Review of advances in the development of laccases for the valorization of lignin to enable the production of lignocellulosic biofuels and bioproducts.

Biofuels Biorefining Enzymatic depolymerization Laccase Lignin degrading enzymes Lignin valorization

Journal

Biotechnology advances
ISSN: 1873-1899
Titre abrégé: Biotechnol Adv
Pays: England
ID NLM: 8403708

Informations de publication

Date de publication:
Historique:
received: 25 05 2021
revised: 23 07 2021
accepted: 24 07 2021
pubmed: 2 8 2021
medline: 22 3 2022
entrez: 1 8 2021
Statut: ppublish

Résumé

Development and deployment of commercial biorefineries based on conversion of lignocellulosic biomass into biofuels and bioproducts faces many challenges that must be addressed before they are commercially viable. One of the biggest challenges faced is the efficient and scalable valorization of lignin, one of the three major components of the plant cell wall. Lignin is the most abundant aromatic biopolymer on earth, and its presence hinders the extraction of cellulose and hemicellulose that is essential to biochemical conversion of lignocellulose to fuels and chemicals. There has been a significant amount of work over the past 20 years that has sought to develop innovative processes designed to extract and recycle lignin into valuable compounds and help reduce the overall costs of the biorefinery process. Due to the complex matrix of lignin, which is essential for plant survival, the development of a reliable and efficient lignin conversion technology has been difficult to achieve. One approach that has received significant interest relies on the use of enzymes, notably laccases, a class of multi‑copper green oxidative enzymes that catalyze bond breaking in lignin to produce smaller oligomers. In this review, we first assess the different innovations of lignin valorization using laccases within the context of a biorefinery process, and then assess the latest economical advances that these innovations offered. Finally, we review laccase characterization and optimization, as well as the prospects and bottlenecks of this class of enzymes within the industrial and biorefining sectors.

Identifiants

pubmed: 34333091
pii: S0734-9750(21)00115-4
doi: 10.1016/j.biotechadv.2021.107809
pii:
doi:

Substances chimiques

Biofuels 0
lignocellulose 11132-73-3
Lignin 9005-53-2
Laccase EC 1.10.3.2

Types de publication

Journal Article Research Support, U.S. Gov't, Non-P.H.S. Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

107809

Informations de copyright

Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.

Auteurs

Laure M C Leynaud Kieffer Curran (LMC)

Swiss Federal Institute of Technology Lausanne, Lausanne, Vaud, Switzerland; Joint Bioenergy Institute, Emeryville, CA, United States of America; Biological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, United States of America.

Le Thanh Mai Pham (LTM)

Joint Bioenergy Institute, Emeryville, CA, United States of America; Sandia National Laboratories, Livermore, CA, United States of America.

Kenneth L Sale (KL)

Joint Bioenergy Institute, Emeryville, CA, United States of America; Sandia National Laboratories, Livermore, CA, United States of America.

Blake A Simmons (BA)

Joint Bioenergy Institute, Emeryville, CA, United States of America; Biological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, United States of America. Electronic address: basimmons@lbl.gov.

Articles similaires

India Carbon Sequestration Environmental Monitoring Carbon Biomass
Biomass Lignin Wood Populus Microscopy, Electron, Scanning
Citrus Phenylalanine Ammonia-Lyase Stress, Physiological Multigene Family Phylogeny
1.00
Wildfires Humans Australia Forests Indigenous Peoples

Classifications MeSH