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analysis
deveopment of a phaE biosensor as a a biomarker for microorganisms that contain class III PHA synthase. The phaE biosensor has a high specificity for polyhydroxyalkanoate-producing haloarchaea. The lowest amount of genomic DNA of Haloquadratum walsbyi detected by the biosensor is approximately 250 fg. The phaE biosensor can be applied for screening of polyhydroxyalkanoate-producing haloarchaea from environmental samples
analysis
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deveopment of a phaE biosensor as a a biomarker for microorganisms that contain class III PHA synthase. The phaE biosensor has a high specificity for polyhydroxyalkanoate-producing haloarchaea. The lowest amount of genomic DNA of Haloquadratum walsbyi detected by the biosensor is approximately 250 fg. The phaE biosensor can be applied for screening of polyhydroxyalkanoate-producing haloarchaea from environmental samples
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biotechnology
recombinant protein production and purification from Escherichia coli is often accompanied with expensive and complicated procedures, especially for therapeutic proteins. By using an intein cleavable polyhydroxyalkanoate synthase fusion, recombinant proteins can be first produced and sequestered on a natural resin, the polyhydroxyalkanoate (PHA) inclusions, then separated from contaminating host proteins via simple PHA bead isolation steps, and finally purified by specific release into the soluble fraction induced by a pH reduction
biotechnology
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recombinant protein production and purification from Escherichia coli is often accompanied with expensive and complicated procedures, especially for therapeutic proteins. By using an intein cleavable polyhydroxyalkanoate synthase fusion, recombinant proteins can be first produced and sequestered on a natural resin, the polyhydroxyalkanoate (PHA) inclusions, then separated from contaminating host proteins via simple PHA bead isolation steps, and finally purified by specific release into the soluble fraction induced by a pH reduction
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biotechnology
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recombinant protein production and purification from Escherichia coli is often accompanied with expensive and complicated procedures, especially for therapeutic proteins. By using an intein cleavable polyhydroxyalkanoate synthase fusion, recombinant proteins can be first produced and sequestered on a natural resin, the polyhydroxyalkanoate (PHA) inclusions, then separated from contaminating host proteins via simple PHA bead isolation steps, and finally purified by specific release into the soluble fraction induced by a pH reduction
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biotechnology
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recombinant protein production and purification from Escherichia coli is often accompanied with expensive and complicated procedures, especially for therapeutic proteins. By using an intein cleavable polyhydroxyalkanoate synthase fusion, recombinant proteins can be first produced and sequestered on a natural resin, the polyhydroxyalkanoate (PHA) inclusions, then separated from contaminating host proteins via simple PHA bead isolation steps, and finally purified by specific release into the soluble fraction induced by a pH reduction
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synthesis
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usage of the enzyme for recombinant high-level production of poly(3-hydroxybutyrate), P(3HB), in Escherichia coli and Corynebacterium glutamicum. P(3HB) is the natural aliphatic polyester that can be processed into a wide variety of consumer products, including plastics, films and fibers
synthesis
a Cupriavidus necator polyhydroxyalkanoate-negative transformant harboring the polyhydroxyalkanoate synthase gene from bacterium SC8 is able to accumulate 55 weight% of polyhydroxyalkanoate of the cell dry weight when crude palm kernel oil is used as the carbon source. It produces 14 weight% of polyhydroxyalkanoate when 10 g per l of fructose is used
synthesis
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engineering of an in vivo polylactic acid biosynthesis system in Escherichia coli to synthesize 2-hydroxybutyrate-containing polyhydroxyalkanoate. Propionyl-CoA is used as precursor for 2-ketobutyrate that is converted into 2-hydroxybutyrate-CoA by the sequential actions of Lactococcus lactis (D)-2-hydroxybutyrate dehydrogenase (PanE) and PctCp and then 2-hydroxybutyrate-CoA is polymerized by an engineered PhaC1 from Pseudomonas sp. (mutant E130D/S325T/S477G/Q481K). The recombinant Escherichia coli expressing the system can be grown to 0.66 g/l and successfully produces P(70 mol% 3-hydroxybutyrate-co-18 mol% 3-hydroxybutyrate-co-12 mol% lactate) up to the polyhydroxyalkanoate content of 66 weight% from 20 g/l of glucose, 2 g/l of 3-hydroxybutyrate and 1 g/l of sodium propionate
synthesis
enzyme shows both polyhydroxyalkanoate polymerization and alcoholysis activities, unsing various alcohols other than ethanol for alcoholysis.. Through the use of bifunctional compounds for alcoholysis, the polyhydroxyalkanoate carboxy terminus can be modified with thiol, alkynyl, hydroxy, and benzyl groups, resulting in the functionalization of the polyhydroxyalkanoate carboxy terminus
synthesis
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expansion of the substrate specificity and enhancment of biosynthesis of polyhydroxyalkanoate by site-specific mutagenesis. Mutated PhaC1s are coexpressed with beta-ketothiolase and acetoacetyl-CoA reductase to supply sufficient short-chain length (R)-3-hydroxyacyl-CoA as a substrate. Mutation L484V remarkably enhances the monomer ratio of (R)-3-hydroxybutyrate in a polyhydroxyalkanoate accumulation experiment. Val is the most favorable amino acid for incorporating (R)-3-hydroxybutyrate unit synthesis. A single mutation at Q481M, S482G and A547V obviously increases polyhydroxyalkanoate yields. Q481M and S482G enhance the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation
synthesis
heterologous expression in Escherichia coli with simultaneous overexpression of chaperone proteins. Compared to expression of synthase alone (14.55 mg per liter), coexpression with chaperones results in the production of larger total quantities of enzyme, including a larger proportion in the soluble fraction. The largest increase is seen when the GroEL/GroES system is coexpressed, resulting in approximately 6fold greater enzyme yields (82.37 mg per liter) than in the absence of coexpressed chaperones. The specific activity of the purified enzyme is unaffected by coexpression with chaperones
synthesis
mutant A510S is able to synthesize a lactate-3-hydroxybutanoate copolymer containing 7 mol% lactate and with a averge molecular weight of 320000 Da. The polymer contains a high ratio of an LA-LA-LA triad sequence
synthesis
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biodegradable bio-based polyhydroxyalkanoate (PHA) is gaining much attention as a promising biomaterial that can replace some conventional petroleum-based plastics especially the single use plastics
synthesis
biodegradable bio-based polyhydroxyalkanoate (PHA) is gaining much attention as a promising biomaterial that can replace some conventional petroleum-based plastics especially the single use plastics
synthesis
biodegradable bio-based polyhydroxyalkanoate (PHA) is gaining much attention as a promising biomaterial that can replace some conventional petroleum-based plastics especially the single use plastics. The most studied class I PhaC from Cupriavidus necator (PhaCCn) is often used as a study model to increase its ability to incorporate medium-chain length (MCL) monomers into PHA
synthesis
biodegradable bio-based polyhydroxyalkanoate (PHA) is gaining much attention as a promising biomaterial that could replace some conventional petroleum-based plastics especially the single use plastics. Class II PhaC1 from Pseudomonas sp. 61-3 (PhaC1Ps) is useful in terms of its broad substrate specificity, and engineering of PhaC1Ps successfully increases its short-chain-length (SCL) incorporation into PHA
synthesis
A0A1E8EW93; A0A1E8EW64
poly(3-hydroxyalkanoates) (PHAs) such as poly(3-hydroxybutyrate) (PHB) are suitable biobased and biodegradable candidates to replace petroleum-based nondegradable plastics. Enzyme PhaEC can be used in its biocatalytic production, PHB production in clostridia, method development and evaluation, overview. The successful transfer and expression of phaJ and phaEC in autotrophic gas-fermenting clostridia leading to PHB formation now opens the possibility to establish an economically viable route to biodegradable plastics from waste and greenhouse gases, as the gas fermentation technology has meanwhile matured and is already performed at industrial scale. A novel metabolic pathway leading to 3-hydroxybutyrate has also been engineered that will allow similarly better economic production of this platform chemical
synthesis
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replacement of conventional plastics by bioplastics. Polyhydroxyalkanoates (PHA) are bio-polyesters accumulated in cells by a wide range of bacteria. Polyhydroxyalkanoates production from synthetic waste using Pseudomonas palleronii polyhydroxyalkanoate synthase enzyme activity
synthesis
replacement of conventional plastics by bioplastics. Polyhydroxyalkanoates (PHA) are bio-polyesters accumulated in cells by a wide range of bacteria. Polyhydroxyalkanoates production from synthetic waste using Pseudomonas pseudoflava polyhydroxyalkanoate synthase enzyme activity
synthesis
the enzyme mutant S326T/Q482K might be useful for production of distinct polyhydroxyalkanoate copolymers with improved material properties
synthesis
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the PHA synthase is suitable for the biosynthesis of PHAs that can be used in various biomedical applications due to its ability to incorporate the lipase-degradable monomer sequences of 4-hydroxybutyrate (4HB) and 5-hydroxyvalerate (5HV)
synthesis
the enzyme can be used for polyhydroxyalkanoate production from synthetic wastewater
synthesis
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enzyme shows both polyhydroxyalkanoate polymerization and alcoholysis activities, unsing various alcohols other than ethanol for alcoholysis.. Through the use of bifunctional compounds for alcoholysis, the polyhydroxyalkanoate carboxy terminus can be modified with thiol, alkynyl, hydroxy, and benzyl groups, resulting in the functionalization of the polyhydroxyalkanoate carboxy terminus
-
synthesis
-
biodegradable bio-based polyhydroxyalkanoate (PHA) is gaining much attention as a promising biomaterial that can replace some conventional petroleum-based plastics especially the single use plastics. The most studied class I PhaC from Cupriavidus necator (PhaCCn) is often used as a study model to increase its ability to incorporate medium-chain length (MCL) monomers into PHA
-
synthesis
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the enzyme mutant S326T/Q482K might be useful for production of distinct polyhydroxyalkanoate copolymers with improved material properties
-
synthesis
-
biodegradable bio-based polyhydroxyalkanoate (PHA) is gaining much attention as a promising biomaterial that can replace some conventional petroleum-based plastics especially the single use plastics. The most studied class I PhaC from Cupriavidus necator (PhaCCn) is often used as a study model to increase its ability to incorporate medium-chain length (MCL) monomers into PHA
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synthesis
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expansion of the substrate specificity and enhancment of biosynthesis of polyhydroxyalkanoate by site-specific mutagenesis. Mutated PhaC1s are coexpressed with beta-ketothiolase and acetoacetyl-CoA reductase to supply sufficient short-chain length (R)-3-hydroxyacyl-CoA as a substrate. Mutation L484V remarkably enhances the monomer ratio of (R)-3-hydroxybutyrate in a polyhydroxyalkanoate accumulation experiment. Val is the most favorable amino acid for incorporating (R)-3-hydroxybutyrate unit synthesis. A single mutation at Q481M, S482G and A547V obviously increases polyhydroxyalkanoate yields. Q481M and S482G enhance the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation
-
synthesis
-
a Cupriavidus necator polyhydroxyalkanoate-negative transformant harboring the polyhydroxyalkanoate synthase gene from bacterium SC8 is able to accumulate 55 weight% of polyhydroxyalkanoate of the cell dry weight when crude palm kernel oil is used as the carbon source. It produces 14 weight% of polyhydroxyalkanoate when 10 g per l of fructose is used
-
synthesis
-
poly(3-hydroxyalkanoates) (PHAs) such as poly(3-hydroxybutyrate) (PHB) are suitable biobased and biodegradable candidates to replace petroleum-based nondegradable plastics. Enzyme PhaEC can be used in its biocatalytic production, PHB production in clostridia, method development and evaluation, overview. The successful transfer and expression of phaJ and phaEC in autotrophic gas-fermenting clostridia leading to PHB formation now opens the possibility to establish an economically viable route to biodegradable plastics from waste and greenhouse gases, as the gas fermentation technology has meanwhile matured and is already performed at industrial scale. A novel metabolic pathway leading to 3-hydroxybutyrate has also been engineered that will allow similarly better economic production of this platform chemical
-
synthesis
-
biodegradable bio-based polyhydroxyalkanoate (PHA) is gaining much attention as a promising biomaterial that can replace some conventional petroleum-based plastics especially the single use plastics. The most studied class I PhaC from Cupriavidus necator (PhaCCn) is often used as a study model to increase its ability to incorporate medium-chain length (MCL) monomers into PHA
-
synthesis
-
heterologous expression in Escherichia coli with simultaneous overexpression of chaperone proteins. Compared to expression of synthase alone (14.55 mg per liter), coexpression with chaperones results in the production of larger total quantities of enzyme, including a larger proportion in the soluble fraction. The largest increase is seen when the GroEL/GroES system is coexpressed, resulting in approximately 6fold greater enzyme yields (82.37 mg per liter) than in the absence of coexpressed chaperones. The specific activity of the purified enzyme is unaffected by coexpression with chaperones
-
synthesis
-
mutant A510S is able to synthesize a lactate-3-hydroxybutanoate copolymer containing 7 mol% lactate and with a averge molecular weight of 320000 Da. The polymer contains a high ratio of an LA-LA-LA triad sequence
-
synthesis
-
engineering of an in vivo polylactic acid biosynthesis system in Escherichia coli to synthesize 2-hydroxybutyrate-containing polyhydroxyalkanoate. Propionyl-CoA is used as precursor for 2-ketobutyrate that is converted into 2-hydroxybutyrate-CoA by the sequential actions of Lactococcus lactis (D)-2-hydroxybutyrate dehydrogenase (PanE) and PctCp and then 2-hydroxybutyrate-CoA is polymerized by an engineered PhaC1 from Pseudomonas sp. (mutant E130D/S325T/S477G/Q481K). The recombinant Escherichia coli expressing the system can be grown to 0.66 g/l and successfully produces P(70 mol% 3-hydroxybutyrate-co-18 mol% 3-hydroxybutyrate-co-12 mol% lactate) up to the polyhydroxyalkanoate content of 66 weight% from 20 g/l of glucose, 2 g/l of 3-hydroxybutyrate and 1 g/l of sodium propionate
-
synthesis
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the enzyme can be used for polyhydroxyalkanoate production from synthetic wastewater
-
synthesis
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replacement of conventional plastics by bioplastics. Polyhydroxyalkanoates (PHA) are bio-polyesters accumulated in cells by a wide range of bacteria. Polyhydroxyalkanoates production from synthetic waste using Pseudomonas pseudoflava polyhydroxyalkanoate synthase enzyme activity
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