C12Y114/13008

RECOMBINANT METHANOTROPHIC BACTERIA FOR INDIGO BIOSYNTHESIS AND METHODS THEREOF

The instant disclosure is in the field of biosciences, more particularly towards molecular and industrial biotechnology. The present disclosure relates to recombinant methanotrophic bacteria capable of synthesizing indigo from methane, a method of developing said recombinant methanotrophic bacteria, and a method of indigo biosynthesis by the recombinant methanotrophic bacteria in presence of a methane source.

APPLICATION OF FLAVIN-CONTAINING MONOOXYGENASE 2 (FMO2) IN PREPARING DRUG FOR TREATMENT OF NON-ALCOHOLIC FATTY LIVER DISEASE (NAFLD)
20220313793 · 2022-10-06 · ·

The present invention relates to the field of biomedicine, and the present invention discloses an application of flavin-containing monooxygenase 2 (FMO2) in preparing a drug for treatment of non-alcoholic fatty liver disease (NAFLD). The present invention finds for the first time that FMO2 has an effect of preventing or treating NAFLD.

Protecting group chemistry for clean, reductant-free dyeing

The present disclosure relates to the biosynthesis of indigoid dye precursors and their conversion to indigoid dyes. Specifically, the present disclosure relates to methods of using polypeptides to produce indigoid dye precursors from indole feed compounds, and the use of the indigoid dye precursors to produce indigoid dyes.

PROTECTING GROUP CHEMISTRY FOR CLEAN, REDUCTANT-FREE DYEING

The present disclosure relates to the biosynthesis of indigoid dye precursors and their conversion to indigoid dyes. Specifically, the present disclosure relates to methods of using polypeptides to produce indigoid dye precursors from indole feed compounds, and the use of the indigoid dye precursors to produce indigoid dyes.

METHOD AND RECOMBINANT POLYPEPTIDE FOR INCREASING PRODUCTION OF INDIGOID COMPOUND
20230279367 · 2023-09-07 ·

The present disclosure provides a method for increasing production of an indigoid compound, including the following steps: (a) mutating a wild-type flavin-containing monooxygenase to a mutant flavin-containing monooxygenase expressed in Escherichia coli; and (b) culturing the Escherichia coli in a bacterial culture medium comprising tryptophan to allow the mutant FMO to interact with tryptophan for a predetermined time to convert the tryptophan into the indigoid compound. Compared to the wild-type flavin-containing monooxygenase, the mutant flavin-containing monooxygenase increases production of the indigoid compound. The present disclosure also provides a recombinant polypeptide for increasing production of the indigoid compound.

ENZYMES OF LUCIFERIN BIOSYNTHESIS AND USE THEREOF
20210115476 · 2021-04-22 ·

Present invention is aimed at identification of new fungal luciferin biosynthesis enzymes, nucleic acids able to encode these enzymes, and proteins able to catalyze certain stages of the fungal luciferin biosynthesis. The invention also provides for application of nucleic acids for producing said enzymes in a cell or organism. Methods for in vitro or in vivo preparation of chemical compounds identical to fungal luciferins and preluciferins are also provided. Vectors comprising nucleic acid described in the present invention are also provided. In addition, the present invention provides expression cassettes comprising the nucleic acid of the present invention and regulatory elements necessary for nucleic acid expression in a selected host cell. Besides, cells, stable cell lines, transgenic organisms (e.g. plants, animals, fungi, or microorganisms) including nucleic acids, vectors, or expression cassettes of the present invention are also provided. Present invention also provides combinations of nucleic acids to obtain autonomously luminous cells, cell lines, or transgenic organisms. In preferred embodiments, cells or transgenic organisms are capable to produce fungal luciferin from precursors. In some embodiments, cells or transgenic organisms are capable to produce fungal preluciferin from precursors. In some embodiments, cells or transgenic organisms are capable of bioluminescence in the presence of a fungal luciferin precursor. In some embodiments, cells or transgenic organisms are capable of autonomous bioluminescence. Combinations of proteins for producing luciferin or its precursors from more simple chemical compounds are also provided. A kit containing nucleic acids, vectors, or expression cassettes of the present invention for producing luminous cells, cell lines, or transgenic organisms is also provided.

PROTECTING GROUP CHEMISTRY FOR CLEAN, REDUCTANT-FREE DYEING

The present disclosure relates to the biosynthesis of indigoid dye precursors and their conversion to indigoid dyes. Specifically, the present disclosure relates to methods of using polypeptides to produce indigoid dye precursors from indole feed compounds, and the use of the indigoid dye precursors to produce indigoid dyes.

Protecting group chemistry for clean, reductant-free dyeing

The present disclosure relates to the biosynthesis of indigoid dye precursors and their conversion to indigoid dyes. Specifically, the present disclosure relates to methods of using polypeptides to produce indigoid dye precursors from indole feed compounds, and the use of the indigoid dye precursors to produce indigoid dyes.

Mutated enzyme of flavin containing monooxygenase with increased indigo production and recombinant microorganism producing the same

The present invention relates to a mutated protein of FMO derived from Celeribacter sp. and a gene encoding the same, a vector comprising the gene, a recombinant cell transformed by the vector, a composition for producing indigo comprising them, and a method for increasing indigo production in the recombinant cell using the transformed recombinant cell.

MAGNETICALLY IMMOBILIZED METABOLIC ENZYMES AND COFACTOR SYSTEMS

The present invention provides compositions and methods for producing magnetic bionanocatalysts (BNCs) comprising metabolically self-sufficient systems of enzymes that include P450 monooxygenases or other metabolic enzymes and cofactor regeneration enzymes.