Chemical recyling of plastics using ionic liquids or deep eutectic solvents
US-2024052133-A1 · Feb 15, 2024 · US
US2016289656A1 · US · A1
| Field | Value |
|---|---|
| Publication number | US-2016289656-A1 |
| Application number | US-201615084621-A |
| Country | US |
| Kind code | A1 |
| Filing date | Mar 30, 2016 |
| Priority date | Jun 17, 2011 |
| Publication date | Oct 6, 2016 |
| Grant date | — |
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The invention relates to methods for enriching monomer content in a cycloalkane oxidation process mixed organic waste stream. In particular, the methods involve combining a biocatalyst with a mixed organic waste stream from a cycloalkane oxidation process, and enzymatically converting dimeric and/or oligomeric components of said waste stream into monomeric components. The methods may enrich the content of diacids, adipic acid, and/or other α,ω-difunctional C6 alkanes in the mixed organic waste stream. Additionally, the treated mixed organic waste streams may have improved burning efficiency.
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1 .- 39 . (canceled) 40 . A composition comprising a mixed organic waste stream of a cycloalkane oxidation process and a biocatalyst. 41 . The composition of claim 40 , wherein the mixed organic waste stream is non-volatile residue NVR, water wash, concentrated water extract stream COP acid, a caustic wash stream, or combinations thereof. 42 . The composition of claim 40 , wherein the biocatalyst is an isolated enzyme or an enzyme secreted by a naturally occurring or non-naturally occurring host cell. 43 . The composition of claim 42 , wherein the host cell is tolerant to NVR. 44 . The composition of claim 43 , wherein the host cell is tolerant to at least 1% of the mixed organic waste stream by volume. 45 . The composition of claim 42 , wherein the naturally or non-naturally occurring host cell comprises an endogenous or heterologous ω-oxidation pathway that converts aliphatic fatty acids to diacids via hydroxyl-acids and oxo-acids, and wherein the naturally or non-naturally occurring host cell is an n-alkane utilizing yeast or bacterium. 46 . The composition of claim 45 , where the n-alkane utilizing yeast is Yarrowia lipolytica, Candida tropicalis, C. albicans, C. cloacae, C. guillermondii, C. intermedia, C. maltosa, C. parapsilosis, C. zeylenoides , or combinations thereof, or yeasts of the Rhodotonda, Rhizopus, Trichosporon, Debaryomyces and Lipomyces genera or combinations thereof; and wherein the n-alkane utilizing bacteria is Pseudomonas fluorescens, P. putida, P. aeroginosa, P. oleoverans, Marinobacter hydrocarbonoclasticus, Acinetobacter venetianus, Oleiphilus messinensis, Arthrobacter viscosus, Cupriavidus metallidurans, Rhodococcus erythropolis, Sphingomona spaucimobilis, Burkholderia cepacia, Delftia acidovorans, Alcanivorax diesolei , or combinations thereof. 47 . The composition of 42 , wherein the enzyme is a hydrolase. 48 . The composition of claim 47 , wherein the hydrolase is a lipase (EC 3.1.1.3), esterase (EC 3.1.1.1), cutinase (EC 3.1.1.74), polyhydroxyalkanoate (PHA) depolymerase (EC 3.1.1.75 & EC 3.1.1.76), lactone hydrolase; gluconolactonases (EC 3.1.1.17), a laccase (EC 1.10.3.2), or combinations thereof. 49 . The composition of claim 48 , wherein the lactone hydrolase is 1,4-lactonase (EC 3.1.1.25). 50 . The composition of claim 42 , wherein said enzyme is a P450 cytochrome oxidase, an ω-hydroxylase, ω-oxygenase enzyme or alkane-1-monooxygenase from the class EC 1.14.15.3; a fatty alcohol oxidase; an alcohol dehydrogenase from the class EC 1.1.1.-; a Baeyer-Villiger monooxygenase; a caprolactone lactonohydrolase; a fatty alcohol oxidase; an alcohol dehydrogenase; a cyclohexane-1,2-diol dehydrogenase; a cyclohexane-1,2-dione acylhydrolase; a carboxylesterase from the α,β-hydrolase fold family (EC 3.1.1.-); or combinations thereof. 51 . The composition of claim 42 , wherein the enzyme is a cyclohexanol dehydrogenase/ChnA from the class EC 1.1.1.245; cyclohexanone monooxygenase/ChnB from the class EC 1.14.13.22; gluconolactonase/ChnC from the class EC 3.1.1.17; ChnD from the class EC 1.1.1.2; cyclohexane-1,2-diol dehydrogenase from EC 1.1.1.174; cyclohexane-1,2-dione acylhydrolase from EC 3.7.1.10 or EC 3.7.1.11; or combinations thereof. 52 .- 58 . (canceled)
Poly(3-hydroxyoctanoate) depolymerase (3.1.1.76) · CPC title
Carboxylesterase (3.1.1.1) · CPC title
Poly(3-hydroxybutyrate) depolymerase (3.1.1.75) · CPC title
Triacylglycerol lipase (3.1.1.3) · CPC title
Gluconolactonase (3.1.1.17) · CPC title
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