A laccase with a molecular mass of 67 kDa and inhibitory activity toward HIV-1 reverse transcriptase (IC50 = 7.5 microM) was isolated from fresh fruiting bodies of the Lentinus edodes (Shiitake mushroom). Its characteristics were compared with those of laccases from cultured mushroom mycelia reported earlier. The laccase was unadsorbed on DEAE-cellulose, Affi-gel blue gel and CM-cellulose, but ...

Laccase from Coriolopsis Polyzona was insolubilized as cross-linked enzyme aggregates (CLEAs) for the first time with chitosan as the cross-linking agent. Concentrations between 0.01 and 1.867 g/L of chitosan were used and between 0.05 and 600 mM of 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride. The laccase was precipitated using ammonium sulphate and cross-linked simultaneously. ...

The effect of different substrates and various developmental stages (mycelium growth, primordium appearance, and fruiting-body formation) on laccase production in the edible mushroom Lentinula edodes was studied. The cap of the mature mushroom showed the highest laccase activity, and laccase activity was not stimulated by some well-known laccase inducers or sawdust. For our molecular studies, t...

The cultivation of Trametes versicolor for laccase production and cell growth were strongly dependent on experimental conditions namely physical and chemical parameters as well as nutrient availability and inducer stimulation. Biomass growth was compared for a rich medium and for a defined medium in two different temperatures. The best temperature was 28ºC and the maximum specific growth rates ...

A novel extracellular laccase enzyme produced from Spirulina platensis CFTRI was purified by ultrafiltration, cold acetone precipitation, anion exchange and size exclusion chromatography with 51.5% recovery and 5.8 purification fold. The purified laccase was a monomeric protein with molecular mass of ~66 kDa that was confirmed by zymogram analysis and peptide mass fingerprinting. The optimum pH...

Current understanding of the final oxidative steps leading to lignin deposition in trees and other higher plants is limited with respect to what enzymes are involved, where they are localized, how they are transported, and what factors regulate them. With the use of cell suspension cultures of sycamore maple (Acer pseudoplatanus), an in-depth study of laccase, one of the oxidative enzymes possi...

BACKGROUND The basidiomycete Pleurotus ostreatus is an efficient producer of laccases, a group of enzymes appreciated for their use in multiple industrial processes. The aim of this study was to reveal the molecular basis of the superiority of laccase production by dikaryotic strains compared to their parental monokaryons. METHODOLOGY/PRINCIPAL FINDINGS We bred and studied a set of dikaryotic...

An approach to describe continuous partitioning of Cerrena unicolor laccase in a PEG 6000-phosphate aqueous two-phase system was proposed. The laccase was separated from crude supernatant of C. unicolor-submerged culture, and all the experiments were carried out in 25 °C and pH 7 conditions. Masses of both phases and their compositions at phase equilibrium, as well as laccase activity concentra...

The strain Ganoderma cupreum AG-1 (Genbank accession no. HQ328947) isolated from the decayed wood was evaluated for its ability to decolorize azo dye reactive violet 1 as well as for the production of ligninolytic enzymes. In the initial decolorization study, the strain was capable of decolorizing 19 different azo dyes. The strain was capable of decolorizing dye over a pH range of 4.5-6 at 30 °...

Extracellular laccase was produced by Trametes versicolor IBL-04 using corn cobs as a substrate under pre-optimized culture conditions. A 64kDa laccase enzyme was purified and immobilized on calcium alginate beads using glutaraldehyde as a cross-linking reagent. Maximum enzyme immobilization efficiency (89%) was observed with 2-mm calcium-alginate beads that were developed using 4% (w/v) sodium...