The present invention relates to esterases, more particularly to esterase variants having improved activity and/or 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 invention relates to novel esterases, more particularly to esterase variants having improved activity and/or 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 invention relates to esterases, more particularly to esterase variants having improved activity and/or improved themostability 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 depolymerizing a polymer by combining together the polymer with an enzyme (a hydrolytic enzyme capable of catalyzing cleavage of said (CO)—O bond of an ester or carbonate linkage of the polymer) and an aqueous liquid to provide a reaction mixture. The polymer comprises a (CO)—O bond of an ester or carbonate linkage. The reaction mixture defines a ratio eta (η) of liquid volume, in μL, to total solids, in mg, that is less than 2 μL/mg. Then, allowing an enzyme-catalyzed reaction of the enzyme with the polymer to take place thereby forming a reaction product.

Enzyme-immobilizing MOFs and methods for their use in enzymatically catalyzed reactions are provided. The MOFs are channel-type MOFs that present a hierarchical pore structure comprising a first set of large channels sized for enzyme immobilization and a second set of smaller channels running alongside of the large channels that remain enzyme-free and allow for reactant delivery to the enzymes and product expulsion from the larger channels.

Enzymes are disclosed that have anti-pilling properties and may be used in washing or cleaning agents. A washing or cleaning agent, in particular a liquid detergent, may include a cutinase. A method for cleaning textiles using such a washing or cleaning agent may be useful for removal of soiling, for reducing the pilling effects on textiles, for improving the anti-greying effects, for improving the cleaning performance of such a washing or cleaning agent, and combinations thereof. The cutinase may have at least 65% sequence identity with the amino acid sequence set forth in SEQ ID NO:1 over the entire length thereof and have at least one or more amino acid substitutions at positions 61, 63, 66, 89, 90, 92, 155, 177, 208 and 211.

This technology relates in part to polypeptide compositions and to methods of treatment using the compositions, such as the treatment of diseases or conditions that are accompanied by microbial or viral infections, wounds or sores and the treatment of surfaces contaminated by microbes, viruses or other pathogens.

Novel ways of degrading polyamides including Nylon 6 and Nylon 6,6 (polycaprolactam) are disclosed. Microorganisms originally sourced from the environment are utilized to produce an enzyme(s) useful for degrading polyamides. can be degraded by a cutinase, a lipase, or a combination thereof.

The present invention relates to novel esterase, more particularly to esterase variants having improved thermostability compared to the esterase of SEQ ID N.sup.o 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 PET hydrolase having improved thermal stability is disclosed. The PET hydrolase has a modified amino acid sequence of SEQ ID NO: 2 or a modified amino acid sequence with at least 80% sequence identity of SEQ ID NO: 2, wherein the modification is a substitution of asparagine at position 248 or a corresponding position with proline.