This application relates to laccase variants and uses thereof as eco-friendly biocatalysts in various industrial processes. More in particular, the disclosure relates to a polypeptide with laccase activity comprising an amino acid sequence that is at least 75% identical to the amino acid sequence according to SEQ ID NO: 1, wherein the polypeptide comprises an amino acid residue selected from the group consisting of threonine, proline, alanine, glycine, serine, cysteine, aspartic acid, asparagine and valine at a position corresponding to amino acid 149 of SEQ ID NO: 1.

The present description is related to the field of protein production. It introduces novel host cells with low protease activity, a novel protease regulator, its use in expression systems and protein production, and a method of producing host cells for protein production

The invention relates to the field of degradation of fluor containing substances by bioconversion.

The present invention relates to a laccase enzyme product isolated from a Coriolopsis gallica fungal strain. The laccase enzyme product is characterized in that the laccase enzyme is a thermostable enzyme having a maximum activity at 72 C. and retains at least 50% activity relative to the maximum activity after 20 min incubation at a temperature of 80 C. The invention is also directed to a method for the production of a laccase enzyme product according to the invention, said method encompassing conducting submerged fermentation aerobically of a C. gallica fungal strain in a fermentation medium comprising at least 20 g/L of a carbon source selected from a monosaccharide, a disaccharide, an oligosaccharide, a polysaccharide or any combination thereof; a nitrogen source; and minerals, and to which an inducer of laccase production is added, in a tank bioreactor of at least 200 L that is kept in agitation at between 100 rpm and 220 rpm.

The present application is directed to lettuce plants comprising a mutation in each of at least two different PPO genes, where said mutations reduce the activity of PPO protein compared to a wild type lettuce plant. The present application is also directed to methods for making such lettuce plants.

In a first aspect, the present invention relates to an isolated aqueous enzymatic preparation obtained from the reaction of at least one oxidoreductase enzyme, preferably a laccase, and at least one natural or synthetic product, preferably a natural compound, said natural or synthetic product comprising, in the structure thereof, at least one phenol or alcohol group, which optionally has one or more hydrophobic chains, or at least one sterol group. In a second aspect, the present invention relates to the use of said isolated aqueous enzymatic preparation in the functionalization of the surface of paper or cellulosic substrates.

Provided herein are isolated laccase enzymes and nucleic acids encoding them. Also provided are mediators for laccase reactions. Also provided herein are methods for using laccases to oxidize lignins, other phenolic, and aromatic compounds, such as for bio-bleaching and decolorization of wood pulp under high temperature and pH conditions to facilitate a substantial reduction in use of bleaching chemicals, as well as for treatment of fibers.

The present application relates to laccase variants and uses thereof as eco-friendly biocatalysts in various industrial processes. More in particular, the application relates to a polypeptide with laccase activity comprising an amino acid sequence that is at least 60% identical to the amino acid sequence according to SEQ ID NO: 1, wherein the polypeptide comprises an alanine residue at a position corresponding to amino acid 260 of SEQ ID NO: 1.

The present invention relates to laccase variants having improved enzymatic properties in alkaline conditions and uses thereof as eco-friendly biocatalysts in various industrial processes.

The present disclosure generally relates to biological platforms for the conversion of cellulosic biomass into fuels and chemicals. More specifically, the present disclosure relates to the conversion of cellulosic materials into sugar acids or their salts, which may then be used to produce commodity chemicals. In one aspect, the present disclosure relates to a recombinant host cell including: reduced activity of one or more polypeptides having P-glucosidase activity as compared to a corresponding wild type cell, where each of said one or more polypeptides are encoded by a gene that has at least 80% sequence identity to a gene.