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32. Savelli B, Li Q, Webber M et al (2019) RedoxiBase: a database for ROS homeostasis
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33. Bugg TDH, Williamson JJ, Rashid GMM (2020) Bacterial enzymes for lignin depolymerisation: new biocatalysts for generation of renewable chemicals from biomass. Curr Opin
Chem Biol 55:26–33. https://doi.org/10.1016/j.cbpa.2019.11.007
34. Yoshida T, Sugano Y (2015) A structural and functional perspective of DyP-type peroxidase
family. Arch Biochem Biophys 574:49–55. https://doi.org/10.1016/j.abb.2015.01.022
35. Levasseur A, Piumi F, Coutinho PM et al (2008) FOLy: an integrated database for the
classification and functional annotation of fungal oxidoreductases potentially involved in the
degradation of lignin and related aromatic compounds. Fungal Genet Biol 45(5):638–645.
https://doi.org/10.1016/j.fgb.2008.01.004
36. Abdel-Hamid AM, Solbiati JO, Cann IK (2013) Insights into lignin degradation and its
potential industrial applications. Adv Appl Microbiol 82:1–28. https://doi.org/10.1016/
B978-0-12-407679-2.00001-6
37. Cragg SM, Beckham GT, Bruce NC et al (2015) Lignocellulose degradation mechanisms
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2015.10.018
38. Wong DW (2009) Structure and action mechanism of ligninolytic enzymes. Appl Biochem
Biotechnol 157(2):174–209. https://doi.org/10.1007/s12010-008-8279-z
39. Saez-Jimenez V, Rencoret J, Rodriguez-Carvajal MA et al (2016) Role of surface tryptophan
for peroxidase oxidation of nonphenolic lignin. Biotechnol Biofuels 9:198. https://doi.org/
10.1186/s13068-016-0615-x
40. Ryu K, Kang JH, Wang L et al (2008) Expression in yeast of secreted lignin peroxidase with
improved 2,4-dichlorophenol degradability by DNA shuffling. J Biotechnol 135(3):241–246.
https://doi.org/10.1016/j.jbiotec.2008.04.007
41. Ryu K, Hwang SY, Kim KH et al (2008) Functionality improvement of fungal lignin
peroxidase by DNA shuffling for 2,4-dichlorophenol degradability and H 2 O 2 stability.
J Biotechnol 133(1):110–115. https://doi.org/10.1016/j.jbiotec.2007.09.008
42. Ilić Đurđić K, Ece S, Ostafe R et al (2020) Flow cytometry-based system for screening of
lignin peroxidase mutants with higher oxidative stability. J Biosci Bioeng 129(6):664–671.
https://doi.org/10.1016/j.jbiosc.2019.12.009
43. Sharma A (2020) Lignocellulolytic Enzymology. In: Aggarwal NK, Sharma A (eds) Water
hyacinth: a potential lignocellulosic biomass for bioethanol. Springer International
Publishing, Berlin, pp 21–35. https://doi.org/10.1007/978-3-030-35632-3_3
44. Miyazaki-Imamura C, Oohira K, Kitagawa R et al (2003) Improvement of H 2 O 2 stability of
manganese peroxidase by combinatorial mutagenesis and high-throughput screening using
in vitro expression with protein disulfide isomerase. Protein Eng 16(6):423–428. https://doi.
org/10.1093/protein/gzg054
45. Reading NS, Aust SD (2000) Engineering a disulfide bond in recombinant manganese
peroxidase results in increased thermostability. Biotechnol Prog 16(3):326–333. https://doi.
org/10.1021/bp0000151
46. Saez-Jimenez V, Fernandez-Fueyo E, Medrano FJ et al (2015) Improving the pH-stability of
versatile peroxidase by comparative structural analysis with a naturally-stable manganese
peroxidase. PLoS ONE 10(10):e0140984. https://doi.org/10.1371/journal.pone.0140984
47. Perez-Boada M, Ruiz-Duenas FJ, Pogni R et al (2005) Versatile peroxidase oxidation of
high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and
crystallographic investigation of three long-range electron transfer pathways. J Mol Biol 354
(2):385–402. https://doi.org/10.1016/j.jmb.2005.09.047
464
G.-S. Nguyen et al.
lignin degradation. Biochemistry 53(24):4047–4058. https://doi.org/10.1021/bi500285t
31. Sirim D, Wagner F, Wang L et al (2011) The laccase engineering database: a classification
and analysis system for laccases and related multicopper oxidases. Database (Oxford) 2011:
bar006. https://doi.org/10.1093/database/bar006
32. Savelli B, Li Q, Webber M et al (2019) RedoxiBase: a database for ROS homeostasis
regulated proteins. Redox Biol 26:101247. https://doi.org/10.1016/j.redox.2019.101247
33. Bugg TDH, Williamson JJ, Rashid GMM (2020) Bacterial enzymes for lignin depolymerisation: new biocatalysts for generation of renewable chemicals from biomass. Curr Opin
Chem Biol 55:26–33. https://doi.org/10.1016/j.cbpa.2019.11.007
34. Yoshida T, Sugano Y (2015) A structural and functional perspective of DyP-type peroxidase
family. Arch Biochem Biophys 574:49–55. https://doi.org/10.1016/j.abb.2015.01.022
35. Levasseur A, Piumi F, Coutinho PM et al (2008) FOLy: an integrated database for the
classification and functional annotation of fungal oxidoreductases potentially involved in the
degradation of lignin and related aromatic compounds. Fungal Genet Biol 45(5):638–645.
https://doi.org/10.1016/j.fgb.2008.01.004
36. Abdel-Hamid AM, Solbiati JO, Cann IK (2013) Insights into lignin degradation and its
potential industrial applications. Adv Appl Microbiol 82:1–28. https://doi.org/10.1016/
B978-0-12-407679-2.00001-6
37. Cragg SM, Beckham GT, Bruce NC et al (2015) Lignocellulose degradation mechanisms
across the Tree of Life. Curr Opin Chem Biol 29:108–119. https://doi.org/10.1016/j.cbpa.
2015.10.018
38. Wong DW (2009) Structure and action mechanism of ligninolytic enzymes. Appl Biochem
Biotechnol 157(2):174–209. https://doi.org/10.1007/s12010-008-8279-z
39. Saez-Jimenez V, Rencoret J, Rodriguez-Carvajal MA et al (2016) Role of surface tryptophan
for peroxidase oxidation of nonphenolic lignin. Biotechnol Biofuels 9:198. https://doi.org/
10.1186/s13068-016-0615-x
40. Ryu K, Kang JH, Wang L et al (2008) Expression in yeast of secreted lignin peroxidase with
improved 2,4-dichlorophenol degradability by DNA shuffling. J Biotechnol 135(3):241–246.
https://doi.org/10.1016/j.jbiotec.2008.04.007
41. Ryu K, Hwang SY, Kim KH et al (2008) Functionality improvement of fungal lignin
peroxidase by DNA shuffling for 2,4-dichlorophenol degradability and H 2 O 2 stability.
J Biotechnol 133(1):110–115. https://doi.org/10.1016/j.jbiotec.2007.09.008
42. Ilić Đurđić K, Ece S, Ostafe R et al (2020) Flow cytometry-based system for screening of
lignin peroxidase mutants with higher oxidative stability. J Biosci Bioeng 129(6):664–671.
https://doi.org/10.1016/j.jbiosc.2019.12.009
43. Sharma A (2020) Lignocellulolytic Enzymology. In: Aggarwal NK, Sharma A (eds) Water
hyacinth: a potential lignocellulosic biomass for bioethanol. Springer International
Publishing, Berlin, pp 21–35. https://doi.org/10.1007/978-3-030-35632-3_3
44. Miyazaki-Imamura C, Oohira K, Kitagawa R et al (2003) Improvement of H 2 O 2 stability of
manganese peroxidase by combinatorial mutagenesis and high-throughput screening using
in vitro expression with protein disulfide isomerase. Protein Eng 16(6):423–428. https://doi.
org/10.1093/protein/gzg054
45. Reading NS, Aust SD (2000) Engineering a disulfide bond in recombinant manganese
peroxidase results in increased thermostability. Biotechnol Prog 16(3):326–333. https://doi.
org/10.1021/bp0000151
46. Saez-Jimenez V, Fernandez-Fueyo E, Medrano FJ et al (2015) Improving the pH-stability of
versatile peroxidase by comparative structural analysis with a naturally-stable manganese
peroxidase. PLoS ONE 10(10):e0140984. https://doi.org/10.1371/journal.pone.0140984
47. Perez-Boada M, Ruiz-Duenas FJ, Pogni R et al (2005) Versatile peroxidase oxidation of
high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and
crystallographic investigation of three long-range electron transfer pathways. J Mol Biol 354
(2):385–402. https://doi.org/10.1016/j.jmb.2005.09.047
464
G.-S. Nguyen et al.