Application | Comment | Organism |
---|---|---|
degradation | bisphenol A degradation | Trametes versicolor |
degradation | decolorization of industrial dyes. Evans blue decolorization and detoxification | Bacillus pumilus |
degradation | degradation of endocrine disrupting compounds | Pleurotus ostreatus |
degradation | deinking of old newspaper, indigo carmine decolorization | Rheinheimera sp. |
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 |
environmental protection | decolorization of industrial dyes with different chemical structures and decolorization of industrial wastewaters | Pleurotus ostreatus |
environmental protection | decolorization of industrial dyes. Evans blue decolorization and detoxification | Bacillus pumilus |
environmental protection | deinking of old newspaper, indigo carmine decolorization | Rheinheimera sp. |
synthesis | synthesis of the C-N polydye at basic pHs | Thermothelomyces thermophilus |
Cloned (Comment) | Organism |
---|---|
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 | Comment | Organism |
---|---|---|
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 |
additional information | laccase Lcc4/1, composed of the N-terminus of the Lcc4 and the C-terminus of the Lcc1 laccases | Lentinula edodes |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus licheniformis | - |
- |
- |
Bacillus pumilus | - |
- |
- |
Lentinula edodes | - |
- |
- |
Lentinula edodes | C5NN27 | - |
- |
Pleurotus ostreatus | O60199 | - |
- |
Rheinheimera sp. | - |
- |
- |
Thermothelomyces thermophilus | - |
- |
- |
Trametes versicolor | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
CotA | - |
Bacillus licheniformis |
CotA | - |
Bacillus pumilus |
CotA | - |
Rheinheimera sp. |
lcc1 | - |
Lentinula edodes |
Lcc4 | - |
Lentinula edodes |
POXA1b | - |
Pleurotus ostreatus |