C12P33/00

MICROBIAL PRODUCTION OF MOGROL AND MOGROSIDES

The present invention provides host cells and methods for making mogrol glycosides, including Mogroside V (Mog.V), Mogroside VI (Mog.VI), Iso-Mogroside V (Isomog.V), siamenoside, and glycosylation products that are minor products in Siraitia grosvenorii. The invention provides engineered enzymes and engineered host cells for producing mogrol glycosylation products, such as Mog.V, Mog.VI, and Isomog.V, at high purity and/or yield. The present technology further provides methods of making products containing mogrol glycosides, such as Mog.V, Mog.VI, and Isomog.V, including food products, beverages, oral care products, sweeteners, and flavoring products.

Group of UDP-glycosyltransferase for catalyzing carbohydrate chain elongation and application thereof

The present invention relates to a group of glycosyltransferase, and an application thereof. Specifically, provided is using glycosyltransferase GT29-32, GT29-33, GT29-34, GT29-4, GT29-5, GT29-7, GT29-9, GT29-11, GT29-13, GT29-17, GT29-18, GT29-19, GT29-20, GT29-21, GT29-22, GT29-23, GT29-24, GT29-25, GT29-36, GT29-37, GT29-42, GT29-43, GT29-45, GT29-46, PNUGT29-1, PNUGT29-2, PNUGT29-3, PNUGT29-4, PNUGT29-5, PNUGT29-6, PNUGT29-7, PNUGT29-8, PNUGT29-9, PNUGT29-14, and PNUGT29-15, as well as derived polypeptides thereof to catalyze the first glycosyl at position C-20, the first glycosyl at position C-6, and the first glycosyl at position C-3 of a tetracyclic triterpene compound substrate to elongate a carbohydrate chain, thereby obtaining a catalytic reaction of ginsenoside products such as ginsenoside Rg3, ginsenoside Rd, ginsenoside Rb1, ginsenoside Rb3, saponin DMGG, saponin DMGX, gypenoside LXXV, gypenoside XVII, gypenoside XIII, gypenoside IX, notoginsenoside U, and notoginsenoside R1, notoginsenoside R2, notoginsenoside R3, 3-O-β-(D-xylopyranosyl)-β-(D-glucopyranosyl)-PPD, 3-O-β-(D-xylopyranosyl)-β-(D-glucopyranosyl)-CK, 20-O-Glucosylginsenoside Rf, and Ginsenoside F3. Glycosyltransferase in the present invention can further be applied to construction of artificially synthesized ginsenoside, novel ginsenoside, and derivatives thereof.

BIOSYNTHESIS OF MOGROSIDES

The disclosure relates to enzymes, such as cucurbitadienol synthase (CDS), UDP-glycosyltransferase (UGT), C11 hydroxylase, epoxide hydrolase (EPH), squalene epoxidase (SQE), and/or cytochrome P450 reductase enzymes, recombinant host cells expressing the enzymes, and methods of producing mogrol precursors, mogrol, and/or mogrosides using such recombinant cells.

Methods for selecting microbes from a diverse genetically modified library to detect and optimize the production of metabolites

The present invention relates to genetically modified bacteria and methods of optimizing genetically modified bacteria for the production of a metabolite.

Methods for selecting microbes from a diverse genetically modified library to detect and optimize the production of metabolites

The present invention relates to genetically modified bacteria and methods of optimizing genetically modified bacteria for the production of a metabolite.

OMEGA MURICHOLIC ACID AS A PREGNANE X RECEPTOR LIGAND FOR TREATING HEPATO-INTESTINAL DISEASES

Methods for activating pregnane X receptor (PXR) using co-muricholic acid thereby treating metabolic syndrome, obesity, inflammatory bowel disease, Crohn’s disease, and liver disease, and also thereby increasing CYP3A4 gene and/or protein expression. Also provided are related methods for activating PXR using β-muricholic acid and a bacterium capable of converting β-muricholic acid to co-muricholic acid.

OMEGA MURICHOLIC ACID AS A PREGNANE X RECEPTOR LIGAND FOR TREATING HEPATO-INTESTINAL DISEASES

Methods for activating pregnane X receptor (PXR) using co-muricholic acid thereby treating metabolic syndrome, obesity, inflammatory bowel disease, Crohn’s disease, and liver disease, and also thereby increasing CYP3A4 gene and/or protein expression. Also provided are related methods for activating PXR using β-muricholic acid and a bacterium capable of converting β-muricholic acid to co-muricholic acid.

Coupled, self-sufficient biotransformation of chenodeoxcholic acid to ursodeoxycholic acid and novel enzyme mutants applicable in said process
11634743 · 2023-04-25 · ·

The present invention relates to a coupled biotransformation process of converting chenodeoxycholic acid (CDCA) and related compounds to ursodeoxycholic acid (UDCA) and related compounds. It also relates to the cloning, expression, and biochemical characterization of a novel NADP.sup.+-dependent 7α-hydroxysteroid dehydrogenase (7α-HSDH) from Clostridium difficile, cofactor switch mutants thereof, and their application for the oxidation of bile acids. A further aspect of the invention relates to novel NADP-dependent cofactor switch mutants of the NADP.sup.+-dependent 7α-HSDH of E. coli and their application for the oxidation of bile acids.

Production of sterols in modified yeast

The present invention is related to production of a sterol mix in a modified yeast cell, wherein the amount of zymosterol present in said mix is dramatically reduced or abolished via modification of sterol acyltransferase activity within said yeast. The modified yeast cell can be used for production of vitamin D3 or derivatives and/or metabolites thereof.

UDP-glycosyltransferases

The present disclosure relates a polypeptide having UGT activity, which polypeptide comprises an amino acid sequence which, when aligned with a polypeptide having UGT activity comprising the sequence set out in SEQ ID NO: 2, comprises at least one substitution of an amino acid corresponding to any of amino acids at positions 35, 189, 280, 284, 285, 334 or 373, said positions being defined with reference to SEQ ID NO: 2 and wherein the polypeptide has one or more modified properties as compared with a reference polypeptide having UGT activity. A polypeptide according to the disclosure may be used in a recombinant cell for the production of steviol or a steviol glycoside.