43 results about "3-hydroxypropionaldehyde" patented technology

Organisms are provided which express enzymes such as glycerol dehydratase, diol dehydratase, acyl-CoA transferase, acyl-CoA synthetase β-ketothiolase, acetoacetyl-CoA reductase, PHA synthase, glycerol-3-phosphate dehydrogenase and glycerol-3-phosphatase, which are useful for the production of PHAs. In some cases one or more of these genes are native to the host organism and the remainder are provided from transgenes. These organisms produce poly (3-hydroxyalkanoate) homopolymers or co-polymers incorporating 3-hydroxypropionate or 3-hydroxyvalerate monomers wherein the 3-hydroxypropionate and 3-hydroxyvalerate units are derived from the enzyme catalysed conversion of diols. Suitable diols that can be used include 1,2-propanediol, 1,3 propanediol and glycerol. Biochemical pathways for obtaining the glycerol from normal cellular metabolites are also described. The PHA polymers are readily recovered and industrially useful as polymers or as starting materials for a range of chemical intermediates including 1,3-propanediol, 3-hydroxypropionaldehyde, acrylics, malonic acid, esters and amines.

The present invention provides a hydrogenation catalyst effective for hydrogenating 3-hydroxypropionaldehyde to 1,3-propanediol. The hydrogenation catalyst comprises an α-alumina support, nickel, ruthenium, and a promoter. The nickel is deposited on the α-alumina support, and the ruthenium and the promoter are deposited on the nickel and the α-alumina support. The α-alumina support comprises at least 92 wt. % of the catalyst, and the nickel comprises from 1 wt. % to 6 wt. % of the catalyst. The present invention also provides a process of hydrogenating 3-hydroxypropionaldehyde to 1,3-propanediol with the catalyst.

The present invention relates to improvements in the production of 1,3-propanediol (PDO), wherein an aqueous solution of 3-hydroxypropionaldehyde (HPA) is formed and the HPA is hydrogenated to produce a crude PDO mixture. A modification of the process involves treating the crude PDO mixture with acidic zeolites, acidic cation exchange resins, or soluble acids to convert the MW176 cyclic acetal to a more volatile species that can be easily separated from PDO by distillation. Another improvement involves removing water from the crude 1,3-propanediol mixture and contacting the resulting mixture with a solid acid purifying agent at a temperature of about 50-250°C to convert the MW132 cyclic acetal to the more volatile The cyclic acetal, and the separation of the more volatile cyclic acetal from the 1,3-propanediol by distillation or stripping.

A microorganism genetically modified for the bioproduction of 1,3-propanediol from sucrose, wherein the microorganism includes:a two-step metabolic pathway for the production of 1,3-propanediol, including a first step of decarboxylation of 4-hydroxy-2-ketobutyrate with an enzyme having a 2-keto acid decarboxylase activity, and a second step of reduction of the obtained 3-hydroxypropionaldehyde with an enzyme having hydroxy aldehyde reductase activity, andgenes enabling the microorganism to utilize sucrose as sole carbon source.A method for the biological preparation of 1,3-propanediol by fermentation, including cultivating said microorganism genetically modified, wherein the culture is performed in an appropriate medium including a source of sucrose, and recovering the 1,3-propanediol being produced.

The provided separate and recovery method for non-reacted acrolein in preparation process of 3-hydroxypropionaldehyde comprises: leading gas into the tower bottom for gas stripping the acrolein from reaction product and absorb it in absorption tower with water. This invention has high recovery and prepares the material with the absorbed liquid for acrolein hydration reaction.

The invention relates to a modified microorganism for the production of PDO from a carbon substrate wherein the microorganism includes a three-step metabolic pathway including a first step of conversion of 2,4-dihydroxybutyrate (DHB) to obtain 2-oxo-4-hydroxybutyrate (OHB) by an enzyme having 2,4-DHB dehydrogenase activity, a second step of decarboxylation of the OHB to obtain 3-hydroxypropionaldehyde by an enzyme having 2-oxo-4-hydroxybutyrate decarboxylase activity, and a third step of reduction of the obtained 3-hydroxypropionaldehyde to obtain PDO with an enzyme having 3-hydroxypropionaldehyde reductase activity and the genes enabling the microorganism for the synthesis of DHB.