New approach of bioprocessing towards lignin biodegradation.

Liu, Y; Luo, G; Ngo, HH; Zhang, S

New approach of bioprocessing towards lignin biodegradation.

Liu, Y Luo, G Ngo, HH Zhang, S

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Publisher:: Elsevier BV
Publication Type:: Journal Article
Citation:: Bioresour Technol, 2022, 361, pp. 127730
Issue Date:: 2022-10

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Field	Value	Language
dc.contributor.author	Liu, Y
dc.contributor.author	Luo, G
dc.contributor.author	Ngo, HH
dc.contributor.author	Zhang, S
dc.date.accessioned	2023-01-19T04:12:52Z
dc.date.available	2022-07-29
dc.date.available	2023-01-19T04:12:52Z
dc.date.issued	2022-10
dc.identifier.citation	Bioresour Technol, 2022, 361, pp. 127730
dc.identifier.issn	0960-8524
dc.identifier.issn	1873-2976
dc.identifier.uri	http://hdl.handle.net/10453/165211
dc.description.abstract	Bio-utilization of lignocellulosic biomass is of huge significance as it can directly replace petroleum resources by producing liquid fuels and organic chemical products in a more sustainable way. However, studies on developing lignin-degrading microbial resources are still very few, which affects on establishing a consolidated bioprocessing of lignocellulosic resource. The main aim of this work is to discover thermostable laccases for lignin thermo-biodegradation by metagenome-mining and biochemical characterization. Results indicate that 124 putative thermostable laccase genes were identified from generated metagenomes. Significantly, 3 rationally selected proteins showed actual activity and structural stability at temperatures up to 60 °C and pH values as low as 4.87. These active recombinant enzymes verify a practical advance in the functional prediction of target proteins, and simultaneous sequence-to-function relationships in this metagenome. In short, the identified thermostable laccase genes in this work could expand range of lignin biocatalysts and contribute to build an efficient lignin biorefinery.
dc.format	Print-Electronic
dc.language	eng
dc.publisher	Elsevier BV
dc.relation.ispartof	Bioresour Technol
dc.relation.isbasedon	10.1016/j.biortech.2022.127730
dc.rights	info:eu-repo/semantics/closedAccess
dc.subject.classification	Biotechnology
dc.subject.mesh	Biodegradation, Environmental
dc.subject.mesh	Biomass
dc.subject.mesh	Laccase
dc.subject.mesh	Lignin
dc.subject.mesh	Metagenome
dc.subject.mesh	Lignin
dc.subject.mesh	Laccase
dc.subject.mesh	Biomass
dc.subject.mesh	Biodegradation, Environmental
dc.subject.mesh	Metagenome
dc.title	New approach of bioprocessing towards lignin biodegradation.
dc.type	Journal Article
utslib.citation.volume	361
utslib.location.activity	England
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Engineering and Information Technology
pubs.organisational-group	/University of Technology Sydney/Faculty of Engineering and Information Technology/School of Civil and Environmental Engineering
pubs.organisational-group	/University of Technology Sydney/Strength - CTWW - Centre for Technology in Water and Wastewater Treatment
utslib.copyright.status	closed_access	*
dc.date.updated	2023-01-19T04:12:50Z
pubs.publication-status	Published
pubs.volume	361

Abstract:

Bio-utilization of lignocellulosic biomass is of huge significance as it can directly replace petroleum resources by producing liquid fuels and organic chemical products in a more sustainable way. However, studies on developing lignin-degrading microbial resources are still very few, which affects on establishing a consolidated bioprocessing of lignocellulosic resource. The main aim of this work is to discover thermostable laccases for lignin thermo-biodegradation by metagenome-mining and biochemical characterization. Results indicate that 124 putative thermostable laccase genes were identified from generated metagenomes. Significantly, 3 rationally selected proteins showed actual activity and structural stability at temperatures up to 60 °C and pH values as low as 4.87. These active recombinant enzymes verify a practical advance in the functional prediction of target proteins, and simultaneous sequence-to-function relationships in this metagenome. In short, the identified thermostable laccase genes in this work could expand range of lignin biocatalysts and contribute to build an efficient lignin biorefinery.

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http://hdl.handle.net/10453/165211