Provided is ω3 desaturase having high enzymatic activity even at normal temperature. A polypeptide which consists of an amino acid sequence having an identity of 80% or more with the amino acid sequence represented by SEQ ID NO: 2 and has ω3 desaturation activity on C20 fatty acid, and a gene thereof.

An identified 90 bp sequence insertion in the GB0331 genome disrupts the coding sequence of the FAD2-1D gene near the 3′ end of the protein coding region. This sequence is not found in reference genomes of other Gossypium species. This DNA segment can be used to track the high oleic fad-2-1D mutant allele for introgression into cotton varieties such as Pima and upland cotton varieties. This enables a non-GMO strategy to elevate the oleic acid content of commercial cottonseed oil.

The present invention generally relates to methods and materials involved in producing tobacco plants having reduced levels of conversion of nicotine to nornicotine. In certain embodiments, the invention is directed to mutations in a nicotine demethylase gene, tobacco plants comprising mutations in a nicotine demethylase gene, and tobacco compositions and products thereof. In other embodiments, the invention is directed toward nicotine demethylase RNA interference, tobacco plants comprising a nicotine demethylase RNA interference transgene, and tobacco compositions and products thereof.

The present invention relates to a mutant onion (Allium cepa) plant, which is resistant to a pathogen of viral, bacterial, fungal or oomycete origin. The mutant onion plant has a reduced level, reduced activity or complete absence of AcDMR6 protein as compared to a wild type onion plant.

The present disclosure relates to the novel activity of the enzymatic composition containing lytic polysaccharide monooxygenases (LPMOs) that are bacterial (Auxiliary Activity 10, AA10) and/or fungal (Auxiliary Activity 9, AA9) for degrading polyethylene terephthalate (PET) and related plastic polymers. The genes that encode KpLPMO10A (AA10) and AfLPMO9A (AA9) were isolated from Kitasatospora papulosa and Aspergillus fischeri microorganisms, respectively. Methods such as atomic force microscopy (AFM) and X-ray photoelectron spectroscopy (XPS) detected alterations in the superficial chemical composition and morphology of the PET found in liquid bottles when treated with LPMOs. The gentle temperature conditions used during the LPMO-PET reaction suit the use of these enzymes to help canonical enzymes (PETases) deconstruct plastics, which is beneficial for the circular economy for PET.

A method for the enzymatic conversion of a phenol substrate into a corresponding catechol product comprises the step of incubating the phenol substrate with a Ralstonia solanacearum tyrosinase enzyme, or a functional derivative thereof, in a reaction mixture, for a period of time sufficient to allow the enzyme convert at least some of the phenol substrate into the catechol product.

The present invention provides engineered proline hydroxylase polypeptides for the production of hydroxylated compounds, polynucleotides encoding the engineered proline hydroxylases, host cells capable of expressing the engineered proline hydroxylases, and methods of using the engineered proline hydroxylases to prepare compounds useful in the production of active pharmaceutical agents.

The present disclosure relates to mutant enzymes and bacterial strains constructed to produce paraxanthine and 7-methylxanthine from caffeine and methods for the manufacture and use thereof.

The present disclosure relates to a light-driven system which is able to chemically modify an organic substrate with high efficiency and in a cost-effective manner. Also provided are methods for chemically modifying an organic substrate using the present systems and methods for manufacturing such systems.

The invention relates to a plastic compound comprising at least one polyolefin and a biological entity that degrades said polyolefin. The invention further relates to a process for preparing a plastic article wherein at least one polyolefin and one biological entity that degrades said polyolefin are mixed at a temperature at which the polyolefin is in a partially or totally molten state.