summarizes key microbial clades and species described to date as a source of
ligninolytic enzymes.
Efforts in categorizing and organizing information on enzymes involved in
microbial lignin degradation has led to the establishment of several databases.
Notable examples are: (i) eLignin Microbial Database [22], focusing on intracellular
conversions; (ii) Laccase and Multicopper Oxidase Engineering Database (LccED)
[31] focusing mainly on multicopper oxidases and (iii) RedoxiBase [32] containing
comprehensive databases of different peroxidase and other oxidoreductase classes
such as superoxide dismutases, blue copper proteins, glutathione reductases, etc.
Recently, lignin-degrading enzymes are being discovered at an increasing rate,
thanks to the growing number of published genomes and metagenomes, the rapid
advancements in bioinformatics, and the availability of low-cost computing power.
For relevant approaches deployed in new enzyme discovery it is referred to Sect. 3.
The next sub-sections cover the main enzyme classes found to be active on lignin
and involved in its depolymerization. For an overview, see Fig. 2.
Table 1 (continued)
Organism
Enzymes
Bacteria
Firmicutes
Bacillus atrophaeus
Lac [112, 113]
Bacillus
amyloliquefaciens
Lac [114]
Bacillus licheniformis
Lac [115]
Bacillus pumilus
Lac [116]
Bacillus subtilis
Lac [117, 118]
Geobacillus sp.
Lac [119]
Actinobacteria
Amycolatopsis sp.
DyP [112]
Rhodococcus jostii
DyP [120]
Steptomyces coelicolor
DyP, Lac [58]
Thermobifida fusca
DyP [50]
Steptomyces griseus
Lac [121]
Steptomyces ipomoea
Lac [122]
Steptomyces lavendulae
Lac [123]
a-proteobacteria
Azospirillum lipoferum
Lac [124, 125]
Novosphingobium spp.
Eth [73]
Sinorhizobium meliloti
Lac [126]
Sphingomonas
paucimobilis
Eth [127, 128]
c-proteobacteria
Escherichia coli
DyP, Lac [129, 130]
Pseudomonas spp.
MnP, Dyp, Lac [131–133]
Deinococcus-Thermus
Thermus thermophilus
Lac [134]
Archaea
Euryarchaeota
Haloferax volcanii
Lac [135]
Pyrobaculum
aerophilum
Lac [136]
Recent Advances in Enzymatic Conversion of Lignin …
447
ligninolytic enzymes.
Efforts in categorizing and organizing information on enzymes involved in
microbial lignin degradation has led to the establishment of several databases.
Notable examples are: (i) eLignin Microbial Database [22], focusing on intracellular
conversions; (ii) Laccase and Multicopper Oxidase Engineering Database (LccED)
[31] focusing mainly on multicopper oxidases and (iii) RedoxiBase [32] containing
comprehensive databases of different peroxidase and other oxidoreductase classes
such as superoxide dismutases, blue copper proteins, glutathione reductases, etc.
Recently, lignin-degrading enzymes are being discovered at an increasing rate,
thanks to the growing number of published genomes and metagenomes, the rapid
advancements in bioinformatics, and the availability of low-cost computing power.
For relevant approaches deployed in new enzyme discovery it is referred to Sect. 3.
The next sub-sections cover the main enzyme classes found to be active on lignin
and involved in its depolymerization. For an overview, see Fig. 2.
Table 1 (continued)
Organism
Enzymes
Bacteria
Firmicutes
Bacillus atrophaeus
Lac [112, 113]
Bacillus
amyloliquefaciens
Lac [114]
Bacillus licheniformis
Lac [115]
Bacillus pumilus
Lac [116]
Bacillus subtilis
Lac [117, 118]
Geobacillus sp.
Lac [119]
Actinobacteria
Amycolatopsis sp.
DyP [112]
Rhodococcus jostii
DyP [120]
Steptomyces coelicolor
DyP, Lac [58]
Thermobifida fusca
DyP [50]
Steptomyces griseus
Lac [121]
Steptomyces ipomoea
Lac [122]
Steptomyces lavendulae
Lac [123]
a-proteobacteria
Azospirillum lipoferum
Lac [124, 125]
Novosphingobium spp.
Eth [73]
Sinorhizobium meliloti
Lac [126]
Sphingomonas
paucimobilis
Eth [127, 128]
c-proteobacteria
Escherichia coli
DyP, Lac [129, 130]
Pseudomonas spp.
MnP, Dyp, Lac [131–133]
Deinococcus-Thermus
Thermus thermophilus
Lac [134]
Archaea
Euryarchaeota
Haloferax volcanii
Lac [135]
Pyrobaculum
aerophilum
Lac [136]
Recent Advances in Enzymatic Conversion of Lignin …
447