122. Molina-Guijarro JM, Pérez J, Muñoz-Dorado J et al (2009) Detoxification of azo dyes by a
novel pH-versatile, salt-resistant laccase from Streptomyces ipomoea. Int Microbiol 12
(1):13–21. https://doi.org/10.2436/20.1501.01.77
123. Suzuki T, Endo K, Ito M et al (2003) A thermostable laccase from Streptomyces lavendulae
REN-7: purification, characterization, nucleotide sequence, and expression. Biosci Biotechnol Biochem 67(10):2167–2175. https://doi.org/10.1271/bbb.67.2167
124. Diamantidis G, Effosse A, Potier P et al (2000) Purification and characterization of the first
bacterial laccase in the rhizospheric bacterium Azospirillum lipoferum. Soil Biol Biochem 32
(7):919–927. https://doi.org/10.1016/S0038-0717(99)00221-7
125. Givaudan A, Effosse A, Faure D et al (1993) Polyphenol oxidase in Azospirillum lipoferum
isolated from rice rhizosphere: Evidence for laccase activity in non-motile strains of
Azospirillum lipoferum. FEMS Microbiol Lett 108(2):205–210. https://doi.org/10.1111/j.
1574-6968.1993.tb06100.x
126. Pawlik A, Wójcik M, Rułka K et al (2016) Purification and characterization of laccase from
Sinorhizobium meliloti and analysis of the lacc gene. Int J Biol Macromol 92:138–147.
https://doi.org/10.1016/j.ijbiomac.2016.07.012
127. Masai E, Katayama Y, Nishikawa S et al (1999) Characterization of Sphingomonas
paucimobilis SYK-6 genes involved in degradation of lignin-related compounds. J Ind
Microbiol Biotechnol 23(4–5):364–373. https://doi.org/10.1038/sj.jim.2900747
128. Picart P, de María PD, Schallmey A (2015) From gene to biorefinery: microbial b-etherases
as promising biocatalysts for lignin valorization. Front Microbiol 6. https://doi.org/10.3389/
fmicb.2015.00916
129. Grass G, Rensing C (2001) CueO is a multi-copper oxidase that confers copper tolerance in
Escherichia coli. Biochem Biophys Res Commun 286(5):902–908. https://doi.org/10.1006/
bbrc.2001.5474
130. Liu X, Yuan Z, Wang J et al (2017) Crystal structure and biochemical features of
dye-decolorizing peroxidase YfeX from Escherichia coli O157 Asp143 and Arg232 play
divergent roles toward different substrates. Biochem Biophys Res Commun 484(1):40–44.
https://doi.org/10.1016/j.bbrc.2017.01.081
131. Kalyani DC, Phugare SS, Shedbalkar UU et al (2011) Purification and characterization of a
bacterial peroxidase from the isolated strain Pseudomonas sp. SUK1 and its application for
textile dye decolorization. Ann Microbiol 61(3):483–491. https://doi.org/10.1007/s13213010-0162-9
132. Lambertz C, Ece S, Fischer R et al (2016) Progress and obstacles in the production and
application of recombinant lignin-degrading peroxidases. Bioengineered 7(3):145–154.
https://doi.org/10.1080/21655979.2016.1191705
133. McMahon AM, Doyle EM, Brooks S et al (2007) Biochemical characterisation of the
coexisting tyrosinase and laccase in the soil bacterium Pseudomonas putida F6. Enzyme
Microb Technol 40(5):1435–1441. https://doi.org/10.1016/j.enzmictec.2006.10.020
134. Miyazaki K (2005) A hyperthermophilic laccase from Thermus thermophilus HB27.
Extremophiles 9(6):415–425. https://doi.org/10.1007/s00792-005-0458-z
135. Uthandi S, Saad B, Humbard MA et al (2010) LccA, an Archaeal laccase secreted as a
highly stable glycoprotein into the extracellular medium by Haloferax volcanii. Appl
Environ Microbiol 76(3):733–743. https://doi.org/10.1128/AEM.01757-09
136. Fernandes AT, Damas JM, Todorovic S et al (2010) The multicopper oxidase from the
archaeon Pyrobaculum aerophilum shows nitrous oxide reductase activity. FEBS J 277
(15):3176–3189. https://doi.org/10.1111/j.1742-4658.2010.07725.x
137. Alcalde M, Bulter T (2003) Colorimetric assays for screening laccases. In: Arnold FH,
Georgiou G (eds) Directed enzyme evolution: screening and selection methods. Methods in
molecular biology
™ . Humana Press, Totowa, pp 193–201. https://doi.org/10.1385/1-59259396-8:193
Recent Advances in Enzymatic Conversion of Lignin …
469
novel pH-versatile, salt-resistant laccase from Streptomyces ipomoea. Int Microbiol 12
(1):13–21. https://doi.org/10.2436/20.1501.01.77
123. Suzuki T, Endo K, Ito M et al (2003) A thermostable laccase from Streptomyces lavendulae
REN-7: purification, characterization, nucleotide sequence, and expression. Biosci Biotechnol Biochem 67(10):2167–2175. https://doi.org/10.1271/bbb.67.2167
124. Diamantidis G, Effosse A, Potier P et al (2000) Purification and characterization of the first
bacterial laccase in the rhizospheric bacterium Azospirillum lipoferum. Soil Biol Biochem 32
(7):919–927. https://doi.org/10.1016/S0038-0717(99)00221-7
125. Givaudan A, Effosse A, Faure D et al (1993) Polyphenol oxidase in Azospirillum lipoferum
isolated from rice rhizosphere: Evidence for laccase activity in non-motile strains of
Azospirillum lipoferum. FEMS Microbiol Lett 108(2):205–210. https://doi.org/10.1111/j.
1574-6968.1993.tb06100.x
126. Pawlik A, Wójcik M, Rułka K et al (2016) Purification and characterization of laccase from
Sinorhizobium meliloti and analysis of the lacc gene. Int J Biol Macromol 92:138–147.
https://doi.org/10.1016/j.ijbiomac.2016.07.012
127. Masai E, Katayama Y, Nishikawa S et al (1999) Characterization of Sphingomonas
paucimobilis SYK-6 genes involved in degradation of lignin-related compounds. J Ind
Microbiol Biotechnol 23(4–5):364–373. https://doi.org/10.1038/sj.jim.2900747
128. Picart P, de María PD, Schallmey A (2015) From gene to biorefinery: microbial b-etherases
as promising biocatalysts for lignin valorization. Front Microbiol 6. https://doi.org/10.3389/
fmicb.2015.00916
129. Grass G, Rensing C (2001) CueO is a multi-copper oxidase that confers copper tolerance in
Escherichia coli. Biochem Biophys Res Commun 286(5):902–908. https://doi.org/10.1006/
bbrc.2001.5474
130. Liu X, Yuan Z, Wang J et al (2017) Crystal structure and biochemical features of
dye-decolorizing peroxidase YfeX from Escherichia coli O157 Asp143 and Arg232 play
divergent roles toward different substrates. Biochem Biophys Res Commun 484(1):40–44.
https://doi.org/10.1016/j.bbrc.2017.01.081
131. Kalyani DC, Phugare SS, Shedbalkar UU et al (2011) Purification and characterization of a
bacterial peroxidase from the isolated strain Pseudomonas sp. SUK1 and its application for
textile dye decolorization. Ann Microbiol 61(3):483–491. https://doi.org/10.1007/s13213010-0162-9
132. Lambertz C, Ece S, Fischer R et al (2016) Progress and obstacles in the production and
application of recombinant lignin-degrading peroxidases. Bioengineered 7(3):145–154.
https://doi.org/10.1080/21655979.2016.1191705
133. McMahon AM, Doyle EM, Brooks S et al (2007) Biochemical characterisation of the
coexisting tyrosinase and laccase in the soil bacterium Pseudomonas putida F6. Enzyme
Microb Technol 40(5):1435–1441. https://doi.org/10.1016/j.enzmictec.2006.10.020
134. Miyazaki K (2005) A hyperthermophilic laccase from Thermus thermophilus HB27.
Extremophiles 9(6):415–425. https://doi.org/10.1007/s00792-005-0458-z
135. Uthandi S, Saad B, Humbard MA et al (2010) LccA, an Archaeal laccase secreted as a
highly stable glycoprotein into the extracellular medium by Haloferax volcanii. Appl
Environ Microbiol 76(3):733–743. https://doi.org/10.1128/AEM.01757-09
136. Fernandes AT, Damas JM, Todorovic S et al (2010) The multicopper oxidase from the
archaeon Pyrobaculum aerophilum shows nitrous oxide reductase activity. FEBS J 277
(15):3176–3189. https://doi.org/10.1111/j.1742-4658.2010.07725.x
137. Alcalde M, Bulter T (2003) Colorimetric assays for screening laccases. In: Arnold FH,
Georgiou G (eds) Directed enzyme evolution: screening and selection methods. Methods in
molecular biology
™ . Humana Press, Totowa, pp 193–201. https://doi.org/10.1385/1-59259396-8:193
Recent Advances in Enzymatic Conversion of Lignin …
469