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Literature summary extracted from

  • Stanzione, I.; Pezzella, C.; Giardina, P.; Sannia, G.; Piscitelli, A.
    Beyond natural laccases extension of their potential applications by protein engineering (2020), Appl. Microbiol. Biotechnol., 104, 915-924 .
    View publication on PubMed

Application

EC Number Application Comment Organism
1.10.3.2 degradation bisphenol A degradation Trametes versicolor
1.10.3.2 degradation decolorization of industrial dyes. Evans blue decolorization and detoxification Bacillus pumilus
1.10.3.2 degradation degradation of endocrine disrupting compounds Pleurotus ostreatus
1.10.3.2 degradation deinking of old newspaper, indigo carmine decolorization Rheinheimera sp.
1.10.3.2 energy production a CotA mutant from Bacillus licheniformis, operating in basic media and seawater, is effective in catalyzing the bioelectrocatalytic O2 reduction, suggesting a prospective enzyme application for sustainable production of energy from seawater and oxygen Bacillus licheniformis
1.10.3.2 environmental protection decolorization of industrial dyes with different chemical structures and decolorization of industrial wastewaters Pleurotus ostreatus
1.10.3.2 environmental protection decolorization of industrial dyes. Evans blue decolorization and detoxification Bacillus pumilus
1.10.3.2 environmental protection deinking of old newspaper, indigo carmine decolorization Rheinheimera sp.
1.10.3.2 synthesis synthesis of the C-N polydye at basic pHs Thermothelomyces thermophilus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.10.3.2 expression of laccase Lcc4/1 (composed of the N-terminus of the Lcc4 and the C-terminus of the Lcc1 laccases) in tobacco cell culture Lentinula edodes

Protein Variants

EC Number Protein Variants Comment Organism
1.10.3.2 additional information an alkaline laccase mutant form is chosen and further evolved for the synthesis of the C-N polydye at basic pHs. Over 11500 clones derived form 3 rounds of directed and focused evolution are screened through a high-throughput colorimetric assay, and a variant with 3.5-fold improved activity relative to that of the wild type is selected Thermothelomyces thermophilus
1.10.3.2 additional information laccase Lcc4/1, composed of the N-terminus of the Lcc4 and the C-terminus of the Lcc1 laccases Lentinula edodes
1.10.3.2 additional information laccase Lcc4/1, composed of the N-terminus of the Lcc4 and the C-terminus of the Lcc1 laccases. The fusion enzyme is more efficient, compared to Lcc1, in decolorizing RBBR and poly-R478, even if the latter is only in the presence of a redox mediator Lentinula edodes

Organism

EC Number Organism UniProt Comment Textmining
1.10.3.2 Bacillus licheniformis
-
-
-
1.10.3.2 Bacillus pumilus
-
-
-
1.10.3.2 Lentinula edodes
-
-
-
1.10.3.2 Lentinula edodes C5NN27
-
-
1.10.3.2 Pleurotus ostreatus O60199
-
-
1.10.3.2 Rheinheimera sp.
-
-
-
1.10.3.2 Thermothelomyces thermophilus
-
-
-
1.10.3.2 Trametes versicolor
-
-
-

Synonyms

EC Number Synonyms Comment Organism
1.10.3.2 CotA
-
 Bacillus licheniformis
1.10.3.2 CotA
-
 Bacillus pumilus
1.10.3.2 CotA
-
 Rheinheimera sp.
1.10.3.2 lcc1
-
 Lentinula edodes
1.10.3.2 Lcc4
-
 Lentinula edodes
1.10.3.2 POXA1b
-
 Pleurotus ostreatus