You are on page 1of 17

See discussions, stats, and author profiles for this publication at: https://www.researchgate.

net/publication/346626074

LIGNIN DEGRADING ENZYMES AND THEIR INDUSTRIAL APPLICATIONS

Chapter · January 2020

CITATIONS READS
0 244

1 author:

Rachana Choudhary
Shri Shankaracharya Group of Institutions
19 PUBLICATIONS   8 CITATIONS   

SEE PROFILE

Some of the authors of this publication are also working on these related projects:

LIGNOCELLULOLYTIC FUNGAL ISOLATION AND SCREENING FOR THEIR LACCASE PRODUCING ABILITY BHUNESHWARI NAYAKa1, RACHANA CHOUDHARYb AND M.G. ROYMOMc
View project

HEMIDESMUS INDICUS (ANANTMOOL): RARE HERB OF CHHATTISGARH View project

All content following this page was uploaded by Rachana Choudhary on 12 December 2020.

The user has requested enhancement of the downloaded file.


Phenomenon in Environmental and Nano Science, Pages 275-289
Edited by: Kavita Sharma and Ravi Sharma
Copyright O 2021, Jaya Publishing House, Delhi, India
22
LIGNIN DEGRADING ENZYMES AND
THEIR INDUSTRIAL APPLICATIONS
Bhuneshwari Nayak1, Rachana Choudhary 2* and M.G. Roymon2
Department of Microbiology and Biotechnology, St. Thomas College, Ruabandha, Bhilai-490020 (CG)
Department of Microbiology, Shri Shankaracharya Mahavidyalayay, Junwani, Bhilai-490020 (CG)
Email: rachanadin@gmail.com

Abstract
Lignin is one of the most primitive organic polymers for modern applications. This chapter portrays
the concepts of lignin degrading enzymes and their insights. The chapter also portrays the
industrial applications of these enzymes ranging from food industries to biotechnological
applications with detailed sub-application areas. Additionally, the chapter opens the gate for
researching the application of enzymes in more enhanced applications like WFRC (Weather and
Forecasting Research Model).
Keywords: Enzymes, Lignin, Organic Polymers, Biotechnology.

Introduction
Lignin is a complex constituent of the wood. After cellulose, lignin is one of the most
bountiful organic polymers in plants. In wood it is present in 20-40% and in gramineae
present in 15-20%. It is the sole chemical composition of angiosperm and gymnosperm
(Jiang, 2001). Lignin is a complex chemical compound linked with mainly three monomers
coniferyl alcohol, sinapyl alcohol and coumaryl alcohol. On the bases of their monomers
it will be divided in to three types; guaiacyl lignin polymerized by guaiacyl propane,
syringyl lignin polymerized by syringyl propane and hydroxy-phenyl lignin polymerized by
hydroxy-phenyl propane. Usually, gymnosperm contains guaiacyl (G) lignin; monocotyledon
contains guaiacyl-syringyl-hydroxy-phenyl (GSH) lignin and dicotyledon contains guaiacyl-
syringyl (GS) lignin (Wei and Song, 2001).

Structure of lignin
It consists of aromatic rings with the units of guaiacyl propane, para-hydroxy-phenyl-
propane and phenyl-propane units. Lignin is part of secondary cell wall of plants. It is
276 Phenomenon in Environmental and Nano Science

different from cellulose and hemicellulose (Ralph et al., 2004). It has highly resistance to
biological degradation and chemicals (Martinez et al., 2005). Lignin is composed of three
basic units ofp-coumary1 alcohol, coniferyl alcohol and sinapyl alcohol (Liu et al., 2008;
Cai et al., 2010).

Fig. 1. Structure of a lignin molecule (Chhabra, 2013).

Lignin Degrading Enzymes


Lignin is highly resistance for biodegradation. White-rot fungi are known to best lignin
degrader. Lignin is mainly degraded by three types of lignolytic enzymes such as lignin
peroxidase, manganese peroxidase and laccase (Eriksson et al., 1990).

Lignin Peroxidase
Lignin peroxidase is an enzyme, which degrade lignin in the plant cells. It produced from
fungi like Phanerochaete chrysosporium. It interacts with veratryl alcohol (lignin polymer),

Fig. 2. Lignin-peroxidase mediated conversion of veratryl alcohol (VA) to veratraldehyde


(Albayrak and Yang, 2002).
Lignin Degrading Enzymes and their Industrial Applications 277

which is secondary metabolites and acts as cofactor. Lignin peroxidase enzyme catalyzes
the chemical reaction. Use 1,2-bis (3,4-dimethoxypheny1) propane-1,3-diol and H2O2 use
as substrate (Renganathan et al., 1986).

1. Manganese Peroxidase
Manganese peroxidase enzyme belongs to oxidoreductase family. It discovered in 1985
from Phanerochaete chrysosporium (Glenn and Gold, 1985; Paszcynski et al., 1985).
Manganese peroxidase enzyme catalyzes the chemical reaction. Use Mn (II) H+ and
H2O2 as a substrate. It oxidizes the substrate by one-electron oxidation process with
intermediate cation radical formation (Malherbe and Cloete, 2002).
2Mn (II) + 2H+ + H2 2 2Mn (III) + 2H2 2

Fig. 3. Manganese peroxidase mediated conversion of 2,6-dimethoxyphenoI to cerulignone


(Lopez et a/., 2004).
Laccase
Laccase is a copper- containing polyphenol oxidase (blue multi copper oxidase) enzyme. It
was discovered in the effluence of Japanese lacquer tree Rbus vernicifera (Yoshida, 1883).
It is broadly distributed in fungi, higher plants bacteria and insects. Deuteromycetes,
Ascomycetes, Basidiomycetes and many white-rot fungi are contains laccase (Kunamneni,
2008).

Fig. 4. Catalytic breakdown of 2,6-dimethoxyphenoI by laccase (Arora and Sharma, 2010).


278 Phenomenon in Environmental and Nano Science

Fungal laccase is involved in the lignin degradation and during degradation it removes
potentially toxic phenol from the lignin. It requires oxygen for enzymatic action as a
second substrate. It is capable to catalyze the ring cleavage of aromatic compounds. It
used ABTS, 2,6-dimethoxypheno1, dimethyl-p-phenylenediamine and syringaldazine as a
substrate. It moniterate with an oxygen sensor, through the oxidation process reduces
oxygen to water (Claus, 2004).

Versatile Peroxidase
Versatile peroxidase is a novel class enzyme of ligninolytic peroxidases. It shows combine
properties of lignin peroxidase and manganese peroxidase (Ruiz-Duenas et al., 1999;
Camarero et al., 2000; Martinez, 2002). Little data shows versatile peroxidase oxidizes
lignin or lignin-derivatives. Bjerkandera sp. Strain BOSSS is first reported versatile
peroxidase secretes in vitro testing (Moreira et al., 2001).

Fig. S. Oxidation of manganese and aromatic substrates by versatile peroxidase (Ravichandran


and Sridhar, 2016).

Lignin Degrading Microbes


Basidiomycetes group fungi are mainly degrades lignin and its derivatives. In environment
it will be ability to grow in accommodate detrimental conditions and act as environmental
natural lignocelluloses destroyers. Leaf litter, white rot and brown rot fungi are present
in these groups (Cho et al., 2009). Lignin is natural aromatic polymer and recalcitrant
aromatic polymer on the earth. They are mostly degrading by white rot fungi by enzymatic
combustion. Basidiomycete’s families as well as Ascomycetes family fungi also degrade
lignin in nature (Kirk and Farrell, 1987).
Lignin Degrading Enzymes and their Industrial Applications 279

Table 1: Lignin degrading enzyme producing fungi

S. No. Organisms References


1. Fungi
1. Trametes versicolor Dion, 1951
2. Glomerella sp. Mayer and Harel, 1979
3. Podospora anserina Durrens, 1981
4. Aspergillus nidulans Kurtz and Champe, 1982
5. Fomes annosus Haars and Huttermann, 1983
6. Daedalea flavida Arora and Sandhu, 1985
7. Schizophyllum commune De Vries et al., 1986
8. Pleurotus ostreatus Arora and Sandhu, 1987
9. Pleurotus sajor-caju Bourbonnais & Paice, 1988
10. Polyporus pinsitus Huttermann et at., 1989
11. Rigidoporus lignosus Galliano et at., 1991
12. Armillaria ostoyae Robene-Saustrade et at., 1992
13. Ceriporiopsis subvermispora Ruttimann-Johnson et al., 1993
14. Agaricus bisporus Bonnen et al., 1994
15. Ganoderma trabeum Palaez et al., 1995
16. Pycnoporus cinnabarinus Eggert et at., 1996
17. Ganoderma lucidum Perumal, 1997
18. Trametes trogii Garzillo et at., 1998
19. Lentinula edodes D’Annible et al., 1999
20. Marasmius quercophilus Farnet et al., 2000
21. Phellinus ribis Min et al., 2001
22. Trametes modesta Nyanhongo et at., 2002
23. Piloderma byssinum Chen et at., 2003
24. Volvariella volvacea Chen et at., 2004
25. lrpex lacteus Svobodova, 2005
26. Volvariella speciosa Fasola et al., 2007
27. Ganoderma austral Mendonca et al., 2008
28. Lentinus polychrous Suwannawong et at., 2010
29. Pycnoporus sanguineus Kalarani et at., 2011
30. Lentinus squarrosulus Tripathi et at., 2012
II. Bacteria
1. Azospirillum lipoferum Givaudan et al., 1993;
2. Aquifex aeolicus Deckert et al., 1998
3. Escherichia coli Sanchez-Amat et a/., 2001
4. Pyrobaculum aerophilum Fitz-Gibbon et at., 2002
[Table Contd.
280 Phenomenon in Environmental and Nano Science

Contd. Table]

S. No. Organisms References


5. g-proteobacterium Bains et at., 2003
6. Thermos thermophiles Miyazaki, 2005
7. Streptomyces galbus Sharma et al., 2007
III. Insect
1. Bombyx mori Yamazaki, 1972
2. Lucilia cuprina Barrett, 1987
3. Anapheles gambiae Dittmer et at., 2004
4. Nephotettix cincticeps Hattori et al., 2005

Industrial Applications of Lignin Degrading Enzymes


D’Souza et al. (2006) studied that ligninolytic enzyme such as lignin-peroxidase (lip),
Manganase-peroxidase (MnP) and laccase had three major classes of lignin degrading
enzymes, which have great potential for industrial applications.

Food Industries
In the food industries laccase is the known a best wine stabilizer. They easily control to
the haze formation. Haze formation occure in the presence of phenolic compound such
as proanthocyanidins (Osma et al., 2010). Brijwani et al. (2010) reported to presence of
enzyme in dough they improve the dough consistency and also Enhance the gulten structure.
After the addition of laccase in the dough, they showed softness, volume increasing and
crumb changes into the structure.

Paper and Pulp Industries


While using wood for paper making, lignin is the main compound and harsh chemicals
(sulphite, chlorine and oxygen based oxidants) or strong acid used for processing. These
compounds generate water pollution and soil pottution (heavy soil) (Scott et al., 1998).
Laccase is capable to depolymerize and de-lignifing the wood pulp fiber, use in chlorine-
free in bio-palpation process (Camarero et al., 2004; Vikineswary et al., 2006).

Textile Industries
In the textile industry various dyes are secrested with wast water. Generally effluents of
waste water are highly coloured with COD (chemical oxygen demand) and BOD (biological
oxygen demand) (Nagraj and Kumar, 2006). Trametes versicolor (white rot fungi) help
in the decolourazation of dyes (Roseline et al., 2013).
Lignin Degrading Enzymes and their Industrial Applications 281

Laccase enzyme are applicable for denim finishing, it is a new trend. For stone-
washed look of denim fabrics pre-bleach, rinsing and neutralize by sodium hypochloride.
All steps of denim processing are cause substantial environmental pollution. For bleaching
of denim fabrics Trametes versicolor secretes laccase at normal environmental conditions
(Sharma et al., 2005). Some textile dyes degradation showed in the table no. 2.

Bioremediation
Lignolytic enzymes producing microorganisms are capable to degrade lignin. They also
degrade several xenobiotic compounds and recalcitrant pollutants like PHA
(polyhydroxyalkanoates). White rot fungi totally mineralized the lignin compounds. It
generates the research interest in the industries and environmental microbiology fields
(Van and Villaverde, 2005; Ruiz-Duenas and Martinez, 2009; Dashtban et al., 2010).
Bioremediation by ligninolytic enzymes showed in the table no. 2.

Table 2: Ligninolytic enzymes used in the processing of textile dyes and bioremediations

S. Compounds Organisms Ligninolytic References


No. enzymes
1. Textile dyes Phanerochaete Manganese Koyani et al., 2013
chrysosporium peroxidase
2. Azo dyes Pleurotus ostreatus Manganese Arunkumar and
peroxidase Sheik Abdulla, 2014
3. PHAs Pleurotus ostreatus Laccase and Pozdnyakova
versatile peroxidase et al., 2010
4. Bentazon Ganoderma lucidum Manganese De Silva et at., 2009
peroxidase and
laccase
5. Textile effluents Phanerochaete Laccase Miranda et al., 2013
chrysosporium,
Curvularia lunata
6. Poly R-478 lrpex lacteus Manganese Wang et at., 2013
(polymeric peroxidase
model dye)
7. Olive oil waste- Hapalopilus croceus, Manganese Koutrotsios and
water Phanerochaete peroxidase, Zervakis, 2014
chrysosporium, manganese
lrpex lacteus independent
peroxidase and
laccase
8. Endocrine Cerrena unicolor Laccase Songulashvili
disrupters et al., 2012
9. Nonyphenol Pleurotus ostretus Laccase Macellaro et al., 2014
[Table Contd.
282 Phenomenon in Environmental and Nano Science

Contd. Table]

S. Compounds Organisms Ligninolytic References


No. enzymes
10. Naphthalene, Lentinula edodes Laccase Wong et at., 2013
Benzo[a]
anthracene
and anthracene
11. Diclofenac and Aspergillus oryzae laccase Nguyen et at., 2014
bisphenol A
12. Salicylic acid, Trametes versicolor Laccase Nguyen et at., 2014
triclosan, naproxen,
diclofenac,
ibuprofen and
gemfibrozil

Bio-Ethanol Production
Production of fuel ethanol by wood hydrolysates fermentation is very difficult. White-rot
fungi are capable to degrade lignin. White-rot fungi (Trametes versicolor) secrete
peroxidases (lignin peroxidase and manganese peroxidase) and phenol oxidase laccase,
which is transform the aromatic compounds of wood (Lipin et al., 2013). Saccharomyces
cerevisiae is used for ethanolic fermentation. Peroxidases and laccase a phenol oxidase
increase the productivity of ethanol (Olsson, 1996).

Conclusion
Ligninolytic enzymes are involved in recalcitrant polymer lignin and complex lignin polymers
degradation. They are highly versatile group in nature and very wide applicable in various
industries. Ligninolytic enzymes applications in industries and also found in WRFC (Weather
Research and Forecasting Model) have (a) paper whitening, (b) textile industries in
degradation of industrial dye, (c) biotechnological application and (d) xenobiotics compounds
degradation, including herbicides, polycyclic aromatic hydrocarbons, phenolics and other
pesticides. Laccase as an oxidase used in many industrial, agricultural and medicinal
applications (Arora and Sharma, 2010). Fungal enzyme laccase had been used for decades
in enzyme-technology industries (Shukla, 2014).

References
1. Abadulla, E., Tzanov, T., Costa, S., Bobra, K. H., Cavaco-Paulo, A., & Gubitz, G. M.
(2000). Decolorization and detoxification of textile dyes with a laccase from Trametes
hirsute. Applied and Environmental Microbiology, 66, 3357-3362.
Lignin Degrading Enzymes and their Industrial Applications 283

2. Arora, D. S., & Sandhu, D. K. (1985). Survey of some Indian soil for laccase
producing fungi and their lignin degrading ability. Proceedings- Plant Science- Indian
Academy of Sciences, 94, 567-574.
3. Arora, D. S., & Sandhu, D. K. (1987). Decomposition of angiospermic wood sawdust
and laccase production by two Pleurotus species. Journal of Basic Microbiology,
27, 179-184.
4. Arora, D. S., & Sharma, R. K. (2010). Ligninolytic fungal laccases and their
biotechnological applications. Applied Biochemistry and Biotechnology, 160, 1760-
1788.
5. Arunkumar, M., & Sheik Abdulla, S. H. (2014). Hyper-production of manganese
peroxidase by mutant Pleurotus osttreatus MTCC 142 and its applications in
biodegradation of textile azo dyes. Desalination Water Treatment, 1, 1-12.
6. Albayrak, N., & Yang, S. T. (2002). Production of galacto-oligosaccharides from
lactose by Aspergillus oryze beta-galactosidase immobilized on cotton cloth.
Biotechnology and Bioengineering, 77, 8-19.
7. Bains, J., Capalash, N., & Sharma, P. (2003). Laccase from a non melanogenic,
alkalotolerant g-proteobacterium TB isolated from industrial waste water drained
soil. Biotechnology Letters, 25, 1155-1159.
8. Barrett, F. M. (1987). Phenoloxidases from larval cuticle of the sheep blowfly,
Lucilia cuprina: characterization, developmental changes, and inhibition by
antiphenoloxidase antibodies. Archives of Insect Biochemistry and Physiology, 5,
99-118.
9. Bonnen, A. M., Anton, L. H., & Orth, A. B. (1994). Lignin-degrading enzymes of
the commercial button mushroom, Agaricus bisporus. Applied and Environmental
Microbiology, 60, 960-965.
10. Bourbonnais, R., & Paice, M. G. (1988). Veratryl alcohol oxidases from the lignin-
degrading basidiomycete Pleurotus sajor-caju. The Biochemical Journal, 255,
445-450.
11. Brijwani, K., Rigdon, A., & Vadlani, P. V. (2010). Fungal laccase production, function,
and application in food processing. Enzyme Research.
12. Cai, Y., Li, G., Nie, J., Lin, Y., Nie, F., Zhang, J., & Xu, Y. (2010). Study of the
structure and biosynthetic pathway of lignin in stone cells of pear. Scientia
Horticulturae, 125, 374-379.
13. Camarero, S., Ruiz-Duenas, F. J., Sarkar, S., Martinez, M. J., & Martinez, A. T.
(2000). The cloning of a new peroxidase found in lignocelluloses cultures of Pleurotus
eryngii and sequence comparison with other fungal peroxidases. FEMS Microbiology
Letters, 191, 37—43.
14. Camarero, S., Garcia, O., Vidal, T., Colom, J., Del Rio, J. C., Gutierrez, A., Gras J.
M., Monje, R., Martinez, M. J., & Martinez, A. T. (2004). Efficient bleaching of non-
284 Phenomenon in Environmental and Nano Science

wood high-quality paper pulp using laccase-mediator systems. Enzyme and Microbial
Technology, 35, 113-120.
15. Chen, D. M., Bastias, B. A. Taylor, A. F. S., & Cairney, J. W. G. (2003). Identification
of laccase-like genes in ectomycorrhizal basidiomycetes and transcriptional regulation
by nitrogen in Piloderma byssinum. The New Phytologist, 157, 547-554.
16. Chen, S., Ge, W., & Buswell, J. A. (2004). Biochemical and molecular characterization
of a laccase from the edible straw mushroom Volvariella volvacea. European
Journal of Biochemistry, 271, 318-328.
17. Chhabra, N. (2013). Diet and nutrition. Biochemistry for Medicos.
18. Cho, N. S., Wilkolazka, A. J., Staszczak, M., Cho, H. Y., & Ohga, S. (2009). The
role of laccase from white rot fungi to stress conditions. Journal of the Faculty of
Agriculture, 54, 81-83.
19. Claus, H. (2004). Laccases: Structure, reaction, distribution. Micron, 35, 93-96.
20. D’Annibale, A., Stazi, S. R., Vinciguerra, V., & Mattia, E. D. (1999). Characterization
of immobilized laccase from Lentinula edodes and itsuse in olive-mill wastewater
treatment. Process Biochemistry, 34, 697-706.
21. D’souza, D. T., Tiwari, R., Sah, A. K., & Raghukumar, C. (2006). Enhanced production
of laccase by a marine fungus during treatment of colored effluents and synthetic
dyes. Enzyme and Microbial Technology, 38, 504-511.
22. Dashtban, M., Schraft, H., Syed, T., & Qin, W. (2010). Fungal biodegradation and
enzyme modification of lignin. International Journal of Biochemistry and Molecular
Biology, 1, 36-50.
23. De Silva, C. J., De Souza, C. G. M., De Oliveira, A. L., Bracht, A., Costa, M. A.
F., & Peralta, R. M. (2009). Comparative removal of bentazon by Ganoderma
lucidum in liquid and solid state cultures. Current Microbiology, 60, 350-355.
24. De Vries, O. M. H., Kooistra, W. H. C. F., & Wessels, G. M. (1986). Formation of
extracellular laccase by Schizophyllum commune dikaryon. Holzforschung, 46,
135-147.
25. Deckert, G., Patrick, V., Warren, P. V., Gaosterland, T., & Ronald, V. (1998). The
complete genome of the hyperthermophilic bacterium Aquifex aeolicus. Nature,
392, 353-358.
26. Dion, W. M. (1951). Production and properties of a polyphenol oxidase from the
fungus Polyporus versicolor. Canadian Journal of Botany, 30, 9-20.
27. Dittmer, N. T., Suderman, R. J., Jiang, H., Zhu, Y., Gorman, M. J., Kramer, K. J.,
& Kanost, M. R. (2004). Characterization of cDNAs encoding putative laccase-like
multicopper oxidases and developmental expression in the tobacco homworm, Manduca
sexta and the malaria mosquito Anopheles gambiae. Insect Biochemistry and
Molecular Biology, 34, 29-41.
Lignin Degrading Enzymes and their Industrial Applications 285

28. Durrens, P. (1981). The phenoloxidase of the ascomycete Podospora anserine: The
three forms of major laccase activity. Archives of Microbiology, 130, 121-124.
29. Eggert, C., Temp, U., & Eriksson, K. E. L. (1996). The ligninolytic system of the
white rot fungus Pycnoporus cinnabarinus: Purification and characterization of
laccase. Applied and Environmental Microbiology, 62, I I 51-1158.
30. Eriksson, K. E., Blanchette, R. A., & Ander, P. (1990). Microbiol and enzymatic
degradation of wood and wood components. Springer, Berlin Heidelberg, 407.
31. Farnet, A. M., Criquet, S., Tagger, S., Gill, G., & Le Petit, J. (2000). Purification,
partial characterization and reactivity with aromatic compounds of two laccases from
Marasmius quercophilus strain 17. Canadian Journal of Microbiology, 46, 1-6.
32. Fasola, T. R., Gbolagade, J. S., & Fasidi, I. O. (2007). Nutritional requirements of
Volvariella speciose (Fr.Ex.Fr.) Singer, a Nigerian edible mushroom. Food Chemistry,
100, 904-908.
33. Fitz-Gibbon, S. T., Lander, H., Kim, U. J., Stetter, K. O., Simon, M. I., & Miller, J.
H. (2002). Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
aerophilum. Proc Natl Acad Sci USA, 99, 984-989.
34. Galliano, H., Gas, G., & Seris, J. L. (1991). Lignin degradation by Rigidoporus
lignosus involves synergistic action of two oxidizing enzymes: MnP and laccase.
Enzyme and Microbial Technology, 13, 478-482.
35. Garzillo, A. M. V., Colao, M. C., Caruso, C., Caporale, C., Celletti, D., & Buonocore,
V. (1998). Laccase from the white rot fungus Trametes trogii. Applied Microbiology
and Biotechnology, 49, 545-551.
36. Givaudan, A., Effosse, A., Faure, D., Potier, P., Bouillant, M. L., & Bally, R. (1993).
Polyphenol oxidase in Azospirillum lipoferum isolated from rice rhizosphere: Evidance
for laccase activity in non-motile strains of Azospirillum lipoferum. FEMS
Microbiology Letters, 108, 205-210.
37. Glenn, J. K., & Gold, M. H. (1985). Purification and characterization of an extracellular
Mn (II)-dependent peroxidase from the lignin-degrading basidiomycete Phanerochaete
chrysosporium. Archives of Biochemistry and Biophysics, 242, 329-341.
38. Haars, A., & Huttermann, A. (1983). Laccase induction in the white rot fungus
Heterobasidion annosum (Fr.) Bref. (Fomes annosus Fr. Cooke). Archives of
Microbiology, 134, 309-313.
39. Hattori M., Konishi H., Tamura Y., Konno K., & Sogawa K. (2005). Laccasetype
phenoloxidase in salivary glands and watery saliva of the green rice leafhopper,
Nephotettix cincticeps. Journal of Insect Physiology, 51, 1359-1365.
40. Huttermann, R., Milstein, O., Nicklas, B., Trojanowski, J., Haars, A., & Kharazipour,
A. (1989). Enzymatic modification of lignin for technical use. In W. G. Glasser & S.
Sarkanen (Eds.), Lignin-properties and materials. ACS symposium series.
Washington, DC: American Chemical Society, 397, 361-370.
286 Phenomenon in Environmental and Nano Science

41. Jiang, T. D. (2001). Lignin. Beijing: Chemical Industry Press.


42. Kalarani, R., Suffian, M. A., & Alimin, A. K. (2011). Optimization of nutrient levels
for laccase fermentation using statistical techniques. Asia-Pacific Journal of
Molecular Biology and Biotechnology, 19, 73-81.
43. Kirk, T. K., & Farrell, R. L. (1987). Enzymatic “combustion” The microbial degradation
of lignin. Annual Review of Microbiology, 41, 465-501.
44. Koutrotsios, G., & zervakis, G. I. (2014). Comparative examination of the olive mill
wastewater biodegradation process by various wood-rot macrofungi. Biomed Research
International.
45. Koyani, R. D., Sanghvi, G. V., Sharma, R. K., & Rajput, K. S. (2013). Contribution
of lignin degrading enzymes in decolourisation and degradation of reactive textile
dyes. International Biodeterioration & Biodegradation, 77, I -9.
46. Kunamneni, A., Ghazi, I., Camarero, S., Ballesteros, A., Plou, F. J., & Alcalde, M.
(2008). Decoloriozation of synthetic dyes by laccase immobilized on epoxy-activated
carriers. Process Biochemistry, 43, 169-178.
47. Kurtz, M. B., & Champe, S. P. (1982). Purification and characterization of the
conidial laccase of Aspergillus nidulans. Journal of Bacteriology, 151, 1338-1345.
48. Lipin, D., Mundur, S., Mishra, C. S., & Thankamani, V. (2013). Ligninolytic enzymes
for application in treatment of effluent from pulp and paper industries. Journal o/
Environmental Research and Technology, 1, 14-26.
49. Liu, Q., Wang, S., Zheng, Y., Luo, Z., & Cen, K. (2008). Mechanism study of wood
lignin pyrolysis by using TG-FTIR analysis. Journal of Analytical and Applied
Pyrolysis, 82, 170-177.
50. Lopez, C., Moreira, M. T., Feijoo, G., & Lema, J. M. (2004). Dye decolorization by
manganese peroxidase in an enzymatic membrane bioreactor. Biotechnology Progress,
20, 74-81.
51. Macellaro, G., Pezzella, C., Cicatiello, P., Sannia, G., & Piscitelli, A. (2014). Fungal
laccases degradation of endocrine disrupting compounds. Biomed Research
International, 1-8.
52. Malherbe, S., & Cloete, T. E. (2002). Lignocellulose biodegradation: Fundamentals
and applications. Reviews in Environmental Science & Biotechnology, 1, l05- ll4.
53. Martinez, A. T. (2002). Molecular biology and structure-function of lignin degrading
heme peroxidases. Enzyme and Microbial Technology, 30, 425—444.
54. Matrinez, T. A., Francisco, M. S., Duenas, R. J., Ferrerira, P., Camarero, S., Guillen,
F., Matrizen, M. J., Gutrierrez, A., & Rio, J. C. (2005). Biodegradation of lignocellulosics:
microbial chemical and enzymatic aspects of fungal attack of lignin. Research Reviews,
8, 195-204.
55. Mayer, A. M., & Harel, E. (1979). Polyphenol oxidase in plants. Phytochemistry, 18,
193-215.
Lignin Degrading Enzymes and their Industrial Applications 287

56. Mendonca, R. T., Jara, J. F., Gonzalez, V., Elissetche, J. P., & Freer, J. (2008).
Evolution of the white-rot fungi Ganoderma austral and Ceriporiops is
subvermispora in biotechnological applications. Journal of Industrial Microbiology
and Biotechnology, 35, 1323-1330.
57. Min, K. L., Kim, Y. H., Kim, Y. M., Jung, H. S., & Hah, Y. C. (2001). Characterization
of a novel laccase produced by the wood-rotting fungus Phellinus ribis. Archives
of Biochemistry and Biophysics, 392, 279-286.
58. Miranda, Rde. C., Gomes, Ede, B., Pereiro, N. Jr., Marin-Morales, M. A., Machado,
K. M., & Gusmao, N. Bde. (2013). Biotreatment of textile effluent in static bioreactor
by Curvularia lunata VRNI 6179 and Phanerochaete chrysosporium VRNI 6181.
Bioresource Technology, 142, 361-367.
59. Miyazaki, H. (2005). A hyperthermophilic laccase from Thermos thermophilus HB27.
Extremophiles, 9, 415-425.
60. Moreira, M. T., Sierra-Alvarez, R., Lema, J. M., Feijoo, G., & Field, J. A. (2001).
Oxidation of lignin in eucalyptus kraft pulp by manganese peroxidase from Bjerkandera
sp. strain BOSSS. Bioresource Technology, 78, 71—79.
61. Nagraj, C. M., & Kumar, A. (2006). Distillery waste water treatment and disposal.
International Journal of Environmental Science and Technology, 3.
62. Nguyen, L. N., Hai, F. I., Yang, S., Kang, J., Leusch, F. D. L., Roddick, F., Price,
W. E., & Nghiem, L. D. (2014). Removal of pharmaceuticals, steroid hormones,
phytoestrogens, UV-filters, industrial chemical and pesticides by Trametes versicolor
role of biosorption and biodegradation. International Biodeterioration &
Biodegradation, 88, 169-175.
63. Nguyen, L. N., Hai, F. I., Price, W. E., Leusch, F. D. L., Roddick, F., Ngo, H. H.,
Guo, W., Magram, S. F. & Nghiem, L. D. (2014). The effects of mediator and
granular activated carbon addition on degradation of trace organic contaminants by
an enzymatic membrane reactor. Bioresource Technology, 167, 169-177.
64. Nyanhongo, G. S., Gomes, J., Giibitz, G. M., Zvauya, R., Read, J., & Steiner, W.
(2002). Decolorization of textile dyes by laccases from a newly isolated strain of
Trametes modesta. Water Research, 6, 1449-1456.
65. Olsson, L., & Hahn, H. B. (1996). Fermentation of lignocellulosic hydrolysates for
ethanol production. Journal of Enzyme and Microbial Technology, 18, 312-331.
66. Osma, J. F., Toca-Herrera, J. L., & Rodriguez-Couto, S. (2010). Uses of laccases
in the food industry. Enzyme Research.
67. Palaez, F., Martinez, M. J., & Martinez, A. I. (1995). Screening of 68 species of
basidiomycetes involved in lignin degradation. Mycological Research, 99, 37-42.
68. Paszcynski, A., Huynh, V. B., & Crawford, R. (1985). Enzymatic activities of an
extracellular, manganese dependent peroxidase from Phanerochaete chrysosporium.
FEMS Microbiology Letters, 82, 37-41.
288 Phenomenon in Environmental and Nano Science

69. Perumal, K. (1997). Biochemical studies of lignolyticenzymes of Ganoderma lucidum,


a white rot fungus and its application in treatment of paper mill effluent. Ph.D thesis,
University of Madras.
70. Pozdnyakova, N., Nikiforova, S., & Turkovakaya, 0. (2010). Influence of PHAs on
ligninolytic enzymes of the fungus Pleurotus ostreatus D1. Open Life Sciences, 5,
82-94.
71. Ralph, J. K., lundquist, G., Drunow, F. L. H., Kim, P. F., Schataz, J. M., Martia, R.
D., Hatfiled, S. A., Ralph, J. H. C., & Boerjan, W. (2004). Lignin natural polymers
from oxidative coupling of 4-hydroxyphenyl propanoid. Phytochemistry Reviews, 3,
29-60.
72. Ravichandran, A., & Shridhar, M. (2016). Versatile peroxidases: Super peroxidases
with potential biotechnological applications-a mini review. Journal of Veterinary &
Animal Research, 4, 277-280.
73. Renganathan, V., Miki, K., & Gold, M. H. (1986). Role of molecular oxygen in lignin
peroxidase. 246, 155- l6l.
74. Robene-Saustrade, I., Lung-Escarmant, B., Bonno, J. J., & Taris, B. (1992).
Identification and partial characterization of an extracellular manganese-dependent
phenol oxidase in Armillaria ostoyae and Armillaria mellea. European Journal of
Forest Pathology, 22, 227-236.
75. Roseline, Jebapriya, G., & Joel, G. J. (2013). Bioremediation of textile dye using
white-rot fungi: a review. International Journal of Current Research and Review,
5, 1-13.
76. Ruiz-Duenas, F. J., Martinez, M. J., & Martinez, A. T. (1999). Molecular
characterization of a novel peroxidase isolated from the ligninolytic fungus Pleurotus
eryngii. Molecular Microbiology, 31, 223—235.
77. Ruiz-Duenas, F. J., & Martinez, A. T. (2009). Microbial degradation of lignin: how
a bulky recalcitrant polymer is efficiently recycled in nature and how we can take
advantage to this. Microbial Technology, 2, 164-177.
78. Ruttimann-Johnson, C., Salas, L., Vicuna, R., & Kirk, T. K. (1993). Extracellular
enzyme production and synthetic lignin mineralization by Ceriporiopsis subvermispora.
Applied and Environmental Microbiology, 59, I 792-1797.
79. Sanchez-Amat, A., Lucas-Elio, P., Fernandez, E., & Garcia-Borron, J. C. (2001).
Molecular cloning and functional characterization of a unique multipotent polyphenol
oxidase from Marinomonas mediterranea. Biochimica et Biophysica Acta, 1547, 104-
116.
80. Scott, G. M., Akhtar, M., Lentz, M. J., Swaney, R. E (1998). Engineering, scale-up,
and economic aspects of fungal pretreatment of wood chips. In environmentally
friendly technologies for the pulp and paper industry (Eds Young, R. A. and Akhtar,
M.), John Wiley & Sons, Inc. New York, 341-383.
Lignin Degrading Enzymes and their Industrial Applications 289

81. Sharma, H. S. S., Whiteside, L., & Kernaghan, K. (2005). Enzymatic treatment of
flax fibre at the roving stage for production of wet spun yarn. Journal of Enzyme
Microbial Technology, 37, 386-396.
82. Sharma, P., Goe1, R., and Capalash, N. (2007). Bacterial laccase. World Journal of
Microbiology and Biotechnology, 23, 823-832.
83. Shukla, A. K. (2014). Biodiversity in Aspergillus nidulans group on the basis of
Lipases profile. International Journal of Research in Sciences, 3, 1391-1394.
84. Songulashvili, G., Jimenez-Tobon, G. A., Jaspers, C., & Penninckx, M. J. (2012).
Immobilized laccase of Cerrena unicolor for elimination of endocrine disruptor
micropollutants. Fungal Biology, 116, 883-889.
85. Suwannawong, P., Khammuang, S., & Sarnthima, R. (2010). Decolorization of
rhodamine B and congo red by partial purified laccase from Lentinus polychrous
Lev. Journal of Biochemical Technology, 2, 182-186.
86. Svobodova, K. (2005). The implication of ligninolytic enzymes in the decolorization
of synthetic dyes by white-rot fungus Irpex lacteus. PhD Thesis, University, Prague
Czech Republic.
87. Tripathi, A., Upadhyay, R. C., & Singh, S. (2012). Extracellular ligninolytic enzymes
in Be jerkandera adusta and Lentinus squarrosulus. Indian Journal of
Microbiology, 59, 381-387.
88. Van der, Z. F. P., & Villaverde, S. (2005). Combined anaerobic-aerobic treatment of
azo dyes a short review of bioreactor studies. Water Research, 39, 1425-1440.
89. Vikineswary, S., Abdullah, N., Renuvathani, M., Sekaran, M., Pandey, A., & Jones,
G. E. B. (2006). Productivity of laccase in solid substrate fermentation of selected
agro-residues by Pycnoporu ssanguineus. Bioresource Technology, 97, I 71-177.
90. Wang, G., Liu, C., Hong, J., Ma, Y. X., Zhang, K., Huang, X., Zou, S., & Zhang, M.
(2013). Comparision of process configurations for ethanol production from acid- and
alkali-pretreated corncob by Saccharomyces cerevisiae strains with and without b-
glucosidase expression. Journal of Biotechnology, 142, l54-161.
91. Wei, J. H., & Song, Y. R. (2001). Recent advances in study of lignin biosynthesis and
manipulation. Journal of Integrative Plant Biology, 43, 771—779.
92. Wong, K. S., Cheung, M. K., Au, C. H., & Kwan, H. S. (2013). A novel Lentinula
edodes laccase and its enzymology suggest guaiacol-based laccase engineering for
bioremediation. PLoS One, 8, 1-12.
93. Yamazaki, H. I. (1972). Cuticular phenoloxidase from the silkwonn, Bombyx mori:
properties, solubilization, and purification. Insect Biochemistry and Molecular Biology,
2, 431-444.
94. Yoshida, H. (1883). Chemistry of lacquer (Urusbi) part 1. Journal of the Chemical
Society, 43, 472-486.
View publication stats

You might also like