Lignin-degrading enzymes

FEBS Journal

Volumn 282, Issue 7, 2015, Pages 1190-1213

  Pollegioni, Loredano ^a   Tonin, Fabio ^a   Rosini, Elena ^a  

^a UNIVERSITY OF INSUBRIA   (Italy)

Author keywords

biorefinery; green biotechnology; lignin valorization; ligninolytic enzymes; lignocellulosic biomass

Indexed keywords

CELLULOSE; ENZYME; ETHER DERIVATIVE; HEMICELLULOSE; LIGNIN; LIGNIN DEGRADING ENZYME; LIGNOCELLULOSE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; FUNGAL PROTEIN; LACCASE; LIGNIN PEROXIDASE; PEROXIDASE;

BACTERIA; BIOCATALYST; BIOTECHNOLOGY; CATABOLISM; CHEMICAL BOND; CHEMICAL MODIFICATION; DEGRADATION; ENZYME ENGINEERING; FOSSIL; INDUSTRY; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN ENGINEERING; REVIEW; WHITE ROT FUNGUS; BIOCATALYSIS; CHEMISTRY; KINETICS; OXIDATION REDUCTION REACTION;

FUNGI;

BACTERIAL PROTEINS; BIOCATALYSIS; FUNGAL PROTEINS; KINETICS; LACCASE; LIGNIN; OXIDATION-REDUCTION; PEROXIDASES; PROTEIN ENGINEERING;

EID: 84926010646     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.13224     Document Type: Review

References (128)

1. Mai C, Majcherczyk A, &, Huttermann A, (2000) Chemo-enzymatic synthesis and characterization of graft copolymers from lignin and acrylic compounds. Enzyme Microb Technol 27, 167-175.
2. FitzPatrick M, Champagne P, Cunningham MF, &, Whitney RA, (2010) A biorefinery processing perspective: treatment of lignocellulosic materials for the production of value-added products. Biores Technol 101, 8915-8922.
3. Pandey MP, &, Kim CS, (2011) Lignin depolymerization and conversion: a review of thermochemical methods. Chem Eng Technol 34, 29-41.
4. Zhou CH, Xia X, Lin CX, Tong DS, &, Beltramini J, (2011) Catalytic conversion of lignocellulosic biomass to fine chemicals and fuels. Chem Soc Rev 40, 5588-5617.
5. Nanayakkara S, Patti AF, &, Saito K, (2014) Chemical depolymerization of lignin involving the redistribution mechanism with phenols and repolymerization of depolymerized products. Green Chem 16, 1897-1903.
6. Dashtban M, Schraft H, Syed TA, &, Qin W, (2010) Fungal biodegradation and enzymatic modification of lignin. Int J Biochem Mol Biol 1, 36-50.
7. Wong DWS, (2009) Structure and action mechanism of ligninolytic enzymes. Appl Biochem Biotech 157, 174-209.
8. Forney LJ, Reddy CA, Tien M, &, Aust SD, (1982) The involvement of hydroxyl radical derived from hydrogen peroxide in lignin degradation by the white rot fungus Phanerochaete chrysosporium. J Biol Chem 257, 11455-11462.
9. Bourbonnais R, Leech D, &, Paice MG, (1998) Electrochemical analysis of the interactions of laccase mediators with lignin model compounds. Biochim Biophys Acta 1379, 381-390.
10. Crestini C, Jurasek L, &, Argyropoulos DS, (2003) On the mechanism of the laccase-mediator system in the oxidation of lignin. Chem Eur J 9, 5371-5378.
11. Cañas AI, &, Camarero S, (2010) Laccases and their natural mediators: biotechnological tools for sustainable eco-friendly processes. Biotechnol Adv 28, 694-705.
12. Lange H, Decina S, &, Crestini C, (2013) Oxidative upgrade of lignin-recent routes reviewed. Eur Polym J 49, 1151-1173.
13. Asgher M, Shahid M, Kamal S, &, Iqbal HMN, (2014) Recent trends and valorization of immobilization strategies and ligninolytic enzymes by industrial biotechnology. J Mol Catal B-Enzym 101, 56-66.
14. Welinder KG, Mauro JM, &, Norskov-Lauritsen L, (1992) Structure of plant and fungal peroxidases. Biochem Soc Trans 20, 337-340.
15. Wang W, &, Wen X, (2009) Expression of lignin peroxidase H2 from Phanerochaete chrysosporium by multi-copy recombinant Pichia strain. J Environ Sci 21, 218-222.
16. Valli K, Wariishi H, &, Gold MH, (1990) Oxidation of monomethoxylated aromatic compounds by lignin peroxidase: role of veratryl alcohol in lignin biodegradation. Biochemistry 29, 8535-8539.
17. Hammel KE, Tien M, Kalyanaraman B, &, Kirk TK, (1985) Mechanism of oxidative C alpha-C beta cleavage of a lignin model dimer by Phanerochaete chrysosporium ligninase. Stoichiometry and involvement of free radicals. J Biol Chem 260, 8348-8353.
18. Lundell T, Wever R, Floris R, Harvey P, Hatakka A, Brunow G, &, Schoemaker H, (1993) Lignin peroxidase L3 from Phlebia radiata. Pre-steady-state and steady-state studies with veratryl alcohol and a non-phenolic lignin model compound 1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol. Eur J Biochem 211, 391-402.
19. Baciocchi E, Fabbri C, &, Lanzalunga O, (2003) Lignin peroxidase-catalyzed oxidation of nonphenolic trimeric lignin model compounds: fragmentation reactions in the intermediate radical cations. J Org Chem 68, 9061-9069.
20. Choinowski T, Blodig W, Winterhalter KH, &, Piontek K, (1999) The crystal structure of lignin peroxidase at 1.70 A resolution reveals a hydroxy group on the cbeta of tryptophan 171: a novel radical site formed during the redox cycle. J Mol Biol 286, 809-827.
21. Edwards SL, Raag R, Wariishi H, Gold MH, &, Poulos TL, (1993) Crystal structure of lignin peroxidase. PNAS 90, 750-754.
22. Poulos TL, Edwards SL, Wariishi H, &, Gold MH, (1993) Crystallographic refinement of lignin peroxidase at 2 A. J Biol Chem 268, 4429-4440.
23. Blodig W, Smith AT, Doyle WA, &, Piontek K, (2001) Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism. J Mol Biol 305, 851-861.
24. Doyle WA, Blodig W, Veitch NC, Piontek K, &, Smith AT, (1998) Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis. Biochemistry 37, 15097-150105.
25. Gelpke MDS, Lee J, &, Gold MH, (2002) Lignin peroxidase oxidation of veratryl alcohol: Effects of the mutants H82A, Q222A, W171A, and F267L. Biochemistry 41, 3498-3506.
26. Coconi-Linares N, Magaña-Ortíz D, Guzmán-Ortiz DA, Fernández F, Loske AM, &, Gõmez-Lim MA, (2014) High-yield production of manganese peroxidase, lignin peroxidase, and versatile peroxidase in Phanerochaete chrysosporium. Appl Microbiol Biotechnol 98, 9283-9294.
27. Nie G, Reading NS, &, Aust SD, (1998) Expression of the lignin peroxidase H2 gene from Phanerochaete chrysosporium in Escherichia coli. Biochem Biophys Res Commun 249, 146-150.
28. Gelpke MDS, Mayfield-Gambill M, Cereghino GPL, &, Gold MH, (1999) Homologous expression of recombinant lignin peroxidase in Phanerochaete chrysosporium. Appl Environ Microbiol 65, 1670-1674.
29. Wang HK, Lu FP, Sun WF, &, Du LX, (2004) Heterologous expression of lignin peroxidase of Phanerochaete chrysosporium in Pichia methanolica. Biotechnol Lett 26, 1569-1573.
30. Xie J, Feng L, Xu N, Zhu GH, Yang J, Xu XL, &, Fu SY, (2007) Studies on the fusion of ligninolytic enzyme cDNAs and their expression. Bioresources 2, 598-604.
31. Hammel KE, Jensen KA Jr, Mozuch MD, Landucci LL, Tien M, &, Pease EA, (1993) Ligninolysis by a purified lignin peroxidase. J Biol Chem 268, 12274-12281.
32. Haemmerli SD, Leisola MSA, &, Fiechter A, (1986) Polymerisation of lignins by ligninases from Phanerochaete chrysosporium. FEMS Microbiol Lett 35, 33-36.
33. Brunow G, (2005) Methods to reveal the structure of lignin. In Lignin, Humic Substances and Coal. Biopolymers Online (, Hofrichter M, &, Steinbüchel A, eds), pp. 89-116. Wiley-VHC, Weinheim.
34. Ghaffar SH, &, Fan M, (2013) Structural analysis for lignin characteristics in biomass straw. Biomass Bioenergy 57, 264-279.
35. Glenn JK, &, Gold MH, (1985) Purification and characterization of an extracellular Mn(II)-dependent peroxidase from the lignin-degrading basidiomycete, Phanerochaete chrysosporium. Arch Biochem Biophys 242, 329-341.
36. Paszczynski A, Huynh VB, &, Crawford R, (1986) Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium. Arch Biochem Biophys 244, 750-765.
37. Wariishi H, Valli K, &, Gold MH, (1991) In vitro depolymerization of lignin by manganese peroxidase of Phanerochaete chrysosporium. Biochem Biophys Res Commun 176, 269-275.
38. Hammel KE, &, Cullen D, (2008) Role of fungal peroxidases in biological ligninolysis. Curr Opin Plant Biol 11, 349-355.
39. Sundaramoorthy M, Kishi K, Gold MH, &, Poulos TL, (1997) Crystal structures of substrate binding site mutants of manganese peroxidase. J Biol Chem 272, 17574-17580.
40. Sundaramoorthy M, Kishi K, Gold MH, &, Poulos TL, (1994) The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-A resolution. J Biol Chem 269, 32759-32767.
41. Gelpke MD, Youngs HL, &, Gold MH, (2000) Role of arginine 177 in the MnII binding site of manganese peroxidase. Studies with R177D, R177E, R177N, and R177Q mutants. Eur J Biochem 267, 7038-7045.
42. Sundaramoorthy M, Youngs HL, Gold MH, &, Poulos TL, (2005) High-resolution crystal structure of manganese peroxidase: substrate and inhibitor complexes. Biochemistry 44, 6463-6470.
43. Whitwam R, &, Tien M, (1996) Heterologous expression and reconstitution of fungal Mn peroxidase. Arch Biochem Biophys 333, 439-446.
44. Gu L, Lajoie C, &, Kelly C, (2003) Expression of a Phanerochaete chrysosporium manganese peroxidase gene in the yeast Pichia pastoris. Biotechnol Progr 19, 1403-1409.
45. Jiang F, Kongsaeree P, Charron R, Lajoie C, Xu H, Scott G, &, Kelly C, (2008) Production and separation of manganese peroxidase from heme amended yeast cultures. Biotechnol Bioeng 99, 540-549.
46. Timofeevski SL, Nie G, Reading NS, &, Aust SD, (1999) Addition of veratryl alcohol oxidase activity to manganese peroxidase by site-directed mutagenesis. Biochem Biophys Res Commun 256, 500-504.
47. Timofeevski SL, Nie G, Reading NS, &, Aust SD, (2000) Substrate specificity of lignin peroxidase and a S168W variant of manganese peroxidase. Arch Biochem Biophys 373, 147-153.
48. Sutherland GR, &, Aust SD, (1996) The effects of calcium on the thermal stability and activity of manganese peroxidase. Arch Biochem Biophys 332, 128-134.
49. Nie G, Reading NS, &, Aust SD, (1999) Relative stability of recombinant versus native peroxidases from Phanerochaete chrysosporium. Arch Biochem Biophys 365, 328-334.
50. Reading NS, &, Aust SD, (2000) Engineering a disulfide bond in recombinant manganese peroxidase results in increased thermostability. Biotechnol Progr 16, 326-333.
51. 2O2. FEBS Lett 509, 111-114.
52. Ufot UF, &, Akpanabiatu MI, (2012) An engineered Phlebia radiata manganese peroxidase: expression, refolding, purification and preliminary characterization. Am J Mol Biol 2, 359-370.
53. Hofrichter M, Ullrich R, Pecyna MJ, Liers C, &, Lundell T, (2010) New and classic families of secreted fungal heme peroxidases. Appl Microbiol Biotechnol 87, 871-897.
54. Ruiz-Duenas FJ, Morales M, Perez-Boada M, Choinowski T, Martinez MJ, Piontek K, &, Martinez AT, (2007) Manganese oxidation site in Pleurotus eryngii versatile peroxidase: a site-directed mutagenesis, kinetic, and crystallographic study. Biochemistry 46, 66-77.
55. Perez-Boada M, Ruiz-Duenas FJ, Pogni R, Basosi R, Choinowski T, Martinez MJ, Piontek K, &, Martinez AT, (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, 385-402.
56. Ruiz-Duenas FJ, Martinez MJ, &, Martinez AT, (1999) Heterologous expression of Pleurotus eryngii peroxidase confirms its ability to oxidize Mn(2+) and different aromatic substrates. Appl Environ Microbiol 65, 4705-4707.
57. Tien M, Kirk TK, Bull C, &, Fee JA, (1986) Steady-state and transient-state kinetic studies on the oxidation of 3,4-dimethoxybenzyl alcohol catalyzed by the ligninase of Phanerocheate chrysosporium Burds. J Biol Chem 261, 1687-1693.
58. Caramelo L, Martinez MJ, &, Martinez AT, (1999) A search for ligninolytic peroxidases in the fungus Pleurotus eryngii involving α-keto-γ-thiomethylbutyric acid and lignin model dimers. Appl Environ Microbiol 65, 916-922.
59. Fernandez-Fueyo E, Ruiz-Duenas FJ, Martinez MJ, Romero A, Hammel KE, Medrano FJ, &, Martinez AT, (2014) Ligninolytic peroxidase genes in the oyster mushroom genome: heterologous expression, molecular structure, catalytic and stability properties, and lignin-degrading ability. Biotechnol Biofuels 7, 2.
60. Tsukihara T, Honda Y, &, Watanabe T, (2006) Molecular breeding of white rot fungus Pleurotus ostreatus by homologous expression of its versatile peroxidase MnP2. Appl Microbiol Biotechnol 71, 114-120.
61. Tsukihara T, Honda Y, Sakai R, &, Watanabe T, (2006) Exclusive overproduction of recombinant versatile peroxidase MnP2 by genetically modified white rot fungus, Pleurotus ostreatus. J Biotechnol 126, 431-439.
62. Mohorcic M, Bencina M, Friedrich J, &, Jerala R, (2009) Expression of soluble versatile peroxidase of Bjerkandera adusta in Escherichia coli. Bioresour Technol 100, 851-858.
63. 2 stability study of active Pleurotus eryngii versatile peroxidase in Escherichia coli. Biotechnol Lett 34, 1537-1543.
64. Garcia-Ruiz E, Gonzalez-Perez D, Ruiz-Duenas FJ, Martinez AT, &, Alcalde M, (2012) Directed evolution of a temperature-, peroxide- and alkaline pH-tolerant versatile peroxidase. Biochem J 441, 487-498.
65. Bao X, Huang X, Lu X, &, Li JJ, (2014) Improvement of hydrogen peroxide stability of Pleurotus eryngii versatile ligninolytic peroxidase by rational protein engineering. Enz Microb Tech 54, 51-58.
66. Roberts JN, Singh R, Grigg JC, Murphy MEP, Bugg TDH, &, Eltis LD, (2011) Characterization of dye-decolorizing peroxidases from Rhodococcus jostii RHA1. Biochemistry 50, 5108-5119.
67. Ahmad M, Taylor CR, Pink D, Burton K, Eastwood D, Bending GD, &, Bugg TD, (2010) Development of novel assays for lignin degradation: comparative analysis of bacterial and fungal lignin degraders. Mol BioSyst 6, 815-821.
68. Singh R, Grigg JC, Qin W, Kadla JF, Murphy ME, &, Eltis LD, (2013) Improved manganese-oxidizing activity of DypB, a peroxidase from a lignolytic bacterium. ACS Chem Biol 8, 700-706.
69. Brown ME, Barros T, &, Chang MC, (2012) Identification and characterization of a multifunctional dye peroxidase from a lignin-reactive bacterium. ACS Chem Biol 7, 2074-2081.
70. Giardina P, Faraco V, Pezzella C, Piscitelli A, Vanhulle S, &, Sannia G, (2010) Laccases: a never-ending story. Cell Mol Life Sci 67, 369-385.
71. Thurston CF, (1994) The structure and function of fungal laccases. Microbiol-Sgm 140, 19-26.
72. Piontek K, Antorini M, &, Choinowski T, (2002) Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers. J Biol Chem 277, 37663-37669.
73. Bertrand T, Jolivalt C, Briozzo P, Caminade E, Joly N, Madzak C, &, Mougin C, (2002) Crystal structure of a four-copper laccase complexed with an arylamine: insights into substrate recognition and correlation with kinetics. Biochemistry 41, 7325-7333.
74. Skalova T, Dohnalek J, Ostergaard LH, Ostergaard PR, Kolenko P, Duskova J, Stepankova A, &, Hasek J, (2009) The structure of the small laccase from Streptomyces coelicolor reveals a link between laccases and nitrite reductases. J Mol Biol 385, 1165-1178.
75. Xu F, (1996) Catalysis of novel enzymatic iodide oxidation by fungal laccase. Appl Biochem Biotech 59, 221-230.
76. Xu F, (1997) Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases. J Biol Chem 272, 924-928.
77. Kawai S, Nakagawa M, &, Ohashi H, (1999) Aromatic ring cleavage of a non-phenolic beta-O-4 lignin model dimer by laccase of Trametes versicolor in the presence of 1-hydroxybenzotriazole. FEBS Lett 446, 355-358.
78. Kawai S, Asukai M, Ohya N, Okita K, Ito T, &, Ohashi H, (1999) Degradation of a non-phenolic beta-O-4 substructure and of polymeric lignin model compounds by laccase of Coriolus versicolor in the presence of 1-hydroxybenzotriazole. FEMS Microbiol Lett 170, 51-57.
79. LaFayette PR, Eriksson KE, &, Dean JF, (1999) Characterization and heterologous expression of laccase cDNAs from xylem tissues of yellow-poplar (Liriodendron tulipifera). Plant Mol Biol 40, 23-35.
80. Bollag JM, &, Leonowicz A, (1984) Comparative studies of extracellular fungal laccases. Appl Environ Microbiol 48, 849-854.
81. Otterbein L, Record E, Longhi S, Asther M, &, Moukha S, (2000) Molecular cloning of the cDNA encoding laccase from Pycnoporus cinnabarinus I-937 and expression in Pichia pastoris. Eur J Biochem 267, 1619-1625.
82. Molina-Guijarro JM, Perez J, Munoz-Dorado J, Guillen F, Moya R, Hernandez M, &, Arias ME, (2009) Detoxification of azo dyes by a novel pH-versatile, salt-resistant laccase from Streptomyces ipomoea. Int Microbiol 12, 13-21.
83. Li Q, Ge L, Cai J, Pei J, Xie J, &, Zhao L, (2014) Comparison of two laccases from Trametes versicolor for application in the decolorization of dyes. J Microbiol Biotechnol 24, 545-555.
84. Li Q, Pei J, Zhao L, Xie J, Cao F, &, Wang G, (2014) Overexpression and characterization of laccase from Trametes versicolor in Pichia pastoris. Appl Biochem Microbiol 50, 140-147.
85. Theerachat M, Emond S, Cambon E, Bordes F, Marty A, Nicaud JM, Chulalaksananukul W, Guieysse D, Remaud-Simeon M, &, Morel S, (2012) Engineering and production of laccase from Trametes versicolor in the yeast Yarrowia lipolytica. Bioresour Technol 125, 267-274.
86. Mate D, Garcia-Burgos C, Garcia-Ruiz E, Ballesteros AO, Camarero S, &, Alcalde M, (2010) Laboratory evolution of high-redox potential laccases. Chem Biol 17, 1030-1041.
87. Camarero S, Pardo I, Canas AI, Molina P, Record E, Martinez AT, Martinez MJ, &, Alcalde M, (2012) Engineering platforms for directed evolution of laccase from Pycnoporus cinnabarinus. Appl Environ Microbiol 78, 1370-1384.
88. Leontievsky A, Myasoedova N, Pozdnyakova N, &, Golovleva L, (1997) 'Yellow' laccase of Panus tigrinus oxidizes non-phenolic substrates without electron-transfer mediators. FEBS Lett 413, 446-448.
89. Leontievsky AA, Vares T, Lankinen P, Shergill JK, Pozdnyakova NN, Myasoedova NM, Kalkkinen N, Golovleva LA, Cammack R, Thurston CF, et al,. (1997) Blue and yellow laccases of ligninolytic fungi. FEMS Microbiol Lett 156, 9-14.
90. Palmieri G, Giardina P, Bianco C, Scaloni A, Capasso A, &, Sannia G, (1997) A novel white laccase from Pleurotus ostreatus. J Biol Chem 272, 31301-31307.
91. Zhao D, Zhang X, Cui D, &, Zhao M, (2012) Characterisation of a novel white laccase from the deuteromycete fungus Myrothecium verrucaria NF-05 and its decolourisation of dyes. PLoS ONE 7, e38817.
92. Hullo MF, Moszer I, Danchin A, &, Martin-Verstraete I, (2001) CotA of Bacillus subtilis is a copper-dependent laccase. J Bacteriol 183, 5426-5430.
93. Martins LO, Soares CM, Pereira MM, Teixeira M, Costa T, Jones GH, &, Henriques AO, (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, 18849-18859.
94. Enguita FJ, Martins LO, Henriques AO, &, Carrondo MA, (2003) Crystal structure of a bacterial endospore coat component. A laccase with enhanced thermostability properties. J Biol Chem 278, 19416-19425.
95. Durao P, Chen Z, Fernandes AT, Hildebrandt P, Murgida DH, Todorovic S, Pereira MM, Melo EP, &, Martins LO, (2008) Copper incorporation into recombinant CotA laccase from Bacillus subtilis: characterization of fully copper loaded enzymes. J Biol Inorg Chem 13, 183-193.
96. Koschorreck K, Richter SM, Ene AB, Roduner E, Schmid RD, &, Urlacher VB, (2008) Cloning and characterization of a new laccase from Bacillus licheniformis catalyzing dimerization of phenolic acids. Appl Microbiol Biotechnol 79, 217-224.
97. 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.
98. Reiss R, Ihssen J, &, Thony-Meyer L, (2011) Bacillus pumilus laccase: a heat stable enzyme with a wide substrate spectrum. BMC Biotechnol 11, 9.
99. Machczynski MC, Vijgenboom E, Samyn B, &, Canters GW, (2004) Characterization of SLAC: a small laccase from Streptomyces coelicolor with unprecedented activity. Protein Sci 13, 2388-2397.
100. Eugenio ME, Hernandez M, Moya R, Martin-Sampedro R, Villar JC, &, Arias ME, (2011) Evaluation of a new laccase produced by Streptomyces Ipomoea on biobleaching and ageing of Kraft pulps. Bioresources 6, 3231-3241.
101. Dube E, Shareck F, Hurtubise Y, Daneault C, &, Beauregard M, (2008) Homologous cloning, expression, and characterisation of a laccase from Streptomyces coelicolor and enzymatic decolourisation of an indigo dye. Appl Microbiol Biotechnol 79, 597-603.
102. Otsuka Y, Sonoki T, Ikeda S, Kajita S, Nakamura M, &, Katayama Y, (2003) Detection and characterization of a novel extracellular fungal enzyme that catalyzes the specific and hydrolytic cleavage of lignin guaiacylglycerol beta-aryl ether linkages. Eur J Biochem 270, 2353-2362.
103. Sato Y, Moriuchi H, Hishiyama S, Otsuka Y, Oshima K, Kasai D, Nakamura M, Ohara S, Katayama Y, Fukuda M, et al,. (2009) Identification of three alcohol dehydrogenase genes involved in the stereospecific catabolism of arylglycerol-beta-aryl ether by Sphingobium sp. strain SYK-6. Appl Environ Microbiol 75, 5195-5201.
104. Meux E, Prosper P, Masai E, Mulliert G, Dumarcay S, Morel M, Didierjean C, Gelhaye E, &, Favier F, (2012) Sphingobium sp SYK-6 LigG involved in lignin degradation is structurally and biochemically related to the glutathione transferase omega class. FEBS Lett 586, 3944-3950.
105. Reiter J, Strittmatter H, Wiemann LO, Schieder D, &, Sieber V, (2013) Enzymatic cleavage of lignin beta-O-4 aryl ether bonds via net internal hydrogen transfer. Green Chem 15, 1373-1381.
106. Tanamura K, Abe T, Kamimura N, Kasai D, Hishiyama S, Otsuka Y, Nakamura M, Kajita S, Katayama Y, Fukuda M, et al,. (2011) Characterization of the third glutathione S-transferase gene involved in enantioselective cleavage of the beta-aryl ether by Sphingobium sp. strain SYK-6. Biosci Biotechnol Biochem 75, 2404-2407.
107. Sonoki T, Masai E, Sato K, Kajita S, &, Katayama Y, (2009) Methoxyl groups of lignin are essential carbon donors in C1 metabolism of Sphingobium sp. SYK-6. J Basic Microbiol 49 (Suppl. 1), S98-S102.
108. Bugg TD, Ahmad M, Hardiman EM, &, Rahmanpour R, (2011) Pathways for degradation of lignin in bacteria and fungi. Nat Prod Rep 28, 1883-1896.
109. Masai E, Katayama Y, Nishikawa S, &, Fukuda M, (1999) Characterization of Sphingomonas paucimobilis SYK-6 genes involved in degradation of lignin-related compounds. J Ind Microbiol Biotechnol 23, 364-373.
110. Kasai D, Masai E, Miyauchi K, Katayama Y, &, Fukuda M, (2005) Characterization of the gallate dioxygenase gene: three distinct ring cleavage dioxygenases are involved in syringate degradation by Sphingomonas paucimobilis SYK-6. J Bacteriol 187, 5067-5074.
111. Masai E, Sasaki M, Minakawa Y, Abe T, Sonoki T, Miyauchi K, Katayama Y, &, Fukuda M, (2004) A novel tetrahydrofolate-dependent O-demethylase gene is essential for growth of Sphingomonas paucimobilis SYK-6 with syringate. J Bacteriol 186, 2757-2765.
112. Martinez AT, Speranza M, Ruiz-Duenas FJ, Ferreira P, Camarero S, Guillen F, Martinez MJ, Gutierrez A, &, del Rio JC, (2005) Biodegradation of lignocellulosics: microbial, chemical, and enzymatic aspects of the fungal attack of lignin. Int Microbiol 8, 195-204.
113. Guillen F, Martinez MJ, Munoz C, &, Martinez AT, (1997) Quinone redox cycling in the ligninolytic fungus Pleurotus eryngii leading to extracellular production of superoxide anion radical. Arch Biochem Biophys 339, 190-199.
114. Henriksson G, Ander P, Pettersson B, &, Pettersson G, (1995) Cellobiose dehydrogenase (Cellobiose oxidase) from Phanerochaete chrysosporium as a wood degrading enzyme-studies on cellulose, xylan and synthetic lignin. Appl Microbiol Biotechnol 42, 790-796.
115. Henriksson G, Johansson G, &, Pettersson G, (2000) A critical review of cellobiose dehydrogenases. J Biotechnol 78, 93-113.
116. Eltis LD, &, Bolin JT, (1996) Evolutionary relationships among extradiol dioxygenases. J Bacteriol 178, 5930-5937.
117. Williams PA, Assinder SJ, &, Shaw LE, (1990) Construction of hybrid xylE genes between the two duplicate homologous genes from TOL plasmid pWW53: comparison of the kinetic properties of the gene products. J Gen Microbiol 136, 1583-1589.
118. Junca H, Plumeier I, Hecht HJ, &, Pieper DH, (2004) Difference in kinetic behaviour of catechol 2,3-dioxygenase variants from a polluted environment. Microbiology 150, 4181-4187.
119. Carboni-Oerlemans C, Dominguez de Maria P, Tuin B, Bargeman G, van der Meer A, &, van Gemert R, (2006) Hydrolase-catalysed synthesis of peroxycarboxylic acids: biocatalytic promiscuity for practical applications. J Biotechnol 126, 140-151.
120. Duncan S, Jing Q, Katona A, Kazlauskas RJ, Schilling J, Tschirner U, &, Aldajani WW, (2010) Increased saccharification yields from aspen biomass upon treatment with enzymatically generated peracetic acid. Appl Biochem Biotechnol 160, 1637-1652.
121. Wiermans L, Perez-Sanchez M, &, Dominguez de Maria P, (2013) Lipase-mediated oxidative delignification in non-aqueous media: formation of de-aromatized lignin-oil and cellulase-accessible polysaccharides. ChemSusChem 6, 251-255.
122. Varnai A, Huikko L, Pere J, Siika-Aho M, &, Viikari L, (2011) Synergistic action of xylanase and mannanase improves the total hydrolysis of softwood. Biores Technol 102, 9096-9104.
123. Kudanga T, &, Le Roes-Hill M, (2014) Laccase applications in biofuels production: current status and future prospects. Appl Microbiol Biotechnol 98, 6525-6542.
124. Chen YR, Sarkanen S, &, Wang YY, (2012) Lignin-degrading enzyme activities. Methods Mol Biol 908, 251-268.
125. Wariishi H, Akileswaran L, &, Gold MH, (1988) Manganese peroxidase from the basidiomycete Phanerochaete chrysosporium: spectral characterization of the oxidized states and the catalytic cycle. Biochemistry 27, 5365-5370.
126. Solomon EI, Penfield KW, Gewirth AA, Lowery MD, Shadle SE, Guckert JA, &, LaCroix LB, (1996) Electronic structure of the oxidized and reduced blue copper sites: contributions to the electron transfer pathway, reduction potential, and geometry. Inorg Chim Acta 243, 67-78.
127. Kawai S, Nakagawa M, &, Ohashi H, (2002) Degradation mechanisms of a nonphenolic beta-O-4 lignin model dimer by Trametes versicolor laccase in the presence of 1-hydroxybenzotriazole. Enzy Microb Tech 30, 482-489.
128. Heinfling A, Ruiz-Duenas FJ, Martinez MJ, Bergbauer M, Szewzyk U, &, Martinez AT, (1998) A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta. FEBS Lett 428, 141-146.