Abstract:
This application describes methods, including non-naturally occurring methods, for biosynthesizing 3-hydroxy-3-methylglutaryl-coA and intermediates thereof, as well as non-naturally occurring hosts for producing 3-hydroxy-3-methylglutaryl-coA. This application also describes methods, including non-naturally occurring methods, for biosynthesizing isoprene and intermediates thereof, as well as non-naturally occurring hosts for producing isoprene.
Abstract:
This document describes biochemical pathways for producing a difunctional product having an odd number of carbon atoms in vitro or in a recombinant host, or salts or derivatives thereof, by forming two terminal functional groups selected from carboxyl, amine, formyl, and hydroxyl groups in an aliphatic carbon chain backbone having an odd number of carbon atoms synthesized from (i) acetyl-CoA and propanedioyl-CoA via one or more cycles of methyl ester shielded carbon chain elongation or (ii) propanedioyl-[acp] via one or more cycles of methyl ester shielded carbon chain elongation. The biochemical pathways and metabolic engineering and cultivation strategies described herein rely on enzymes or homologs accepting methyl ester shielded aliphatic carbon chain backbones and maintaining the methyl ester shield for at least one further enzymatic step following one or more cycles of methyl ester shielded carbon chain elongation.
Abstract:
A side stream compounding unit is coupled to a continuous polyamide manufacturing system and is configured to divert polyamide from the manufacturing system, mixes additive with polyamide, and then return the polyamide-additive mixture to a main stream of polyamide in the manufacturing system.
Abstract:
This document describes biochemical pathways for producing pimeloyl-CoA using a polypeptide having the enzymatic activity of a hydroperoxide lyase to form non-3-enal and 9- oxononanoate from 9-hydroxyperoxyoctadec-10,12-dienoate. Non-3-enal and 9-oxononanoate can be enzymatically converted to pimeloyl-CoA or a salt thereof using one or more polypeptides having the activity of a dehydrogenase , a CoA ligase , an isomerase , a reductase , a thioesterase , a monooxygenase , a hydratase , and/or a thiolase . Pimeloyl-CoA can be enzymatically converted to pimelic acid, 7-aminoheptanoic acid, 7-hydroxyheptanoic acid, heptamethylenediamine, or 1,7-heptanediol, or corresponding salts thereof. This document also describes recombinant microorganisms producing pimeloyl-CoA, as well as pimelic acid, 7-aminoheptanoic acid, 7-hydroxyheptanoic acid, heptamethylenediamine, and 1,7-heptanediol, or corresponding salts thereof.
Abstract:
This document describes biochemical pathways for producing 6-hydroxyhexanoic acid using a monooxygenase to form a 7-hydroxyoctanoate intermediate, which can be converted to 6-hydroxyhexanoate using a polypeptide having monooxygenase , secondary alcohol dehydrogenase , or esterase activity. 6-hydroxyhexanoic acid can be enzymatically converted to adipic acid, caprolactam, 6-aminohexanoic acid, hexamethylenediamine or 1,6-hexanediol. This document also describes recombinant hosts producing 6-hydroxyhexanoic acid as well as adipic acid, caprolactam, 6-aminohexanoic acid, hexamethylenediamine and 1,6-hexanediol.
Abstract:
This document describes biochemical pathways for producing a difunctional product having an odd number of carbon atoms in vitro or in a recombinant host, or salts or derivatives thereof, by forming two terminal functional groups selected from carboxyl, amine, formyl, and hydroxyl groups in an aliphatic carbon chain backbone having an odd number of carbon atoms synthesized from (i) acetyl-CoA and propanedioyl-CoA via one or more cycles of methyl ester shielded carbon chain elongation or (ii) propanedioyl-[acp] via one or more cycles of methyl ester shielded carbon chain elongation, The biochemical pathways and metabolic engineering and cultivation strategies described herein rely on enzymes or homologs accepting methyl ester shielded aliphatic carbon chain backbones and maintaining the methyl ester shield for at least one further enzymatic step following one or more cycles of methyl ester shielded carbon chain elongation.
Abstract:
Described herein are methods of preparing high molecular weight polyamides which reduce or eliminate the production of unwanted gels during the production process. These methods reduce the formation of undesired polyamide gel by polishing the internal surfaces of the production equipment, thereby providing surfaces with smaller surface roughness values.
Abstract:
This disclosure describes methods for regulating the biosynthesis of pimelic acid, 7-arninoheptanoate, 7-hydroxyheptanoate, heptamethyJenediamine, 7-aminoheptanol, or 1,7-heptanedioi by channeling increased flux through the biosynthesis pathway to obtain an intermediate required for growth of the host microorganism.
Abstract:
The present disclosure provides novel polypeptides with improved 3-buten-2- ol dehydratase activity, polypeptides with improved linalool dehydratase activity, and polypeptides with catalytic activity in the conversion of 3-methyl-3-buten-2-ol to isoprene. Methods of making and using the polypeptides are also provided.
Abstract:
Disclosed herein are methods for recovering diphosphite-containing compounds from mixtures comprising organic mononitriles and organic dinitriles, using liquid-liquid extraction. Also disclosed are pre-treatments to enhance extractability of the diphosphite-containing compounds.