48. Garcia-Ruiz E, Gonzalez-Perez D, Ruiz-Dueñas FJ et al (2012) Directed evolution of a
temperature-, peroxide- and alkaline pH-tolerant versatile peroxidase. Biochem J 441
(1):487–498. https://doi.org/10.1042/BJ20111199
49. Colpa DI, Fraaije MW, van Bloois E (2014) DyP-type peroxidases: a promising and versatile
class of enzymes. J Ind Microbiol Biotechnol 41(1):1–7. https://doi.org/10.1007/s10295013-1371-6
50. Rahmanpour R, Rea D, Jamshidi S et al (2016) Structure of Thermobifida fusca DyP-type
peroxidase and activity towards Kraft lignin and lignin model compounds. Arch Biochem
Biophys 594:54–60. https://doi.org/10.1016/j.abb.2016.02.019
51. Brissos V, Tavares D, Sousa AC et al (2017) Engineering a Bacterial DyP-type peroxidase
for enhanced oxidation of lignin-related phenolics at alkaline pH. ACS Catalysis 7(5):3454–
3465. https://doi.org/10.1021/acscatal.6b03331
52. Solomon EI, Heppner DE, Johnston EM et al (2014) Copper active sites in biology. Chem
Rev 114(7):3659–3853. https://doi.org/10.1021/cr400327t
53. Reiss R, Ihssen J, Richter M et al (2013) Laccase versus laccase-like multi-copper oxidase: a
comparative study of similar enzymes with diverse substrate spectra. PLoS ONE 8(6):
e65633. https://doi.org/10.1371/journal.pone.0065633
54. Ravi K, Abdelaziz OY, Nöbel M et al (2019) Bacterial conversion of depolymerized Kraft
lignin. Biotechnol Biofuels 12(1):56. https://doi.org/10.1186/s13068-019-1397-8
55. Bourbonnais R, Paice MG, Reid ID et al (1995) Lignin oxidation by laccase isozymes from
Trametes
versicolor
and
role
of
the
mediator
2,2′-azinobis
(3-ethylbenzthiazoline-6-sulfonate) in kraft lignin depolymerization. Appl Environ Microbiol 61(5):1876–1880
56. Jones SM, Solomon EI (2015) Electron transfer and reaction mechanism of laccases. Cell
Mol Life Sci 72(5):869–883. https://doi.org/10.1007/s00018-014-1826-6
57. Zhu Y, Zhang Y, Zhan J et al (2019) Axial bonds at the T1 Cu site of Thermus thermophilus
SG0.5JP17–16 laccase influence enzymatic properties. FEBS Open Bio 9 (5):986–995.
https://doi.org/10.1002/2211-5463.12633
58. Machczynski MC, Vijgenboom E, Samyn B et al (2004) Characterization of SLAC: a small
laccase from Streptomyces coelicolor with unprecedented activity. Protein Sci 13(9):2388–
2397. https://doi.org/10.1110/ps.04759104
59. Skalova T, Dohnalek J, Ostergaard LH et al (2009) The structure of the small laccase from
Streptomyces coelicolor reveals a link between laccases and nitrite reductases. J Mol Biol
385(4):1165–1178. https://doi.org/10.1016/j.jmb.2008.11.024
60. Mate DM, Alcalde M (2015) Laccase engineering: from rational design to directed
evolution. Biotechnol Adv 33(1):25–40. https://doi.org/10.1016/j.biotechadv.2014.12.007
61. Durao P, Bento I, Fernandes AT et al (2006) Perturbations of the T1 copper site in the CotA
laccase from Bacillus subtilis: structural, biochemical, enzymatic and stability studies. J Biol
Inorg Chem 11(4):514–526. https://doi.org/10.1007/s00775-006-0102-0
62. Gupta N, Lee FS, Farinas ET (2010) Laboratory evolution of laccase for substrate
specificity. J Mol Catal B: Enzym 62(3–4):230–234. https://doi.org/10.1016/j.molcatb.2009.
10.012
63. Chen Y, Luo Q, Zhou W et al (2017) Improving the catalytic efficiency of Bacillus pumilus
CotA-laccase by site-directed mutagenesis. Appl Microbiol Biotechnol 101(5):1935–1944.
https://doi.org/10.1007/s00253-016-7962-1
64. Kataoka K, Komori H, Ueki Y et al (2007) Structure and function of the engineered
multicopper oxidase CueO from Escherichia coli—deletion of the methionine-rich helical
region covering the substrate-binding site. J Mol Biol 373(1):141–152. https://doi.org/10.
1016/j.jmb.2007.07.041
65. Hämäläinen V, Grönroos T, Suonpää A et al (2018) Enzymatic processes to unlock the
lignin value. Front Bioeng Biotechnol 6. https://doi.org/10.3389/fbioe.2018.00020
66. Zerva A, Simić S, Topakas E et al (2019) Applications of microbial laccases: patent review
of the past decade (2009–2019). Catalysts 9(12). https://doi.org/10.3390/catal9121023
Recent Advances in Enzymatic Conversion of Lignin …
465
temperature-, peroxide- and alkaline pH-tolerant versatile peroxidase. Biochem J 441
(1):487–498. https://doi.org/10.1042/BJ20111199
49. Colpa DI, Fraaije MW, van Bloois E (2014) DyP-type peroxidases: a promising and versatile
class of enzymes. J Ind Microbiol Biotechnol 41(1):1–7. https://doi.org/10.1007/s10295013-1371-6
50. Rahmanpour R, Rea D, Jamshidi S et al (2016) Structure of Thermobifida fusca DyP-type
peroxidase and activity towards Kraft lignin and lignin model compounds. Arch Biochem
Biophys 594:54–60. https://doi.org/10.1016/j.abb.2016.02.019
51. Brissos V, Tavares D, Sousa AC et al (2017) Engineering a Bacterial DyP-type peroxidase
for enhanced oxidation of lignin-related phenolics at alkaline pH. ACS Catalysis 7(5):3454–
3465. https://doi.org/10.1021/acscatal.6b03331
52. Solomon EI, Heppner DE, Johnston EM et al (2014) Copper active sites in biology. Chem
Rev 114(7):3659–3853. https://doi.org/10.1021/cr400327t
53. Reiss R, Ihssen J, Richter M et al (2013) Laccase versus laccase-like multi-copper oxidase: a
comparative study of similar enzymes with diverse substrate spectra. PLoS ONE 8(6):
e65633. https://doi.org/10.1371/journal.pone.0065633
54. Ravi K, Abdelaziz OY, Nöbel M et al (2019) Bacterial conversion of depolymerized Kraft
lignin. Biotechnol Biofuels 12(1):56. https://doi.org/10.1186/s13068-019-1397-8
55. Bourbonnais R, Paice MG, Reid ID et al (1995) Lignin oxidation by laccase isozymes from
Trametes
versicolor
and
role
of
the
mediator
2,2′-azinobis
(3-ethylbenzthiazoline-6-sulfonate) in kraft lignin depolymerization. Appl Environ Microbiol 61(5):1876–1880
56. Jones SM, Solomon EI (2015) Electron transfer and reaction mechanism of laccases. Cell
Mol Life Sci 72(5):869–883. https://doi.org/10.1007/s00018-014-1826-6
57. Zhu Y, Zhang Y, Zhan J et al (2019) Axial bonds at the T1 Cu site of Thermus thermophilus
SG0.5JP17–16 laccase influence enzymatic properties. FEBS Open Bio 9 (5):986–995.
https://doi.org/10.1002/2211-5463.12633
58. Machczynski MC, Vijgenboom E, Samyn B et al (2004) Characterization of SLAC: a small
laccase from Streptomyces coelicolor with unprecedented activity. Protein Sci 13(9):2388–
2397. https://doi.org/10.1110/ps.04759104
59. Skalova T, Dohnalek J, Ostergaard LH et al (2009) The structure of the small laccase from
Streptomyces coelicolor reveals a link between laccases and nitrite reductases. J Mol Biol
385(4):1165–1178. https://doi.org/10.1016/j.jmb.2008.11.024
60. Mate DM, Alcalde M (2015) Laccase engineering: from rational design to directed
evolution. Biotechnol Adv 33(1):25–40. https://doi.org/10.1016/j.biotechadv.2014.12.007
61. Durao P, Bento I, Fernandes AT et al (2006) Perturbations of the T1 copper site in the CotA
laccase from Bacillus subtilis: structural, biochemical, enzymatic and stability studies. J Biol
Inorg Chem 11(4):514–526. https://doi.org/10.1007/s00775-006-0102-0
62. Gupta N, Lee FS, Farinas ET (2010) Laboratory evolution of laccase for substrate
specificity. J Mol Catal B: Enzym 62(3–4):230–234. https://doi.org/10.1016/j.molcatb.2009.
10.012
63. Chen Y, Luo Q, Zhou W et al (2017) Improving the catalytic efficiency of Bacillus pumilus
CotA-laccase by site-directed mutagenesis. Appl Microbiol Biotechnol 101(5):1935–1944.
https://doi.org/10.1007/s00253-016-7962-1
64. Kataoka K, Komori H, Ueki Y et al (2007) Structure and function of the engineered
multicopper oxidase CueO from Escherichia coli—deletion of the methionine-rich helical
region covering the substrate-binding site. J Mol Biol 373(1):141–152. https://doi.org/10.
1016/j.jmb.2007.07.041
65. Hämäläinen V, Grönroos T, Suonpää A et al (2018) Enzymatic processes to unlock the
lignin value. Front Bioeng Biotechnol 6. https://doi.org/10.3389/fbioe.2018.00020
66. Zerva A, Simić S, Topakas E et al (2019) Applications of microbial laccases: patent review
of the past decade (2009–2019). Catalysts 9(12). https://doi.org/10.3390/catal9121023
Recent Advances in Enzymatic Conversion of Lignin …
465