The pH stability of the free laccase and the immobilized laccase was determined by incubating the enzyme in different buffers (pH 3.0-8.0) for 6 h at 35 °C. The buffers used were Na2HPO4–sodium citrate buffer (pH 3.0-8.0). The immobilized laccase was collected by centrifugation (3500 g for 3 min) and air-dried. The residual specific activities of free or immobilized laccase were then determined...

In order to obtain a more stable and reusable immobilized spore laccase for dye decolorization, the spores from Bacillus pumilus W3 were immobilized on diethylaminoethyl cellulose (DEAE-cellulose). Free and immobilized spore laccase retained 34.38% and 46.11% of their initial activity, respectively, after 10 days incubation at pH 9.0. Their residual activity remained at 27.36% and 31.84% after ...

A white-rot basidiomycete, Phlebia tremellosa, produced a laccase that showed increased activity during degradation of phthalates. A laccase was purified through the ion exchange chromatography and preparative gel electrophoresis, and the estimated molecular weight was 75 kDa. The optimum pH and temperature of the purified laccase was pH 4.0 and 20 degrees C, respectively. The K(m) value of the...

The activity and composition of leafhopper saliva are important in interactions with the host rice plant, and it may play a physiological role in detoxifying toxic plant substances or ingesting sap. We have characterized diphenoloxidase in the salivary glands of Nephotettix cincticeps, its activity as a laccase, and its presence in the watery saliva with the objective of understanding its funct...

The biosynthetic utilization of laccase/mediator system is problematic because the use of organic cosolvent causes significant inhibition of laccase activity. This work explored how the organic cosolvent impacts on the laccase catalytic capacity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) in aqueous solution. Effects of acetone on the kinetic constants of laccase were ...

Laccase activity and stability were improved and modified through the interaction between laccase amino acid residues (e.g., amino groups (NH2) and carboxyl groups (-COOH)) and the chemical reagents thiourea dioxide (TDO) and L-phenylalanine methyl ester hydrochloride (L-PME). Compared with the control sample, the activity of the laccase modified with these chemical reagents was increased by 20...

Fungus-growing termites efficiently decompose plant litter through their symbiotic relationship with basidiomycete fungi of the genus Termitomyces. Here, we investigated phenol-oxidizing enzymes in symbiotic fungi and fungus combs (a substrate used to cultivate symbiotic fungi) from termites belonging to the genera Macrotermes, Odontotermes, and Microtermes in Thailand, because these enzymes ar...

Background: Phenolic compounds, which are produced routinely by industrial and urban activities, possess dangers to live organisms and environment. Laccases are oxidoreductase enzymes with the ability of remediating a wide variety of phenolic compounds to more benign molecules. The purpose of the present research is surface display of a laccase enzyme with adhesin involved in diffuse adhesion (...

Laccases can oxidize a wide range of aromatic compounds and are industrially valuable. Laccases often exist in gene families and may differ from each other in expression and function. Quantitative real-time polymerase chain reaction (qPCR) was used for transcription profiling of eight laccase genes in Cerrena sp. strain HYB07 with validated reference genes. A high laccase activity of 280.0 U/mL...

An efficient transformation and expression system was developed for the industrially relevant basidiomycete Pycnoporus cinnabarinus. This was used to transform a laccase-deficient monokaryotic strain with the homologous lac1 laccase gene placed under the regulation of its own promoter or that of the SC3 hydrophobin gene or the glyceraldehyde-3-phosphate dehydrogenase (GPD) gene of Schizophyllum...