Detergent compositions including polypeptide variants and methods of cleaning and/or treatment of surfaces using such compositions, and fabric treatment compositions including polypeptide variants. The compositions may include surfactants: anionic, nonionic and/or cationic.

The present invention relates to variants with cutinase activity of a parent cutinase, comprising an alteration at one or more (e.g. several) positions corresponding to positions: 36, 37, 40, 78, 90, 114, 150, 196, 216, or 217 of SEQ ID NO: 2, wherein the alteration is a substitution for positions 40, 78, 90, 114, 150, 196 and 216, and a deletion for positions 36, 37 and 217, and wherein the variant has at least 75% but less than 100% sequence identity to the mature polypeptide 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 method for obtaining and methods of producing the variants. It also relates to compositions comprising the variant, and to methods for using the variant.

The present invention is located in the field of biotechnology, it refers to the creation of recombinant enzymes with improved thermostability, from mutations made in the Thermobifida fusca cutinase. Likewise, the present invention refers to the use of recombinant enzymes in the degradation of aromatic and semi-aromatic polymers and their oligomers, such as plastic.

The present invention provides a method to produce RD by using a cutinase to catalyze the esterification of RB under stepwise cooling temperatures, which is related to the field of biosynthesis of organic compounds. The method uses a cutinase from Thermobifida fusca to catalyze the esterification of RB and sophorose to produce RD. The stepwise cooling temperatures are used to reduce the heat inactivation of the enzyme as well as to improve the mass transfer. The method catalyzes the esterification of RB to produce RD in a solvent such as methanol, DMSO and DMF. The reaction is safe, efficient and highly selective. In addition, the method uses stepwise additions of substrate RB and cooling temperatures for the esterification reaction. In this way, it speeds up the initial reaction rate, increases the amount of solved RB as it is converted to RD, and improves the mass transfer to further increase the reaction speed. In summary, the method uses moderate reaction conditions, and has a high yield and a simple purification procedure.

Using the sympathetic printed-matter according to the present invention, a hidden content can be visualized just by wetting. Therefore, it is possible to remove necessities of the sympathetic ink and a special material such as reagent or equipment for visualizing hidden contents. In addition, since the hidden contents disappear by removing water from the sympathetic printed-matter, the sympathetic printed-matter can be used repeatedly. Using the reading confirmation portion, whether or not the sympathetic printed-matter has been read by any other person can be easily determined. In the sympathetic printing method according to the present invention, a hydrophobic substrate can be formed using an existing gas grafting facility, and an ester hydrolase composition and the reading confirmation portion can be formed using an existing printing method. Therefore, a large amount of sympathetic printed-matters can be produced inexpensively and efficiently.

The present invention relates to a method for producing a cutinase-like enzyme (CLE1) in a S. cerevisiae cell, comprising heterologously expressing a codon-optimised nucleic acid encoding the cutinase-like enzyme and operably linked to an engineered promoter in the cell. The invention further relates to recombinant S. cerevisiae cells capable of heterologously expressing the cutinase-like enzyme and to cutinase-like enzyme obtained from the cells or prepared by the methods. Also provided are methods of preparing a cell-free supernatant comprising a cutinase-like enzyme from the recombinant S. cerevisiae cells and the use thereof or of the recombinant S. cerevisiae cells in hydrolysing bioplastic polymers.

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 invention relates to novel esterases, more particularly to esterase variants having improved activity and/or improved thermostability compared to the parent esterase of SEQ ID NO:1, SEQ ID NO:2 or SEQ ID NO:3 in acidic conditions 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 in acidic conditions.

The present invention relates to novel esterases, more particularly to esterase variants having improved activity and/or improved thermostability compared to the parent esterase of SEQ ID NO:1 or SEQ ID NO:2 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 mutated bacterial host cells with increased SpoVG polypeptide expression, and nucleic acid constructs and expression vectors encoding SpoVG polypeptides. The invention also relates to methods of producing a protein of interest using the mutated bacterial host cells.