Enzymatic Functionalization of Wood as an Antifouling Strategy against the Marine Bacterium .

The protection of wood in marine environments is a major challenge due to the high sensitivity of wood to both water and marine microorganisms. Besides, the environmental regulations are pushing the industry to develop novel effective and environmentally friendly treatments to protect wood in marine environments. The present study focused on the development of a new green methodology based on the laccase-assisted grafting of lauryl gallate (LG) onto wood to improve its marine antifouling properties.

Kinetic and thermodynamic study of laccase cross-linked onto glyoxyl Immobead 150P carrier: Characterization and application for beechwood biografting.

In this study, we cross-linked aminated Thermothelomyces thermophilus laccase onto Immobead 150P epoxy carrier, and achieved an immobilization yield of 99.84 %. The optimum temperature and pH values for the oxidation of ABTS by laccase were determined to be 70 °C and pH 3.

Green Binder Based on Enzymatically Polymerized Eucalypt Kraft Lignin for Fiberboard Manufacturing: A Preliminary Study.

The capability of laccase from to drive oxidative polymerization of Kraft lignin (KL) was studied as a previous step before applying this biotechnological approach for the manufacturing of medium-density fiberboards (MDF) at a pilot scale. This method, which improves the self-bonding capacity of wood fibers by lignin enzymatic cross-linking, mimics the natural process of lignification in living plants and trees. An interesting pathway to promote these interactions could be the addition of lignin to the system.

3D Printable Filaments Made of Biobased Polyethylene Biocomposites.

Two different series of biobased polyethylene (BioPE) were used for the manufacturing of biocomposites, complemented with thermomechanical pulp (TMP) fibers. The intrinsic hydrophilic character of the TMP fibers was previously modified by grafting hydrophobic compounds (octyl gallate and lauryl gallate) by means of an enzymatic-assisted treatment. BioPE with low melt flow index (MFI) yielded filaments with low void fraction and relatively low thickness variation.

Stability and kinetic behavior of immobilized laccase from Myceliophthora thermophila in the presence of the ionic liquid 1-ethyl-3-methylimidazolium ethylsulfate.

The use of ionic liquids (ILs) as reaction media for enzymatic reactions has increased their potential because they can improve enzyme activity and stability. Kinetic and stability properties of immobilized commercial laccase from Myceliophthora thermophila in the water-soluble IL 1-ethyl-3-methylimidazolium ethylsulfate ([emim][EtSO4 ]) have been studied and compared with free laccase. Laccase immobilization was carried out by covalent binding on glyoxyl-agarose beads.

Immobilization of laccase on modified silica: stabilization, thermal inactivation and kinetic behaviour in 1-ethyl-3-methylimidazolium ethylsulfate ionic liquid.

Laccase was immobilized on modified silica carrier. The immobilization conditions, pH and enzyme concentration were optimized. Operational stability of 10 reaction cycles showed that immobilized laccase in buffer was stable, presenting an activity loss <30%.

Role of laccase and low molecular weight metabolites from Trametes versicolor in dye decolorization.

The studies regarding decolorization of dyes by laccase may not only inform about the possible application of this enzyme for environmental purposes, but also may provide important information about its reaction mechanism and the influence of several factors that could be involved. In this paper, decolorization of crystal violet and phenol red was carried out with different fractions of extracellular liquids from Trametes versicolor cultures, in order to describe the role of laccase in this reaction. Moreover, the possible role of the low molecular weight metabolites (LMWMs) also produced by the fungus was evaluated.

Recent developments and applications of immobilized laccase.

Laccase is a promising biocatalyst with many possible applications, including bioremediation, chemical synthesis, biobleaching of paper pulp, biosensing, textile finishing and wine stabilization. The immobilization of enzymes offers several improvements for enzyme applications because the storage and operational stabilities are frequently enhanced. Moreover, the reusability of immobilized enzymes represents a great advantage compared with free enzymes.

Effect of heavy metals on the production of several laccase isoenzymes by Trametes versicolor and on their ability to decolourise dyes.

The white-rot fungus Trametes versicolor growing in submerged culture on a basal medium, with barley bran as a carbon source, produced two laccase isoenzymes LacI and LacII. The addition of metal ions to the culture medium was performed to improve the total laccase activity and to determine the effect on the production of laccase isoenzymes. From all the tested metals, only Cu2+ increased laccase activity (up to 12-fold with respect to control cultures) and T.