Genetically engineered bacteria, pharmaceutical compositions thereof, and methods of treating or preventing autoimmune disorders, inhibiting inflammatory mechanisms in the gut, and/or tightening gut mucosal barrier function are disclosed.

The invention relates to compositions and methods, including polynucleotide sequences, amino acid sequences, recombinant host cells and recombinant host cell cultures engineered to produce fatty acid derivative compositions comprising fatty acids, fatty alcohols, fatty aldehydes, fatty esters, alkanes, terminal olefins, internal olefins or ketones. The fatty acid derivative composition is produced extracellularly with a higher titer, yield or productivity than the corresponding wild type or non-engineered host cell.

Microorganisms and methods of producing n-butyraldehyde with enhanced yields are presented in which a microorganism is engineered to enhance the conversion of a carbon source into n-butyraldehyde. The n-butyraldehyde is recovered by way of a gas stripping process that occurs during the conversion process, providing significantly greater product yield than post-fermentation recovery of n-butyraldehyde alone.

An object of the present invention is to provide a microorganism that efficiently produces EPA and a method for producing EPA using the microorganism. The present invention relates to a microorganism having an ability to produce docosahexaenoic acid (DHA), wherein the microorganism contains a protein composed of an amino acid sequence in which at least one of the amino acid residues at positions 6, 65, 230, 231, and 275 in the amino acid sequence represented by SEQ ID NO: 2 has been substituted with another amino acid residue (mutated OrfB), and is capable of producing eicosapentaenoic acid (EPA), and the like.

The present invention discloses a S-adenosyl-L-methionine δ24-sterol-C-methyltransferase mutant C24MTgm-M11. Strain MG1655 (ΔptsG ΔfumAC ΔfumB, panD, aspA, C24MTgm) is constructed based on the polynucleotide encoding the enzyme mutant. Strain MG1655 (Δpts GΔfumAC ΔfumB, panD, aspA, C24MTgm-M11) can produce 480 mg/L 3-aminoisobutyric acid under shake flask fermention. Compared to the wild type strain C24MTgm, the strain containing mutant C24MTgm-M11 has a significantly improved ability to produce 5.8 times' 3-aminobutyric acid.

Provided are a co-immobilized enzyme, a preparation method and use thereof. The co-immobilized enzyme includes: an amino resin carrier, a main enzyme, and a coenzyme. The main enzyme and the coenzyme are co-immobilized on the amino resin carrier, herein the main enzyme is covalent-immobilized on the amino resin carrier, and the coenzyme is immobilized on the amino resin carrier by a mode of covalent and/or non-covalent; and the main enzyme is selected from any one of the following enzymes: transaminase, amino acid dehydrogenase, imine reductase, ketoreductase, enoyl reductase, and monooxygenase. The main enzyme and the coenzyme thereof are co-immobilized on the amino resin carrier for co-immobilization, so the activity and the recycling efficiency of the enzyme are improved.

The use of microorganisms to make alpha-functionalized chemicals and fuels, (e.g. alpha-functionalized carboxylic acids, alcohols, hydrocarbons, amines, and their beta-, and omega-functionalized derivatives), by utilizing an iterative carbon chain elongation pathway that uses functionalized extender units. The core enzymes in the pathway include thiolase, dehydrogenase, dehydratase and reductase. Native or engineered thiolases catalyze the condensation of either unsubstituted or functionalized acyl-CoA primers with an alpha-functionalized acetyl-CoA as the extender unit to generate alpha-functionalized β-keto acyl-CoA. Dehydrogenase converts alpha-functionalized β-keto acyl-CoA to alpha-functionalized β-hydroxy acyl-CoA. Dehydratase converts alpha-functionalized β-hydroxy acyl-CoA to alpha-functionalized enoyl-CoA. Reductase converts alpha-functionalized enoyl-CoA to alpha-functionalized acyl-CoA. The platform can be operated in an iterative manner (i.e. multiple turns) by using the resulting alpha-functionalized acyl-CoA as primer and the aforementioned alpha-functionalized extender unit in subsequent turns of the cycle. Termination pathways acting on any of the four alpha-functionalized CoA thioester intermediates terminate the platform and generate various alpha-functionalized carboxylic acids, alcohols and amines with different β-reduction degree.

An object of the present invention is to provide an animal cell with improved proliferation ability and survival rate, a method for producing the animal cell, and a method for producing a target protein formed of the animal cell. According to the present invention, there is provided an animal cell having a gene encoding a target protein and a foreign gene encoding an isovaleryl-CoA dehydrogenase, in which the isovaleryl-CoA dehydrogenase is overexpressed.

The present disclosure relates to the production of cannabinoids in either recombinant microorganism or in cell-free systems using a combination of enzymes, including but not limited to a PKS enzyme, a npgA enzyme, a cs-OLAS-1, a pp-DVAS-1, a cs-HEX-1 and/or Butiryl synthase.

Provided are a microorganism that produces a diamine compound and a method of producing a diamine compound.

The genetically modified microorganism expresses an enzyme involved in synthesis of a diamine compound, in which the diamine compound is represented by Formula: H.sub.2N—R—NH.sub.2 (wherein, R is a chain or cyclic organic group comprised of one or more atoms selected from the group consisting of C, H, O, N, and S), and the genetically modified microorganism is modified to reduce an activity of an alcohol dehydrogenase compared to a non-reduced strain.