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105. Selinheimo E, Kruus K, Buchert J et al (2006) Effects of laccase, xylanase and their
combination on the rheological properties of wheat doughs. J Cereal Sci 43(2):152–159.
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106. Kurtz MB, Champe SP (1982) Purification and characterization of the conidial laccase of
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108. Chefetz B, Chen Y, Hadar Y (1998) Purification and characterization of laccase from
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109. Kiiskinen L-L, Viikari L, Kruus K (2002) Purification and characterisation of a novel laccase
from the Ascomycete melanocarpus albomyces. Appl Microbiol Biotechnol 59(2–3):198–
204. https://doi.org/10.1007/s00253-002-1012-x
110. Froehner SC, Eriksson K-E (1974) Purification and properties of Neurospora crassa laccase.
J Bacteriol 120(1):458–465
111. Iyer G, Chattoo BB (2003) Purification and characterization of laccase from the rice blast
fungus. Magnaporthe grisea FEMS Microbiol Lett 227(1):121–126. https://doi.org/10.1016/
S0378-1097(03)00658-X
112. de Gonzalo G, Colpa DI, Habib MHM et al (2016) Bacterial enzymes involved in lignin
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113. Narnoliya LK, Agarwal N, Patel SN et al (2019) Kinetic characterization of laccase from
Bacillus atrophaeus, and its potential in juice clarification in free and immobilized forms.
J Microbiol 57(10):900–909. https://doi.org/10.1007/s12275-019-9170-z
114. Wang H, Huang L, Li Y et al (2020) Characterization and application of a novel laccase
derived from Bacillus amyloliquefaciens. Int J Biol Macromol 150:982–990. https://doi.org/
10.1016/j.ijbiomac.2019.11.117
115. Koschorreck K, Schmid RD, Urlacher VB (2009) Improving the functional expression of a
Bacillus licheniformis laccase by random and site-directed mutagenesis. BMC Biotechnol
9:12. https://doi.org/10.1186/1472-6750-9-12
116. Reiss R, Ihssen J, Thöny-Meyer L (2011) Bacillus pumilus laccase: a heat stable enzyme
with a wide substrate spectrum. BMC Biotechnol 11:9. https://doi.org/10.1186/1472-675011-9
117. Hullo M-F, Moszer I, Danchin A et al (2001) CotA of Bacillus subtilis Is a copper-dependent
laccase. J Bacteriol 183(18):5426–5430. https://doi.org/10.1128/JB.183.18.5426-5430.2001
118. Martins LO, Soares CM, Pereira MM et al (2002) Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the
Bacillus subtilis endospore coat. J Biol Chem 277(21):18849–18859. https://doi.org/10.
1074/jbc.M200827200
119. Jeon S-J, Park J-H (2020) Refolding, characterization, and dye decolorization ability of a
highly thermostable laccase from Geobacillus sp. JS12. Protein Expr Purif 173:105646.
https://doi.org/10.1016/j.pep.2020.105646
120. Roberts JN, Singh R, Grigg JC et al (2011) Characterization of dye-decolorizing peroxidases
from Rhodococcus jostii RHA1. Biochemistry 50(23):5108–5119. https://doi.org/10.1021/
bi200427h
121. Endo K, Hayashi Y, Hibi T et al (2003) Enzymological characterization of EpoA, a
laccase-like phenol oxidase produced by Streptomyces griseus. J Biochem 133(5):671–677.
https://doi.org/10.1093/jb/mvg086
468
G.-S. Nguyen et al.
the litter-decomposing fungi Stropharia rugosoannulata and Stropharia coronilla. Chemosphere 83(3):226–232. https://doi.org/10.1016/j.chemosphere.2010.12.094
104. Hatakka A (1994) Lignin-modifying enzymes from selected white-rot fungi: production and
role from in lignin degradation. FEMS Microbiol Rev 13(2–3):125–135. https://doi.org/10.
1111/j.1574-6976.1994.tb00039.x
105. Selinheimo E, Kruus K, Buchert J et al (2006) Effects of laccase, xylanase and their
combination on the rheological properties of wheat doughs. J Cereal Sci 43(2):152–159.
https://doi.org/10.1016/j.jcs.2005.08.007
106. Kurtz MB, Champe SP (1982) Purification and characterization of the conidial laccase of
Aspergillus nidulans. J Bacteriol 151(3):1338–1345
107. Marbach I, Harel E, Mayer AM (1984) Molecular properties of extracellular Botrytis cinerea
laccase. Phytochemistry 23(12):2713–2717. https://doi.org/10.1016/0031-9422(84)83001-0
108. Chefetz B, Chen Y, Hadar Y (1998) Purification and characterization of laccase from
Chaetomium thermophilium and Its role in humification. Appl Environ Microbiol 64
(9):3175–3179
109. Kiiskinen L-L, Viikari L, Kruus K (2002) Purification and characterisation of a novel laccase
from the Ascomycete melanocarpus albomyces. Appl Microbiol Biotechnol 59(2–3):198–
204. https://doi.org/10.1007/s00253-002-1012-x
110. Froehner SC, Eriksson K-E (1974) Purification and properties of Neurospora crassa laccase.
J Bacteriol 120(1):458–465
111. Iyer G, Chattoo BB (2003) Purification and characterization of laccase from the rice blast
fungus. Magnaporthe grisea FEMS Microbiol Lett 227(1):121–126. https://doi.org/10.1016/
S0378-1097(03)00658-X
112. de Gonzalo G, Colpa DI, Habib MHM et al (2016) Bacterial enzymes involved in lignin
degradation. J Biotechnol 236:110–119. https://doi.org/10.1016/j.jbiotec.2016.08.011
113. Narnoliya LK, Agarwal N, Patel SN et al (2019) Kinetic characterization of laccase from
Bacillus atrophaeus, and its potential in juice clarification in free and immobilized forms.
J Microbiol 57(10):900–909. https://doi.org/10.1007/s12275-019-9170-z
114. Wang H, Huang L, Li Y et al (2020) Characterization and application of a novel laccase
derived from Bacillus amyloliquefaciens. Int J Biol Macromol 150:982–990. https://doi.org/
10.1016/j.ijbiomac.2019.11.117
115. Koschorreck K, Schmid RD, Urlacher VB (2009) Improving the functional expression of a
Bacillus licheniformis laccase by random and site-directed mutagenesis. BMC Biotechnol
9:12. https://doi.org/10.1186/1472-6750-9-12
116. Reiss R, Ihssen J, Thöny-Meyer L (2011) Bacillus pumilus laccase: a heat stable enzyme
with a wide substrate spectrum. BMC Biotechnol 11:9. https://doi.org/10.1186/1472-675011-9
117. Hullo M-F, Moszer I, Danchin A et al (2001) CotA of Bacillus subtilis Is a copper-dependent
laccase. J Bacteriol 183(18):5426–5430. https://doi.org/10.1128/JB.183.18.5426-5430.2001
118. Martins LO, Soares CM, Pereira MM et al (2002) Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the
Bacillus subtilis endospore coat. J Biol Chem 277(21):18849–18859. https://doi.org/10.
1074/jbc.M200827200
119. Jeon S-J, Park J-H (2020) Refolding, characterization, and dye decolorization ability of a
highly thermostable laccase from Geobacillus sp. JS12. Protein Expr Purif 173:105646.
https://doi.org/10.1016/j.pep.2020.105646
120. Roberts JN, Singh R, Grigg JC et al (2011) Characterization of dye-decolorizing peroxidases
from Rhodococcus jostii RHA1. Biochemistry 50(23):5108–5119. https://doi.org/10.1021/
bi200427h
121. Endo K, Hayashi Y, Hibi T et al (2003) Enzymological characterization of EpoA, a
laccase-like phenol oxidase produced by Streptomyces griseus. J Biochem 133(5):671–677.
https://doi.org/10.1093/jb/mvg086
468
G.-S. Nguyen et al.