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Electronic Journal of Biotechnology
Universidad Católica de Valparaíso
ISSN: 0717-3458
Vol. 13, Num. 6, 2010
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Electronic Journal of Biotechnology, Vol. 13, No. 6, December 15, 2010
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: camaraoht20@yahoo.com.br
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.
Code Number: ej10080
Abstract
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.
Keywords: laccase, lignin peroxidase, manganese peroxidase, white-rot
fungi.
Introduction
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.
General features (classification, distribution,
structure and mode of action)
Laccases
(benzenediol: oxygen oxidoreductase EC 1.10.3.2) 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 1.11.1.14) 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 1.11.1.13) 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
1.11.1.16) 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).
Biological functions of ligninolytic
enzymes
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.
Potential industry and biotechnological applications
of ligninolytic enzymes
Food
Industry
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).
Textile
industry
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).
Bioremediation
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 3a and b). 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 3a and b). 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 3a and b).
Concluding Remarks
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.
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