Literature summary for 1.10.3.2 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 .

Search for more literature for 1.10.3.2

Application

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(Commentary)

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

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

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

Synonyms

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)