The invention relates to a polypeptide for the hydrolytic cleavage of zearalenone and/or at least one zearalenone derivative, said polypeptide being a hydrolase having an amino acid sequence selected from the group consisting of SEQ ID NO: 1-15 or a functional variant thereof, wherein the sequence of the functional variant is at least 40% identical to at least one of the amino acid sequences. The invention also relates to: an additive containing the polypeptide; an isolated polynucleotide that encodes the polypeptide; and a method for the hydrolytic cleavage of zearalenone and/or of at least one zearalenone derivative using the polypeptide.

The present invention relates to novel esterase, more particularly to esterase variants having improved thermostability compared to the esterase of SEQ ID No 1 and the uses thereof for degrading polyester containing material, such as plastic products. The esterases of the invention are particularly suited to degrade polyethylene terephthalate, and material containing polyethylene terephthalate.

The present disclosure provides compositions and methods of modulating abhydrolase domain-containing protein-2 (ABHD2). The present disclosure provides methods of identifying agents that modulate ABHD2 activity.

The invention concerns a compound characterised by a mono(2-hydroxyethyl) terephthalic acid (MHET) and bis(2-hydroxyethyl) terephthalic acid chemically bonded to a saccharide. Furthermore, the invention concerns a corresponding compound which is used as a synthesis component for polymers or fine chemicals.

The present invention relates to a variant of a parent lipase, which parent lipase has the amino acid sequence of SEQ ID NO: 2, wherein the variant has lipase activity, comprises a substitution at a position corresponding to position 51 and comprises a substitution or remains unaltered at a position corresponding to position 96 of SEQ ID NO: 2. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants.

The present invention relates to a polypeptide having lipolytic enzyme activity, selected from the group consisting of: (a) a polypeptide having at least 65% sequence identity to amino acids 21 to 309 of SEQ ID NO: 1; (b) a polypeptide encoded by a polynucleotide that hybridizes under medium stringency conditions with the polypeptide coding sequence of SEQ ID NO: 2; (c) a polypeptide encoded by a polynucleotide having at least 65% sequence identity to the polypeptide coding sequence of SEQ ID NO: 2; and (d) a fragment of the polypeptide of (a), (b) or (c) that has lipolytic enzyme activity.

Provided is a humanized monoclonal antibody or an antibody fragment thereof that selectively inhibits the enzymatic activity of vascular endothelial lipase and pharmaceutical compositions containing the same as an active ingredient useful for the treatment of arteriosclerosis or metabolic syndrome.

The present invention relates to novel esterase, more particularly to esterase variants having improved thermostability compared to the esterase of SEQ ID No 1 and the uses thereof for degrading polyester containing material, such as plastic products. The esterases of the invention are particularly suited to degrade polyethylene terephthalate, and material containing polyethylene terephthalate.

A method of preparing a wort with an increased level of free amino nitrogen (FAN) comprising: a) preparing a mash from a grist comprising malt and/or adjunct; and b) adding a protease having at least 80% sequence identity to the polypeptide of SEQ ID NO: 1.

The present invention relates to a method for solubilisation or hydrolysis of Municipal Solid Waste (MSW) with an enzyme blend and an enzyme composition for solubilization of Municipal Solid Waste (MSW), the enzyme composition comprising a cellulolytic background composition and a protease, lipase and/or beta-glucanase.