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Front. Biol.    2014, Vol. 9 Issue (6) : 448-471    https://doi.org/10.1007/s11515-014-1336-9
REVIEW
Microbial enzyme systems for lignin degradation and their transcriptional regulation
Takanori FURUKAWA,Fatai Olumide BELLO,Louise HORSFALL()
School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3JR, UK
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Abstract

Lignocellulosic biomass is the most abundant renewable resource in nature and has received considerable attention as one of the most promising alternatives to oil resources for the provision of energy and certain raw materials. The phenolic polymer lignin is the second most abundant constituent of this biomass resource and has been shown to have the potential to be converted into industrially important aromatic chemicals after degradation. However, due to its chemical and structural nature, it exhibits high resistance toward mechanical, chemical, and biological degradation, and this causes a major obstacle for achieving efficient conversion of lignocellulosic biomass. In nature, lignin-degrading microorganisms have evolved unique extracellular enzyme systems to decompose lignin using radical mediated oxidative reactions. These microorganisms produce a set of different combinations of enzymes with multiple isozymes and isoforms by responding to various environmental stimuli such as nutrient availability, oxygen concentration and temperature, which are thought to enable effective decomposition of the lignin in lignocellulosic biomass. In this review, we present an overview of the microbial ligninolytic enzyme systems including general molecular aspects, structural features, and systematic differences in each microorganism. We also describe the gene expression pattern and the transcriptional regulation mechanisms of each ligninolytic enzyme with current data.
Keywords lignocellulose biorefinery      lignin degradation      lignin peroxidases      manganese peroxidases      versatile peroxidases      laccases     
Corresponding Author(s): Louise HORSFALL   
Just Accepted Date: 13 October 2014   Online First Date: 19 November 2014    Issue Date: 13 January 2015
 Cite this article:   
Takanori FURUKAWA,Fatai Olumide BELLO,Louise HORSFALL. Microbial enzyme systems for lignin degradation and their transcriptional regulation[J]. Front. Biol., 2014, 9(6): 448-471.
 URL:  
https://academic.hep.com.cn/fib/EN/10.1007/s11515-014-1336-9
https://academic.hep.com.cn/fib/EN/Y2014/V9/I6/448
Fig.1  Structural model of softwood lignin. Schematic representation of a structural model of softwood lignin proposed by Adler (Adler, 1977) (adapted from (Crestini et al., 2010)).
Fig.2  Chemical structure of the primary lignin monomers. Chemical structure of the three main monolignols p-coumaryl, coniferyl, and sinapyl alcohol is shown.
Fig.3  Common inter-unit linkages found in lignin polymer. Major structural units in the lignin polymer are shown (adapted from (Crestini et al., 2010).
Fig.4  Typical catalytic cycle of general heme peroxidases. The catalytic cycle of general heme peroxidases consist of three step reactions including two-electron oxidation of the resting ferric enzyme [Fe(III)] by hydroxyperoxide to yield Compound I oxo-ferryl intermediate [Fe(VI) = OP·+]. Compound I subsequently oxidizes electron donor substrates (AH) by one-electron oxidation forming Compound II [Fe(VI) = O] and a substrate cation radical (A·). Finally, Compound II oxidizes the substrate by subtracting one electron to return to the native resting state (Dunford 1999).
Fig.5  Three-dimensional structures of ligninolytic enzymes. 3D structures of the ligninolytic enzymes are shown. (A) A lignin peroxidase from P. chrysosporium; Protein Data Bank (PDB) ID: 1LGA (Poulos et al., 1993). (B) A manganese peroxidase from P. chrysosporium; 3M5Q (Sundaramoorthy et al., 2010). (C) A versatile peroxidase from P. erynjii; PDB ID: 3FM1 (Perez-Boada et al., 2005). (D) A laccase from T. versicolor; PDB ID: 1GYC (Piontek et al., 2002). (E) A Dye-decolorizing type peroxidase from R. jostii; PDB ID: 3QNR (Roberts et al., 2011).
Fig.6  Catalytic cycle of laccases. A schematic representation of the catalytic site and the catalytic cycle of laccases, showing the mechanism of reduction and oxidation of the enzyme copper sites. A substrate reduces the T1 site in the resting enzyme, which then transfers the electron to the trinuclear site resulting in a fully reduced state of the enzyme. Thereafter, reduction of one oxygen molecule occurs at the trinuclear center through the formation of oxygen-bound intermediates, peroxy-intermediates and native-intermediates, with two sequential electron transfer resulting in a formation of two molecules of water (Reproduced from (Wong, 2009))
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