Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.10.3.2 (laccase)
 4,656 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Laccase production by pre-growth pellets of Trametes versicolor using two types of textile dyes as inducers was studied. By decoupling the enzyme production phase from the growth phase, it is possible to reduce the time and nutrients required for laccase production. At the glucose maintenance level, the effect of the nitrogen source and textile dye was analysed using response surface methodology. Ammonium chloride was used as the inorganic nitrogen source. Two types of dyes were tested: Grey Lanaset G (GLG), a metal complex dye mixture containing nitrogen; and Alizarin Red (AR), an anthraquinonic dye with no nitrogen in its chemical structure. GLG induces laccase production at a higher extent than AR. Despite the limiting conditions required for the production of laccase, enzyme production increases with increasing ammonium chloride. When AR, the N-free dye, was used as an inducer, the optimal supply of N for laccase production was 1.2 mg/(g dry cell weight x d) as ammonium chloride. The reuse of fungal pellets in the repeated-batch mode under maintenance conditions was found to be a good strategy for improving laccase production, as enzyme production increased to up to seven times the production of the first cycle. It was demonstrated that GLG can be used as an inducer and as an N source and, thus, it is possible to decolorize the dye and to induce laccase production at the same time without adding an extra N source.
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PMID:Laccase production by Trametes versicolor under limited-growth conditions using dyes as inducers. 2353 Mar 21

A cDNA encoding for a laccase was isolated from the white-rot fungus Lenzites gibbosa by RT-PCR and expressed in the Pichia pastoris. The laccase native signal peptide efficiently directed the secretion of the recombinant laccase in an active form. Factors influencing laccase expression, such as pH, cultivation temperature, copper concentration and methanol concentration, were optimized. The recombinant enzyme was purified to electrophoretic homogeneity, and was estimated to have a MW of ~61.5 kDa. The purified enzyme behaved similarly to the native laccase produced by L. gibbosa and efficiently decolorized Alizarin Red, Neutral Red, Congo Red and Crystal Violet, without the addition of redox mediators. The decolorization capacity of this recombinant enzyme suggests that it could be a useful biocatalyst for the treatment of dye-containing effluents. This study is the first report on the synthetic dye decolorization by a recombinant L. gibbosa laccase.
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PMID:Decolorization of Alizarin Red and other synthetic dyes by a recombinant laccase from Pichia pastoris. 2407 22