Abstract:
A polyamide comprising a diamine and a poly(ether glycol) dicarboxylic acid, wherein the poly(ether glycol) dicarboxylic acid has a number-average molecular weight (Mn) of at least 250 Daltons.
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:
Disclosed is a process for removing 2-cyanocyclopentylideneimine (CPI) from a mixture containing CPI and dinitrile. The process comprises reacting CPI with an amine. The reaction may take place in the presence of water, and optionally, a catalyst. CPI is converted to products with a low volatility compared to the dinitrile.
Abstract:
This document describes biochemical pathways for producing 4-hydroxybutyrate, 4-aminobutyrate, putrescine or 1,4-butanediol by forming one or two terminal functional groups, comprised of amine or hydroxyl group, in a C5 backbone substrate such as 2-oxoglutarate or L-glutamate.
Abstract:
This document describes biochemical pathways for producing 7-aminoheptanoic acid using a β-ketoacyl synthase or a β-ketothiolase to form either a 5-amino-3-oxopentanoyl-[ACP] or 5-amino-3-oxopentanoyl-CoA intermediate. 7-aminoheptanoic acid can be enzymatically converted to pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine or 1,7-heptanediol or the corresponding salts thereof. This document also describes recombinant microorganisms producing 7-aminoheptanoic acid as well as pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine and 1,7-heptanediol or the corresponding salts thereof.
Abstract:
This document describes biochemical pathways for biosynthesizing a 3-oxo-7-hydroxyheptanoyl-CoA intermediate using a β-ketothiolase , and enzymatically converting 3-oxo-7-hydroxyheptanoyl-CoA to 7-hydroxyheptanoic acid. - 7-hydroxyheptanoic acid can be further enzymatically converted to pimelic acid, 7-aminoheptanoic acid, heptamethylenediamine or 1,7-heptanediol. This document also describes recombinant hosts producing 7-hydroxyheptanoic acid as well as pimelic acid, 7-aminoheptanoic acid, heptamethylenediamine and 1,7-heptanediol.
Abstract:
Disclosed is a method for inhibiting the formation of by-products from dinitriles, such as the formation of cyclopentylideneimine (CPI) from Adiponitrile (ADN), comprising adding an effective amount of a Brønsted acid to the ADN. Also disclosed is a method of refining a dinitrile compound by distillation the method comprising the steps of: (a) supplying (i) a feedstream comprising the dinitrile compound and (ii) a Brønsted acid to a distillation apparatus; and (b) withdrawing from the distillation apparatus an overhead distillate stream comprising the dinitrile compound.
Abstract:
The present disclosure relates to processes for production of alkene products from their alkene precursors, such as 3~hydroxyacid and alcohols, via either (1) high temperature reactive distillation with steam contact at optimal pH, (2) solvent extraction and Mulzer dehydration, (3) solid phase adsorption, desorption into an organic solvent and catalytic reaction and (4) high temperature reactive distillation with steam contact at optimal pH followed by catalytic conversion.
Abstract:
Described herein are processes and apparatus for the high purity and high concentration recovery of multivalent products via continuous ion exchange from aqueous solutions for further down-stream purification.