandera adusta was used for acrylamide polymerization (Iwahara et al. 2000). MnP from Phanerochaete chrysosporium can degrade styrene that is an important industrial polymer used as a raw material for wrapping and transporting goods, it has polluted water, air and soil (Soto et al. 1991; Lee et al. 2006). MnP is also a redox enzyme with efficient direct electron transfer (DET) properties with electrodes. It is enabled to use for many applications such the development of biosensors based on DET, effective biofuel cells, and selective bioorganic synthesis (Ferapontova et al. 2005) (Table 3).
Ligninolytic enzymes are involved in the degradation of the complex and recalcitrant polymer lignin. This group of enzymes is highly versatile in nature and they find application in a wide variety of industries. The biotechnological significance of these enzymes has led to a drastic increase in the demand for these enzymes in the recent time. Ligninolytic enzymes are promising to replace the conventional chemical processes of several industries. Thus, there is a broad field of investigation that is almost entirely open to new findings and it is quite reasonable to propose that many new applications will be found in the near future.
ABADULLA, E.; TZANOV, T.; COSTA, S.; ROBRA, K.-H.; CAVACO-PAULO, A. and GÜBITZ, G.M. (2000). Decolorization and detoxification of textile dyes with a laccase from Trametes hirsuta. Applied and Environmental Microbiology, vol. 66, no. 8, p. 3357-3362. [CrossRef]
ABRAHAM, W.-R.; NOGALES, B.; GOLYSHIN, P.N.; PIEPER, D.H. and TIMMIS, K.N. (2002). Polychlorinated-biphenol-degrading microbial communities in soils and sediments. Current Opinion in Microbiology, vol. 5, no. 3, p. 246-253. [CrossRef]
AKTA, N. and TANYOLAÇ, A. (2003). Reaction conditions for laccase catalyzed polymerization of catechol. Bioresource Technology, vol. 87, no. 3, p. 209-214. [CrossRef]
ALCALDE, M. (2007). Laccase: biological functions, molecular structure and industrial applications. In: POLAINA, J. and MACCABE, A.P. eds. Industrial enzymes: structure, function and applications. Netherlands-Springer, vol. 26, p. 461-476. [CrossRef]
ANASTASI, A.; COPPOLA, T.; PRIGIONE, V. and VARESE, G. (2009). Pyrene degradation and detoxification in soil by a consortium of basidiomycetes isolated from compost: Role of laccases and peroxidases. Journal of Hazardous Materials, vol. 165, no. 1-3, p. 1229-1233. [CrossRef]
BAIOCCO, P.; BARRECA, A.M.; FABBRINI, M.; GALLI, C. and GENTILI, P. (2003). Promoting laccase activity towards non-phenolic substrates: A mechanistic investigation with some laccase-mediator systems. Organic & Biomolecular Chemistry, vol. 1, no. 1, p. 191-197. [CrossRef]
BAJPAI, P. (2004). Biological bleaching of chemical pulps. Critical Reviews in Biotechnology, vol. 24, no. 1, p. 1-58. [CrossRef]
BALDRIAN, P. (2006). Fungal laccases-occurrence and properties. FEMS Microbiology Reviews, vol. 30, no. 2, p. 215-242. [CrossRef]
BAMFORTH, S.M. and SINGLETON, I. (2005). Bioremediation of polycyclic aromatic hydrocarbons: current knowledge and future directions. Journal of Chemical Technology and Biotechnology, vol. 80, no. 7, p. 726-736. [CrossRef]
BAMINGER, U.; LUDWIG, R.; GALHAUP, C.; LEITNER, C.; KULBE, K.D. and HALTRICH, D. (2001). Continous enzymatic regeneration of redox mediators sed in biotransformation reactions employing flavoproteins. Journal of Molecular Catalysis B: Enzymatic, vol. 11, no. 4-6, p. 541-550. [CrossRef]
BARBOSA, E.S.; PERRONE, D.; VENDRAMINI, A.L.A. and LEITE, S.G.F. (2008). Vanillin production by Phanerochaete chrysosporium grown on green coconut agro-industrial husk in solid state fermentation. BioResources, vol. 3, no. 4, p. 1042-1050.
BARILLI, A.; BELINGHIERI, F.; PASSARELLA, D.; LESMA, G.; RIVA, S.; SILVANI, A. and DANIELI, B. (2004). Enzyme assisted enantioselective synthesis of the alkaloid (+)-aloperine. Tetrahedrom: Asymmetry, vol. 15, no. 18, p. 2921-2925. [CrossRef]
BARR, D.P. and AUST, S.D. (1994). Mechanisms white rot fungi use to degrade pollutants. Environmental Science & Technology, vol. 28, no. 2, p. 78A-87A. [CrossRef]
BAUER, C.G.; KÜHN, A.; GAJOVIC, N.; SKOROBOGATKO, O.; HOLT, P.-J.; BRUCE, N.C.; MAKOWER, A.; LOWE, C.R. and SCHELLER, F.W. (1999). New enzyme sensors for morphine and codeine based on morphine dehydrogenase and laccase. Fresenius’ Journal of Analytical Chemistry, vol. 364, no. 1-2, p. 179-183. [CrossRef]
BELINKY, P.; LASSER, H. and DOSORETZ, C. (2005). Methods of producing lignin peroxidase and its use in skin and hair lightening. Patent IPC Class: AA61K896F1 (Rakuto Bio Technologies Ltda.). Origin: Arlington; VA US, USPC Class: 42462.
BERTRAND, T.; JOLIVALT, C.; BRIOZZO, P.; CAMINADE, E.; JOLY, N.; MADZAK, C. and MOUGIN, C. (2002). Crystal structure of four-copper laccase complexed with an arylamide: insights into substrate recognition and correlation with kinetics. Biochemistry, vol. 41, no. 23, p. 7325-7333. [CrossRef]
BLÁNQUEZ, P.C.; CASAS, N.; FONT, X.; GABARRELL, X.; SARRÁ, M.; CAMINAL, G. and VICENT, T. (2004). Mechanism of textile metal dye biotransformation by Trametes versicolor. Water Research, vol. 38, no. 8, p. 2166-2172. [CrossRef]
BOURBONNAIS, R. and PAICE, M.G. (1990). Oxidation of non-phenolic substrates: An expanded role of laccase in lignin biodegradation. FEBS Letters, vol. 267, no. 1, p. 99-102. [CrossRef]
BOURBONNAIS, R.; PAICE, M.G.; FREIERMUTH, B.; BODIE, E. and BORNEMAN, S. (1997). Reactivities of various mediators and laccase with kraft pulp and lignin model compounds. Applied and Environmental Microbiology, vol. 63, no. 12, p. 4627-4632.
BUMPUS, J.A. and AUST, S.D. (1987). Biodegradation of DDT [1,1,1-trichloro-2,2-bis (4-chlorophenyl) ethane] by the white-rot fungus Phanerochaete chrysosporium. Applied and Environmental Microbiology, vol. 53, no. 9, p. 2001-2008.
BUSWELL, J.A.; ODIER, E. and KIRK, K. (1987). Lignin biodegradation. Critical Reviews in Biotechnology, vol. 6, no. 1, p. 1-60. [CrossRef]
CALL, H.P. and MÜCKE, I. (1997). History, overview and applications of mediated lignolytic systems, especially laccase-mediator-systems (Lignozym®-process). Journal of Biotechnology, vol. 53, no. 2-3, p. 163-202. [CrossRef]
CAMARERO, S.; GARCÍA, O.; VIDAL, T.; COLOM, J.; DEL RIO, J.C.; GUTIÉRREZ, A.; GRAS, J.M.; MONJE, R.; MARTÍNEZ, M.J. and MARTINEZ, A.T. (2004). Efficient bleaching of non-wood high-quality paper pulp using laccase-mediator system. Enzyme and Microbial Technology, vol. 35, no. 2-3, p. 113-120. [CrossRef]
CAMARERO, S.; CAÑAS, A.I.; NOUSIAINEN, P.; RECORD, E.; LOMASCOLO, A.; MARTÍNEZ, M.J. and MARTINEZ, A.T. (2008). p-Hydroxycinnamic acids as natural mediators for laccase oxidation of recalcitrant compounds. Environmental Science & Technology, vol. 42, no. 17, p. 6703-6709. [CrossRef]
CARVALHO, W.; CANILHA, L.; FERRAZ, A. and MILAGRES, A. (2009). Uma visão sobre a estrutura, composição e biodegradação da madeira. Química Nova, vol. 32, no. 8, p. 1-5. [CrossRef]
CHAMPAGNE, P.-P. and RAMSAY, J.A. (2005). Contribution of manganese peroxidase and laccase to dye decoloration by Trametes versicolor. Applied Microbiology and Biotechnology, vol. 69, no. 3, p. 276-285. [CrossRef]
CHANDRA, R.P. and RAGAUSKAS, A.J. (2002). Evaluating laccase-facilitated coupling of phenolic acids to high-yeld kraft pulps. Enzyme and Microbial Technology, vol. 30, no. 7, p. 855-861. [CrossRef]
CHO, N.-S.; WILKOLAZKA, A.J.; STASZCZAK, M.; CHO, H.-Y. and OHGA, S. (2009). The role of laccase from white rot fungi to stress conditions. Journal of the Faculty of Agriculture, Kyushu University, vol. 54, no. 1, p. 81-83.
CHRISTENSON, A.; DIMCHEVA, N.; FERAPONTOVA, E.E.; GORTON, L.; RUZGAS, T.; STOICA, L.; SHLEEV, S.; YAROPOLOV, A.I.; HALTRICH, D.; THORNELEY, R.N.F. and AUST, S.D. (2004). Direct electron transfer between ligninolytic redox enzymes and electrodes. Electroanalysis, vol. 16, no. 13-14, p. 1074-1092. [CrossRef]
CLAUS, H. (2003). Laccases and their occurrence in prokaryotes. Archives of Microbiology, vol. 179, no. 3, p. 145-150. [CrossRef]
CLAUS, H. (2004). Laccases: structure, reactions, distribution. Micron, vol. 35, no. 1-2, p. 93-96. [CrossRef]
COOPER, P. (1993). Removing colour from dye house wastewaters-a critical review of technology available. Journal of the Society of Dyers and Colourists, vol. 109, no. 3, p. 97-101. [CrossRef]
D’ACUNZO, F.; GALLI, C. and MASCI, B. (2002). Oxidation of phenols by laccase and laccase-mediator systems: Solubility and steric issues. European Journal of Biochemistry, vol. 269, no. 21, p. 5330-5335. [CrossRef]
D’SOUZA, S.F. (2001). Microbial biosensors. Biosensors and Bioelectronics, vol. 16, no. 6, p. 337-353. [CrossRef]
DITTMER, N.T.; SUDERMAN, R.J.; JIANG, H.; ZHU, Y.-C.; GORMAN, M.J.; KRAMER, K.J. and KANOST, M.R. (2004). Characterization of cDNAs encoding putative laccase-like multicopper oxidases and developmental expression in the tobacco hornworm, Manduca sexta, and the malaria mosquito, Anopheles gambiae. Insect Biochemistry and Molecular Biology, vol. 34, no. 1, p. 29-41. [CrossRef]
DURÁN, N. and ESPOSITO, E. (2000). Potential applications of oxidative enzymes and phenoloxidases-like compounds in wastewater and soil treatment: a Review. Applied Catalysis B: Environmental, vol. 28, no. 2, p. 83-99. [CrossRef]
ERDEN, E.; UCAR, C.M.; GEZER, T. and PAZARLIOGLU, N.K. (2009). Screening for ligninolytic enzymes from autochthonous fungi and applications for decolorization of Remazole Marine Blue. Brazilian Journal of Microbiology, vol. 40, no. 2, p. 346-353. [CrossRef]
FABBRINI, M.; GALLI, C.; GENTILI, P. and MACCHITELLA, D. (2001). An oxidation of alcohols by oxigen with the enzyme laccase, and mediation by TEMPO. Tetrahedron Letters, vol. 42, no. 43, p. 7551-7553. [CrossRef]
FERAPONTOVA, E.E.; SHLEEV, S.; RUZGAS, T.; STOICA, L.; CHRISTENSON, A.; TKAC, J.; YAROPOLOV, A.I. and GORTON, L. (2005). Direct electrochemistry of proteins and enzymes. Perspectives in Bioanalysis, vol. 1, p. 517-598. [CrossRef]
FERRER, I.; DEZOTTI, M. and DURÁN, N. (1991). Decolorization of Kraft effluent by free and immobilized lignin peroxidases and horseradish peroxidase. Biotechnology Letters, vol. 13, no. 8, p. 577-582. [CrossRef]
GALKIN, S.; VARES, T.; KALSI, M. and HATAKKA, A. (1998). Production of organic acids by different white-rot fungi as detected using capillary zone electrophoresis. Biotechnology Techniques, vol. 12, no. 4, p. 267-271. [CrossRef]
GAYAZOV, R. and RODAKIEWICZ-NOWAK, J. (1996). Semi-continuous production of laccase by Phlebia radiata in different culture media. Folia Microbiologica, vol. 41, no. 6, p. 480-484. [CrossRef]
GIANFREDA, L.; XU, F. and BOLLAG, J.-M. (1999). Laccases: A useful group of oxidoreductive enzymes. Bioremediation Journal, vol. 3, no. 1, p. 1-26. [CrossRef]
GLENN, J.K. and GOLD, M.H. (1985). Purification and characterization of an extracellular Mn(II)-dependent peroxidase from the lignin degrading basidiomycetes, Phanerochaete chrysosporium. Archives of Biochemistry and Biophysics, vol. 242, no. 2, p. 329-341. [CrossRef]
GLENN, J.K.; MORGAN, M.A.; MAYFIELD, M.B.; KUWAHARA, M. and GOLD, M.H. (1983). An extracellular H2O2-requiring enzyme preparation involved in lignin biodegradation by the white rot basidiomycete Phanerochaete chrysosporium. Biochemical and Biophysical Research Communications, vol. 114, no. 3, p. 1077-1083. [CrossRef]
GOMES, E.; AGUIAR, A.P.; CARVALHO, C.C.; BONFÁ, M.R.B.; DA SILVA, R. and BOSCOLO, M. (2009). Ligninases production by Basidiomycetes strains on lignocellulosic agricultural residues and their application in the decolorization of synthetic dyes. Brazilian Journal of Microbiology, vol. 40, no. 1, p. 31-39. [CrossRef]
HAMMEL, K.E. and CULLEN, D. (2008). Role of fungal peroxidases in biological ligninolysis. Current Opinion in Plant Biology, vol. 11, no. 3, p. 349-355. [CrossRef]
HEINZKILL, M.; BECH, L.; HALKIER, T.; SCHNEIDER, P. and ANKE, T. (1998). Characterization of laccases and peroxidases from wood-rotting fungi (Family Coprinaceae). Applied and Environmental Microbiology, vol. 64, no. 5, p. 1601-1606.
HELLER, A. (2004). Miniature biofuel cells. Physical Chemistry Chemical Physics, vol. 6, no. 2, p. 209-216. [CrossRef]
HENRIKSSON, G.; JOHANSSON, G. and PETTERSSON, G. (2000a). A critical review of cellobiose dehydrogenases. Journal of Biotechnology, vol. 78, no. 2, p. 93-113. [CrossRef]
HENRIKSSON, G.; ZHANG, L.; LI, J.; LJUNGQUIST, P.; REITBERGER, T.; PETTERSSON, G. and JOHANSSON, G. (2000b). Is cellobiose dehydrogenase from Phanerochaete chrysosporium a lignin degrading enzyme? Biochimica et Biophysica Acta (BBA)- Protein Structure and Molecular Enzymology, vol. 1480, no. 1-2, p. 83-91. [CrossRef]
HIGUCHI, T. (2004). Microbial degradation of lignin: role of lignin peroxidase, manganese peroxidase, and laccase. Proceedings of the Japan Academy, Series B, vol. 80, no. 5, p. 204-214. [CrossRef]
HOEGGER, P.J.; KILARU, S.; JAMES, T.Y.; THACKER, J.R. and KÜES, U. (2006). Phylogenetic comparison and classification of laccase and related multicopper oxidase protein sequences. The FEBS Journal, vol. 273, no. 10, p. 2308-2326. [CrossRef]
HOFRICHTER, M. (2002). Review: lignin conversion by manganese peroxidase (MnP). Enzyme and Microbial Technology, vol. 30, no. 4, p. 454-466. [CrossRef]
HOFRICHTER, M.; SCHEIBNER, K.; BUBLITZ, F.; SCHNEEGAß, I.; ZIEGENHAGEN, D.; MARTENS, R. and FRITSCHE, W. (1999). Depolymerization of straw lignin by manganese peroxidase from Nematoloma frowardii is accompanied by release of carbon dioxide. Holzforschung, vol. 53, no. 2, p. 161-166. [CrossRef]
HOSHIDA, H.; NAKAO, M.; KANAZAWA, H.; KUBO, K.; HAKUKAWA, T.; MORIMASA, K.; AKADA, R. and NISHIZAWA, Y. (2001). Isolation of five laccase gene sequences from the white-rot fungus Trametes sanguinea by PCR, and cloning, characterization and expression of the laccase cDNA in yeasts. Journal of Bioscience and Bioengineering, vol. 92, no. 4, p. 372-380. [CrossRef]
HOU, H.; ZHOU, J.; WANG, J.; DU, C. and YAN, B. (2004). Enhancement of laccase production by Pleurotus ostreatus and its use for the decolorization of anthraquinone dye. Process Biochemistry, vol. 39, no. 11, p. 1415-1419. [CrossRef]
IWAHARA, K.; HIRATA, M.; HONDA, Y.; WATANABE, T. and KUWAHARA, M. (2000). Free-radical polymerization of acrylamide by manganese peroxidase produced by the white-rot basidiomycetes Bjerkandra adusta. Biotechnology Letters, vol. 22, no. 17, p. 1355-1361. [CrossRef]
KALMIS, E.; YASA, I.; KALYONCU, F.; PAZARBASI, B. and KOÇYIGIT, A. (2008). Ligninolytic enzyme activities in mycellium of some wild and commercial mushrooms. African Journal of Biotechnology, vol. 7, no. 23, p. 4314-4320.
KASINATH, A.; NOVOTNY, C.; SVOBODOVA, K.; PATEL, K.C. and SASECK, V. (2003). Decolorization of synthetic dyes by Irpex lacteus in liquid cultures and packed-bed bioreactor. Enzyme and Microbial Technology, vol. 32, no. 1, p. 167-173. [CrossRef]
KERSTEN, P. and CULLEN, D. (2007). Extracellular oxidative systems of the lignin-degrading Basidiomycete Phanerochaete chrysosporium. Fungal Genetics and Biology, vol. 44, no. 2, p. 77-87. [CrossRef]
KIISKINEN, L.-L.; RÄTTÖ, M. and KRUUS, K. (2004). Screening for novel laccase-producing microbes. Journal of Applied Microbiology, vol. 97, no. 3, p. 640-646. [CrossRef]
KIRK, T.K. and FARRELL, R.L. (1987). Enzymatic “combustion”: The microbial degradation of lignin. Annual Review of Microbiology, vol. 41, no. 1, p. 465-501. [CrossRef]
KISHI, K.; WARIISHI, H.; MARQUEZ, L.; DUNFORD, B.H. and GOLD, M.H. (1994). Mechanisms of manganese peroxidases compound II reduction. Effect of organic acid chelators and pH. Biochemistry, vol. 33, no. 29, p. 8694-8701. [CrossRef]
KÖLLER, G.; MÖEDER, M. and CZIHAL, K. (2000). Peroxidative degradation of selected PCB: A mechanistic study. Chemosphere, vol. 41, no. 12, p. 1827-1834. [CrossRef]
KOROLJOVA-SKOROBOGAT’KO, O.V.; STEPANOVA, E.V.; GAVRILOVA, V.P.; MOROZOVA, O.V.; LUBIMOVA, N.V.; DZCHAFAROVA, A.N.; JAROPOLOV, A.I. and MAKOWER, A. (1998). Purification and characterization of the constitutive form of laccase from the basidiomycete Coriolus hirsutus and effect of inducers on laccase synthesis. Biotechnology and Applied Biochemistry, vol. 28, part 1, p. 47-54.
KRAMER, K.J.; KANOST, M.R.; HOPKINS, T.L.; JIANG, H.; ZHU, Y.-C.; XU, R.; KERWIN, J.L. and TURECEK, F. (2001). Oxidative conjugation of catechols with proteins in insect skeletal systems. Tetrahedron, vol. 57, no. 2, p. 385-392. [CrossRef]
KUNAMNENI, A.; GHAZI, I.; CAMARERO, S.; BALLESTEROS, A.; PLOU, F.J. and ALCALDE, M. (2008). Decolorization of synthetic dyes by laccase immobilized on epoxy-activated carriers. Process Biochemistry, vol. 43, no. 2, p. 169-178. [CrossRef]
KUREK, B.; PETIT-CONIL, M.; SIGOILLOT, J.C.; HERPOEL, I.; RUEL, K.; MOUKHA, S.; JOSELEAU, J.P.; PENNINCKS, M.; ASTHER, M.; GAZZA, G. and DE CHOUDENS, C. (2001). Treatment of high-yield pulp with fungal peroxidases: from laboratory to pilot scale study. In: ARGYROPOULOS, D., ed. ACS symposium series 785, Oxidative delignification chemistry, fundamental and catalysis American Chemical Society, Washington DC, chapter 30, vol. 785, p. 474-486.
KUZNETSOV, B.A.; SHUMAKOVICH, G.P.; KOROLEVA. O.V. and YAROPOLOV, A.I. (2001). On applicability of laccase as label in the mediated and mediatorless electroimmunoassay: Effect of distance on the direct electron transfer between laccase and electrode. Biosensors and Bioelectronics, vol. 16, no. 1-2, p. 73-84. [CrossRef]
LEE, J.-W.; LEE, S.-M.; HONG, E.-J.; JEUNG, E.-B.; KANG, H.-Y.; KIM, M.-K. and CHOI, I.-G. (2006). Estrogenic reduction of styrene monomer degraded by Phanerochaete chrysosporium KFRI 20742. The Journal of Microbiology, vol. 44, no. 2, p. 177-184.
LEONTIEVSKY, A.A.; VARES, T.; LANKINEN, P.; SHERGILL, J.K.; POZDNYAKOVA, N.N.; MYASOEDOVA, N.M.; KALKKINEN, N.; GOLOVLEVA, L.A.; CAMMACK, R.; THURSTON, C.F. and HATAKKA, A. (1997). Blue and yellow laccases of ligninolytic fungi. FEMS Microbiology Letters, vol. 156, no. 1, p. 9-14. [CrossRef]
LESAGE-MEESSEN, L.; DELATTRE, M.; HAON, M.; THIBAULT, J.-F.; CECCALDI, B.C.; BRUNERIE, P. and ASTHER, M. (1996). A two-step bioconversion process for vanillin production from ferulic acid combining Aspergillus niger and Pycnoporus cinnabarinus. Journal of Biotechnology, vol. 50, no. 2-3, p. 107-113. [CrossRef]
LOMASCOLO, A.; STENTELAIRE, C.; ASTHER, M. and LESAGE-MEESSEN, L. (1999). Basidiomycetes as new biotechnological tools to generate natural aromatic flavours for the food industry. Trends in Biotechnology, vol. 17, no. 7, p. 282-289. [CrossRef]
LUND, M. and RAGAUSKAS, A.J. (2001). Enzymatic modification of kraft lignin through oxidative coupling with water-soluble phenols. Applied Microbiology and Biotechnology, vol. 55, no. 6, p. 699-703. [CrossRef]
MAIJALA, P.; METTÃLÃ, A.; KLEEN, M.; WESTIN, C.; POPPIUS-LEVIN, K.; HERRANEN, K.; LEHTO, J.H.; REPONEN, P.; MÃENTAUSTA, O. and HATAKKA, A. (2007). Treatment of softwood chips with enzymes may reduce refining energy consumption and increase surface charge of fibers. In: 10th International Congress on Biotechnology in the Pulp and Paper Industry. Madison Wisconsin, Book of Abstracts. p. 65.
MÄKELÄ, M.; GALKIN, S.; HATAKKA, A. and LUNDELL, T. (2002). Production of organic acids and oxalate decarboxylase inlignin-degrading white rot fungi. Enzyme and Microbial Technology, vol. 30, no. 4, p. 542-549. [CrossRef]
MARTÍNEZ, A.T.; SPERANZA, M.; RUIZ-DUEÑAS, F.J.; FERREIRA, P.; CAMARERO, S.; GUILLÉN, F.; MARTÍNEZ, M.J.; GUTIÉRREZ, A. and DEL RIO, J.C. (2005). Biodegradation of lignocellulosics: microbial, chemical and enzymatic aspects of fungal attack to lignin. International Microbiology, vol. 8, no. 3, p. 195-204.
MARTÍNEZ, A.T.; RUIZ-DUEÑAS, F.J.; MARTÍNEZ, M.J.; RIO, J.C. and GUTIÉRREZ, A. (2009). Enzymatic delignification of plant cell wall: from nature to mill. Current Opinion in Biotechnology, vol. 20, no. 3, p. 348-357. [CrossRef]
MAYER, A.M. and HAREL, E. (1979). Polyphenol oxidases in plants. Phytochemistry, vol. 18, no. 2, p. 193-215. [CrossRef]
MAYER, A.M. and STAPLES, R.C. (2002). Laccase: New functions for an old enzyme. Phytochemistry, vol. 60, no. 6, p. 551-565. [CrossRef]
MC MICHEL, F.C.Jr.; DASS, B.S.; GRULKE, E.A. and REDDY, A.C., G. (1991). Role of manganese peroxidases and lignin peroxidase of Phanerochaete chrysosporium in decolorization of kraft bleach plant effluent. Applied and Environmental Microbiology, vol. 57, no. 8, p. 2368-2375.
MIKOLASCH, A.; HAMMER, E.; JONAS, U.; POPOWSKI, K.; STIELOW, A. and SCHAUER, F. (2002). Synthesis of 3-(3,4-dihydroxyphenyl)-propionic acid derivatives by N-coupling of amines using laccase. Tetrahedrom, vol. 58, no. 38, p. 7589-7593. [CrossRef]
MIKOLASCH, A. and SCHAUER, F. (2009). Fungal laccases as tools for the synthesis of new hybrid molecules and biomaterials. Applied Microbiology and Biotechnology, vol. 82, no. 4, p. 605-624. [CrossRef]
MILSTEIN, O.; NICKLAS, B. and HÜTTERMANN, A. (1989). Oxidation of aromatic compounds in organic solvents with laccase from Trametes versicolor. Applied Microbiology and Biotechnology, vol. 31, no. 1, p. 70-74. [CrossRef]
MINUSSI, R.C.; PASTORE, G.M. and DURÁN, N. (2002). Potential applications of laccase in the food industry. Trends in Food Science and Technology, vol. 13, no. 6-7, p. 205-216. [CrossRef]
MINUSSI, R.C.; MIRANDA, M.A.; SILVA, J.A.; FERREIRA, C.V.; AOYAMA, H.; MARANGONI, S.; ROTILIO, D.; PASTORE, G.M. and DURÁN, N. (2007). Purification, characterization and application of laccase from Trametes versicolor for colour and phenolic removal of olive mill wastewater in the presence of 1-hidroxybenzotriazole. African Journal of Biotechnology, vol. 6, no. 10, p. 1248-1254.
MOREIRA NETO, S.L. (2006). Enzimas ligninoliticas produzidas por Psilocybe castanella CCB444 em solo contaminado com hexaclorobenzeno. São Paulo, Instituto de Botânica da Secretaria do Estado do Meio Ambiente. 110 p.
MOREIRA, M.T.; FEIJOO, G.; CANAVAL, J. and LEMA, J.M. (2003). Semipilot-scale bleaching of Kraft pulp with manganese peroxide. Wood Science and Technology, vol. 37, no. 2, p. 117-123. [CrossRef]
NICOTRA, S.; CRAMAROSSA, M.R.; MUCCI, A.; PAGNONI, U.M.; RIVA, S. and FORTI, L. (2004). Biotransformation of resveratrol: synthesis of trans-dehydrodimers catalyzed by laccases from Myceliophtora thermophyla and from Trametes pubescens. Tetrahedron, vol. 60, no. 3, p. 595-600. [CrossRef]
OHTSUBO, Y.; KUDO, T.; TSUDA, M. and NAGATA, Y. (2004). Strategies for bioremediation of polychlorinated biphenyls. Applied Microbiology and Biotechnology, vol. 65, no. 3, p. 250-258. [CrossRef]
OYADOMARI, M.; SHINOHARA, H.; JOHJIMA, T.; WARIISHI, H. and TANAKA, H. (2003). Electrochemical characterization of lignin peroxidase from the white-rot basidiomycete Phanerochaete chrysosporium. Journal of Molecular Catalysis B: Enzymatic, vol. 21, no. 4-6, p. 291-297. [CrossRef]
PASZCZYNSKI, A.; HUYNH, V.-B. and CRAWFORD, R. (1985). Enzymatic activities of an extracellular, manganese-dependent peroxidase from Phanerochaete chrysosporium. FEMS Microbiology Letters, vol. 29, no. 1-2, p. 37-41. [CrossRef]
PÉRIÉ, F.H. and GOLD, M.H. (1991). Manganese regulation of manganese peroxidase expression and lignin degradation by the white rot fungus Dichomitus squalens. Applied and Environmental Microbiology, vol. 57, no. 8, p. 2240-2245.
PÉRIÉ, F.H.; SHENG, D. and GOLD, M.H. (1996). Purification and characterization of two manganese peroxidase isozymes from the white-rot basidiomycete Dichomitus squalens. Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology, vol. 1297, no. 2, p. 139-148. [CrossRef]
PIONTEK, K.; SMITH, A.T. and BLODIG, W. (2001). Lignin peroxidase structure and function. Biochemical Society Transactions, vol. 29, no. 2, p. 111-116. [CrossRef]
PIONTEK, K.; ANTORINI, M. and CHOINOWSKI, T. (2002). Crystal structure of a laccase from the fungus Trametes versicolor at 1.90 Å resolution containing a full complement of coppers. The Journal of Biological Chemistry, vol. 277, no. 40, p. 37663-37669. [CrossRef]
POINTING, S.B. (2001). Feasibility of bioremediation by white-rot fungi. Applied Microbiology and Biotechnology, vol. 57, no. 1-2, p. 20-33. [CrossRef]
POINTING, S.B.; PELLING, A.L.; SMITH, G.J.D.; HYDE, K.D. and REDDY, A. (2005). Screening of basidiomycetes and xylariaceous fungi for lignin peroxidase and laccase gene-specific sequences. Mycological Research, vol. 109, no. 1, p. 115-124. [CrossRef]
PONZONI, C.; BENEVENTI, E.; CRAMAROSSA, M.R.; RAIMONDI, S.; TREVISI, G.; PAGNONI, U.M.; RIVA, S. and FORTI, L. (2007). Laccase-catalyzed dimerization of hydroxystilbenes. Advanced Synthesis & Catalysis, vol. 349, no. 8-9, p. 1497-1506. [CrossRef]
RIU, J.; SCHÖNSEE, I. and BARCELÓ, D. (1998). Determination of sulfonated azo dyes in groundwater and industrial effluents by automated solid-phase extraction followed by capillary electrophoresis-mass spectrometry. Journal of Mass Spectrometry, vol. 33, no. 7, p. 653-663. [CrossRef]
ROBLES-HERNÁNDEZ, L.; GONZALES-FRANCO, A.C.; CRAWFORD, D.L. and CHUN, W.W.C. (2008). Review of environmental organopollutants degradation by white-rot basidiomycete mushrooms. Tecnociencia Chihuahua, vol. 2, no. 1, p. 32-39.
RODRÍGUEZ, S.; SANROMÁN, M. and GÜBITZ, G.M. (2005). Influence of redox mediators and metal ions on synthetic acid dye decolourization by crude laccase from Trametes hirsuta. Chemosphere, vol. 58, no. 4, p. 417-422. [CrossRef]
RODRÍGUEZ, S. and TOCA, J.L. (2006). Industrial and biotechnological applications of laccases: a review. Biotechnology Advances, vol. 24, no. 5, p. 500-513. [CrossRef]
RUIZ-DUEÑAS, F.J. and MARTÍNEZ, A.T. (2009). Microbial degradation of lignin: how a bulky recalcitrant polymer is efficiently recycled in nature and how we can take advantage of this. Microbial Biotechnology, vol. 2, no. 2, p. 164-177. [CrossRef]
RUIZ-DUEÑAS, F.J.; MORALES, M.; GARCÍA, E.; MIKI, Y.; MARTÍNEZ, M.J. and MARTÍNEZ, A.T. (2009). Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases. Journal of Experimental Botany, vol. 60, no. 2, p. 441-452. [CrossRef]
SAPARRAT, M.C.N.; MOCCHIUTTI, P.; LIGGIERI, C.S.; AULICINO, M.B.; CAFFINI, N.O.; BALATTI, P.A. and MARTÍNEZ, M.J. (2008). Ligninolytic enzyme ability and potential biotechnology applications of the white-rot fungus Grammothele subargentea LPSC no. 436 strain. Process Biochemistry, vol. 43, no. 4 p. 368-375. [CrossRef]
SCORE, A.J.; PALFREYMAN, J.W. and WHITE, N.A. (1997). Extracellular phenoloxidase and peroxidase enzyme production during interspecific fungal interactions. International Biodeterioration & Biodegradation, vol. 39, no. 2-3, p. 225-233. [CrossRef]
SELINHEIMO, E.; KRUUS, K.; BUCHERT, J.; HOPIA, A. and AUTIO, K. (2006). Effects of laccase, xylanase and their combination on the rheological properties of wheat doughs. Journal of Cereal Science, vol. 43, no. 2, p. 152-159. [CrossRef]
SHIN, K.-S. and LEE, Y.-J. (2000). Purification and characterization of a new member of the laccase family from the white-rot basidiomycete Coriolus hirsutus. Archives of Biochemistry and Biophysics, vol. 384, no. 1, p. 109-115. [CrossRef]
SIGOILLOT, C.; CAMARERO, S.; VIDAL, T.; RECORD, E.; ASTHER, M.; PÉREZ-BOADA, M.; MARTÍNEZ, M.J.; SIGOILLOT, J.-C.; ASTHER, M.; COLOM, J.F. and MARTÍNEZ, Á.T. (2005). Comparison of different fungal enzymes for bleaching high-quality paper pulps. Journal of Biotechnology, vol. 115, no. 4, p. 333-343. [CrossRef]
SOARES, C.H.L. (1998). Estudos mecaníticos da degradação de efluentes de indústrias de papel e celulose por fungos basidiomicetos degradadores de madeira. Universidade Estadual de Campinas. Instituto de Química, Campinas, São Paulo, 122 p.
SOLOMON, E.I.; SUNDARAM, U.M. and MACHONKIN, T.E. (1996). Multicopper oxidases and oxygenases. Chemical Reviews, vol. 96, no. 7, p. 2563-2606. [CrossRef]
SONGULASHVILI, G.; ELISASHVILI, V.; WASSER, S.P.; NEVO, E. and HADAR, Y. (2007). Basidiomycetes laccase and manganese peroxidase activity in submerged fermentation of food industry wastes. Enzyme and Microbial Technology, vol. 41, no. 1-2, p. 57-61. [CrossRef]
SOTO, A.M.; JUSTICIA, H.; WRAY, J.W. and SONNENS CHEIN, C. (1991). p-nonyl-phenol: an estrogenic xenobiotic released from “modified” polystyrene. Environmental Health Perspectives, vol. 92, no. 1, p. 167-173.
STAHL, P.; KISSAU, L.; MAZITSCHEK, R.; GIANNIS, A. and WALDMANN, H. (2002). Natural product derived receptor tyrosin kinase inhibitors: Identification of IGFIR, Tie-2 and VEGFR3 inhibitors. Angewandte Chemie (International Edition), vol. 41, no. 7, p. 1174-1178. [CrossRef]
STREBOTNIK, E. and HAMMEL, K.E. (2000). Degradation of nonphenolic lignin by the laccase/1-hidroxybenzotriazole system. Journal of Biotechnology, vol. 81, no. 2-3, p. 179-188. [CrossRef]
SZAMOCKI, R.E.; FLEXER, V.; LEVIN, L.; FORCHIASIN, F. and CALVO, E.J. (2009). Oxygen cathode based on a layer-by-layer self-assembled laccase and osmium redox mediator. Electrochimica Acta, vol. 54, no. 7, p. 1970-1977. [CrossRef]
TREJO-HERNANDEZ, M.R.; LOPEZ-MUNGUIA, A. and QUINTERO RAMIREZ, R. (2001). Residual compost of Agaricus bisporus as a source of crude laccase for enzymic oxidation of phenolic compounds. Process Biochemistry, vol. 36, no. 7, p. 635-639. [CrossRef]
VIKINESWARY, S.; ABDULLAH, N.; RENUVATHANI, M.; SEKARAN, M.; PANDEY, A. and JONES, G.E.B. (2006). Productivity of laccase in solid substrate fermentation of selected agro-residues by Pycnoporus sanguineus. Bioresource Technology, vol. 97, no. 1, p. 171-177. [CrossRef]
WASENBERG, D.; KRYRIAKIDES, I. and AGATHOS, S.N. (2003). White-rot fungi and their enzymes for the treatment of industrial dye effluents. Biotechnology Advances, vol. 22, no. 1-2, p. 161-187. [CrossRef]
WEN, X.; JIA, Y. and LI, J. (2009). Degradation of tetracycline and oxytetracycline by crude lignin peroxidase prepared from Phanerochaete chrysosporium-a white rot fungus. Chemosphere, vol. 75, no. 8, p. 1003-1007. [CrossRef]
WIDSTEN, P. and KANDELBAUER, A. (2008). Laccase applications in the forest products industry: a review. Enzyme and Microbial Technology, vol. 42, no. 4, p. 293-307. [CrossRef]
WONG, Y. and YU, J. (1999). Laccase-catalysed decolorization of synthetic dyes. Water Research, vol. 33, no. 16, p. 3512-3520. [CrossRef]
WYATT, A.M. and BRODA, P. (1995). Informed strain improvement for lignin degradation by Phanerochaete chrysosporium. Microbiology, vol. 141, p. 2811-2822. [CrossRef]
XU, F. (2005). Applications of oxiredoreductases: Recent progress. Industrial Biotechnology, vol. 1, no. 1, p. 38-50. [CrossRef]
YAROPOLOV, A.I.; SKOROBOGAT’KO, O.V.; VARTANOV, S.S. and VARFOLOMEYEV, S.D. (1994). Laccase: properties, catalytic mechanism, and applicability. Applied Biochemistry and Biotechnology, vol. 49, no. 3, p. 257-280. [CrossRef]
ZORN, H.; LANGHOFF, S.; SCHEIBNER, M.; NIMTZ, M. and BERGER, R.G. (2003). A peroxidase from Lepista irina cleaves β,β-Carotene to flavor compounds. Biological Chemistry, vol. 384, no. 7, 1049-1056. [CrossRef]
Note: Electronic Journal of Biotechnology is not responsible if on-line references cited on manuscripts are not available any more after the date of publication.