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species Nonomuraea gerenzanensis growing on alkali lignin. Biotechnol Rep 13:49–57.
https://doi.org/10.1016/j.btre.2016.12.005
139. Chen Y-r, Sarkanen S, Wang Y-Y (2012) Lignin-degrading enzyme activities. In:
Himmel ME (ed) Biomass conversion. Humana Press, Totowa, pp 251–268. https://doi.
org/10.1007/978-1-61779-956-3_21
140. Kosa M, Ragauskas AJ (2012) Bioconversion of lignin model compounds with oleaginous
Rhodococci. Appl Microbiol Biotechnol 93(2):891–900. https://doi.org/10.1007/s00253011-3743-z
141. Lupoi JS, Singh S, Parthasarathi R et al (2015) Recent innovations in analytical methods for
the qualitative and quantitative assessment of lignin. Renew Sustain Energy Rev 49:871–
906. https://doi.org/10.1016/j.rser.2015.04.091
142. Morreel K, Dima O, Kim H et al (2010) Mass spectrometry-based sequencing of lignin
oligomers. Plant Physiol 153(4):1464–1478. https://doi.org/10.1104/pp.110.156489
143. Prothmann J, Spégel P, Sandahl M et al (2018) Identification of lignin oligomers in Kraft
lignin using ultra-high-performance liquid chromatography/high-resolution multiple-stage
tandem mass spectrometry (UHPLC/HRMSn). Anal Bioanal Chem 410(29):7803–7814.
https://doi.org/10.1007/s00216-018-1400-4
144. Reale S, Di Tullio A, Spreti N et al (2004) Mass spectrometry in the biosynthetic and
structural investigation of lignins. Mass Spectrom Rev 23(2):87–126. https://doi.org/10.
1002/mas.10072
145. Saito Y, Tsuchida H, Matsumoto T et al (2018) Screening of fungi for decomposition of
lignin-derived products from Japanese cedar. J Biosci Bioeng 126(5):573–579. https://doi.
org/10.1016/j.jbiosc.2018.05.001
146. Soden DM, O’Callaghan J, Dobson ADW (2002) Molecular cloning of a laccase isozyme
gene from Pleurotus sajor-caju and expression in the heterologous Pichia pastoris host.
Microbiology 148(12):4003–4014. https://doi.org/10.1099/00221287-148-12-4003
147. Tekere M, Mswaka AY, Zvauya R et al (2001) Growth, dye degradation and ligninolytic
activity studies on Zimbabwean white rot fungi. Enzyme Microb Technol 28(4):420–426.
https://doi.org/10.1016/S0141-0229(00)00343-4
148. Levasseur A, Drula E, Lombard V et al (2013) Expansion of the enzymatic repertoire of the
CAZy database to integrate auxiliary redox enzymes. Biotechnol Biofuels 6(1):41. https://
doi.org/10.1186/1754-6834-6-41
149. Lewin A, Lale R, Wentzel A (2017) Expression platforms for functional metagenomics:
emerging technology options beyond Escherichia coli. In: Charles TC, Liles MR,
Sessitsch A (eds) Functional metagenomics: tools and applications. Springer International
Publishing, Cham, pp 13–44. https://doi.org/10.1007/978-3-319-61510-3_2
150. López-Mondéjar R, Algora C, Baldrian P (2019) Lignocellulolytic systems of soil bacteria: a
vast and diverse toolbox for biotechnological conversion processes. Biotechnol Adv 37
(6):107374. https://doi.org/10.1016/j.biotechadv.2019.03.013
151. Kumar A, Anushree KJ et al (2020) Utilization of lignin: a sustainable and eco-friendly
approach. J Energy Inst 93(1):235–271. https://doi.org/10.1016/j.joei.2019.03.005
152. Zeng J, Mills MJL, Simmons BA et al (2017) Understanding factors controlling
depolymerization and polymerization in catalytic degradation of b-ether linked model
lignin compounds by versatile peroxidase. Green Chem 19(9):2145–2154. https://doi.org/10.
1039/C6GC03379B
153. Okuda K, Umetsu M, Takami S et al (2004) Disassembly of lignin and chemical recovery—
rapid depolymerization of lignin without char formation in water–phenol mixtures. Fuel
Process Technol 85(8):803–813. https://doi.org/10.1016/j.fuproc.2003.11.027
154. Shuai L, Amiri MT, Questell-Santiago YM et al (2016) Formaldehyde stabilization
facilitates lignin monomer production during biomass depolymerization. Science 354
(6310):329–333. https://doi.org/10.1126/science.aaf7810
470
G.-S. Nguyen et al.