C12P13/227

Synthesis of bioproducts from lignin-derived aromatics by genetically modified microorganisms

The present invention provides for a method of converting a depolymerized lignin aromatic compound into a bioproduct, comprising: (a) providing a composition comprising a depolymerized lignin aromatic compound, optionally a depolymerized cellulose, and optionally a depolymerized hemicellulose, and (b) introducing a genetically modified microorganism to the composition, wherein the genetically modified microorganism is capable of converting the depolymerized lignin aromatic compound into a bioproduct; such that the depolymerized lignin aromatic compound is converted into a bioproduct.

METHOD FOR THE SYNTHESIS OF TRYPTOPHAN ANALOGS IN AQUEOUS SOLVENTS AT REDUCED TEMPERATURES

The present disclosure provides methods for preparing tryptophans and tryptophan derivatives. The methods include: combining i) an indole substrate or azulene substrate, ii) a serine substrate, and iii) an engineered tryptophan synthase -subunit (TrpB); and maintaining the resulting mixture under conditions sufficient to form the product compound. The engineered TrpB comprises a PLP binding loop mutation, a helix 1 mutation, a strand 7-8 mutation, or a combination thereof. New TrpB variants are also described.

Microorganism of the genus Escherichia producing L-tryptophan and a method for producing L-tryptophan using the same

The present disclosure relates to a microorganism of the genus Escherichia producing more L-tryptophan by inactivating the activity of phosphatase. Additionally, the present disclosure relates to a method for producing L-tryptophan using the microorganism of the genus Escherichia.

ENGINEERED SYNTHASE FOR PRODUCTION OF TRYPTOPHAN DERIVATIVES AND INTRANSIGENT SUBSTRATES

This disclosure relates to modified tryptophan synthase and more particularly to modified beta-subunits of tryptophan synthase. The disclosure further relates to cells expressing such modified subunits and methods of producing non-canonical amino acids.

Directed evolution of a regioselective halogenase for increased thermostability

Compounds and methods are providing involving RebH variants with improved properties. directed evolution based on random mutagenesis was employed to generate a series of RebH variants. RebH variants with improved thermostability and increased activity at elevated temperatures were generated.

GENETIC PERTURBATION OF THE RNA DEGRADOSOME PROTEIN COMPLEX
20190194769 · 2019-06-27 ·

The present disclosure provides novel bacterial strains with altered expression or start codon modification of one or more RNA degradation/processing genes. The RNA degradation genes of the present disclosure are controlled by heterologous promoters. The present disclosure further describes methods for generating microbial strains comprising heterologous promoter sequences operably linked to RNA degradation/processing genes.

MICROORGANISMS PROGRAMMED TO PRODUCE IMMUNE MODULATORS AND ANTI-CANCER THERAPEUTICS IN TUMOR CELLS

Genetically programmed microorganisms, such as bacteria or virus, pharmaceutical compositions thereof, and methods of modulating and treating cancers are disclosed.

MUTANT SPOT PROTEIN AND METHOD FOR PRODUCING L-AMINO ACIDS USING SAME

Provided are a variant SpoT protein and a method of producing an L-amino acid using the same.

NOVEL PROMOTER AND USE THEREOF

The present application relates to a novel promoter and a method for producing target materials using the same. More specifically, the present application relates to a novel polynucleotide having promoter activity, a gene expression cassette, and a host cell comprising the same, and a method for producing target materials using the microorganism.

Methods and enzyme catalysts for the synthesis of non-canonical amino acids

The present disclosure provides methods for preparing ?-substituted tryptophan compounds. The methods include: combining i) an unsubstituted indole or a substituted indole, ii) a ?-substituted serine, and iii) a tryptophan synthase ?-subunit (i.e., a TrpB); and maintaining the resulting mixture under conditions sufficient to form the ?-substituted tryptophan. The TrpB contains at least one amino acid mutation which promotes formation of an amino-acrylate intermediate. New TrpB variants and new ?-substituted tryptophan analogs are also described.