Lignin is the second most abundant constituent of the cell wall of vascular plants, where it protects cellulose towards hydrolytic attack by saprophytic and pathogenic microbes. Its removal represents a key step for carbon recycling in land ecosystems, as well as a central issue for industrial utilization of plant biomass. The lignin polymer is highly recalcitrant towards chemical and biological degradation due to its molecular architecture, where different non‐phenolic phenylpropanoid units form a complex three‐dimensional network linked by a variety of ether and carbon–carbon bonds. Ligninolytic microbes have developed a unique strategy to handle lignin degradation based on unspecific one‐electron oxidation of the benzenic rings in the different lignin substructures by extracellular haemperoxidases acting synergistically with peroxide‐generating oxidases. These peroxidases posses two outstanding characteristics: (i) they have unusually high redox potential due to haem pocket architecture that enables oxidation of non‐phenolic aromatic rings, and (ii) they are able to generate a protein oxidizer by electron transfer to the haem cofactor forming a catalytic tryptophanyl‐free radical at the protein surface, where it can interact with the bulky lignin polymer. The structure–function information currently available is being used to build tailor‐made peroxidases and other oxidoreductases as industrial biocatalysts.
Microbial degradation of lignin: how a bulky recalcitrant polymer is efficiently recycled in nature and how we can take advantage of this
F. J. Ruiz-Dueñas,Angel T. Martı́nez
Published 2009 in Microbial Biotechnology
ABSTRACT
PUBLICATION RECORD
- Publication year
2009
- Venue
Microbial Biotechnology
- Publication date
2009-02-18
- Fields of study
Biology, Materials Science, Chemistry, Environmental Science, Medicine
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
CITATION MAP
EXTRACTION MAP
CLAIMS
- Ligninolytic peroxidases generate a catalytic tryptophanyl-free radical at the protein surface through electron transfer to the haem cofactor, enabling interaction with the bulky lignin polymer.All you need is Python (5d7gwfm5zu) extraction뀨 (7c402c1b98) reviewq (76h6bfydm6) reviewmexicorea (qjvnbu8xg3) review
- Lignin degradation by ligninolytic microbes relies on unspecific one-electron oxidation of benzenic rings by extracellular haemperoxidases acting synergistically with peroxide-generating oxidases.All you need is Python (5d7gwfm5zu) extraction뀨 (7c402c1b98) reviewq (76h6bfydm6) reviewmexicorea (qjvnbu8xg3) review
CONCEPTS
- extracellular haemperoxidases
Peroxidases secreted by ligninolytic microbes that catalyze unspecific one-electron oxidation of benzenic rings in lignin substructures via a haem cofactor.
Aliases: haemperoxidases, peroxidases
All you need is Python (5d7gwfm5zu) extraction뀨 (7c402c1b98) reviewq (76h6bfydm6) reviewmexicorea (qjvnbu8xg3) review - lignin
A highly recalcitrant non-phenolic phenylpropanoid polymer forming a complex three-dimensional network in plant cell walls, linked by ether and carbon–carbon bonds.
Aliases: lignin polymer
All you need is Python (5d7gwfm5zu) extraction뀨 (7c402c1b98) reviewq (76h6bfydm6) reviewmexicorea (qjvnbu8xg3) review - lignin degradation
The biological breakdown of lignin by ligninolytic microbes via extracellular oxidative enzyme systems.
All you need is Python (5d7gwfm5zu) extraction뀨 (7c402c1b98) reviewq (76h6bfydm6) reviewmexicorea (qjvnbu8xg3) review - ligninolytic microbes
Microorganisms that have developed a unique enzymatic strategy for degrading lignin based on extracellular oxidative enzymes.
All you need is Python (5d7gwfm5zu) extraction뀨 (7c402c1b98) reviewq (76h6bfydm6) reviewmexicorea (qjvnbu8xg3) review - peroxide-generating oxidases
Oxidases that produce peroxide and act synergistically with haemperoxidases during lignin degradation.
All you need is Python (5d7gwfm5zu) extraction뀨 (7c402c1b98) reviewq (76h6bfydm6) reviewmexicorea (qjvnbu8xg3) review - redox potential
The oxidation-reduction potential of ligninolytic peroxidases, which is unusually high due to haem pocket architecture.
All you need is Python (5d7gwfm5zu) extraction뀨 (7c402c1b98) reviewq (76h6bfydm6) reviewmexicorea (qjvnbu8xg3) review - tryptophanyl-free radical
A catalytic radical formed at the surface of ligninolytic peroxidases through electron transfer to the haem cofactor, serving as a protein oxidizer that can interact with bulky lignin.
All you need is Python (5d7gwfm5zu) extraction뀨 (7c402c1b98) reviewq (76h6bfydm6) reviewmexicorea (qjvnbu8xg3) review