Acetivibrio thermocellus JW20 strain:DSM 4150
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA28257 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| ABVG02.dat.gz | Other | |||
| ABVG02.fasta.gz | Fasta.gz | |||
| ABVG02.master.dat | Other | |||
| ABVG02.dat.gz | Other |
Items per page: 5 1 - 4 of 4 |
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Project description:Thermophilic cellulose degrading bacterium
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Project description:Enzymes' uncharacterised side activities can have significant effects on reaction products and yields. Hence, their identification and characterisation are crucial for the development of successful reaction systems. Here, we report the presence of feruloyl esterase activity in CtXyn5A from Acetivibrio thermocellus, besides its well-known arabinoxylanase activity, for the first time. Activity analysis of enzyme variants mutated in the catalytic nucleophile, Glu279, confirmed removal of all activity for E279A and E279L, and increased esterase activity while removing xylanase activity for E279S, thus allowing the proposal that both reaction types are catalysed in the same active site in two subsequential steps. The ferulic acid substituent is cleaved off first, followed by hydrolysis of the xylan backbone. The esterase activity on complex carbohydrates was found to be higher than that of a designated ferulic acid esterase (E-FAERU). Therefore, we conclude that the enzyme exhibits a dual function rather than an esterase side activity.
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Project description:Crystalline chitin is a kind of high molecular-weight polymers which is difficult to degrade. N-acetylglucosamine and chitooligosaccharides (COSs) are important agriculture, medicine, cosmetics and food resources. Conversion of crystalline chitin to GlcNAc and COSs using recombinant chitinases is an environmentally compatible, reproducible and products controllable method. Here, we report the ability of Pseudoalteromonas flavipulchra DSM 14401 to degrade crystalline.
2022-04-04 | PXD030600 | Pride
Project description:Transcriptomic analysis of Clostridium thermocellum ATCC 27405 cellulose fermentation
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Project description:Ruminiclostridium thermocellum DSM 1313 strain adhE*(EA) expression was studied along with ∆hydG and ∆hydG∆ech mutants strains deposited under GSE54082. All strains have been described in a study entitled Elimination of hydrogenase post-translational modification blocks H2 production and increases ethanol yield in Clostridium thermocellum. Biswas, et .al. Biotechnology for Biofuels 2015 8:20 Ruminiclostridium (Clostridium) thermocellum is a leading candidate organism for implementing a consolidated bioprocessing (CBP) strategy for biofuel production due to its native ability to rapidly consume cellulose and its existing ethanol production pathway. C. thermocellum converts cellulose and cellobiose to lactate, formate, acetate, H2, ethanol, amino acids, and other products. Elimination of the pathways leading to products such as H2 could redirect carbon flux towards ethanol production. Rather than delete each hydrogenase individually, we targeted a hydrogenase maturase gene (hydG), which is involved in converting the three [FeFe] hydrogenase apoenzymes into holoenzymes by assembling the active site. This functionally inactivated all three Fe-Fe hydrogenases simultaneously, as they were unable to make active enzymes. In the ∆hydG mutant, the [NiFe] hydrogenase-encoding ech was also deleted to obtain a mutant that functionally lacks all hydrogenase. The ethanol yield increased nearly 2-fold in ∆hydG∆ech compared to wild type, and H2 production was below the detection limit. Interestingly, ∆hydG and ∆hydG∆ech exhibited improved growth in the presence of acetate in the medium. Transcriptomic and proteomic analysis reveal that genes related to sulfate transport and metabolism were up-regulated in the presence of added acetate in ∆hydG, resulting in altered sulfur metabolism. Further genomic analysis of this strain revealed a mutation in the bi-functional alcohol/aldehyde dehydrogenase adhE gene, resulting in a strain with both NADH- and NADPH-dependent alcohol dehydrogenase activities, whereas the wild type strain can only utilize NADH. This is the exact same adhE mutation found in ethanol-tolerant C. thermocellum strain E50C, but ∆hydG∆ech is not more ethanol tolerant than the wild type. Targeting protein post-translational modification is a promising new approach to target multiple enzymes simultaneously for metabolic engineering. This GEO study pertains to expression profiles generated for C. thermocellum DSM 1313 strain adhE*(EA)
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Project description:Global gene expression patterns in Clostridium thermocellum from microarray analysis of chemostat culture on cellulose or cellobiose
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Project description:Hungateiclostridium thermocellum DSM 1313 genome sequencing
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Project description:Characterization of lactic acid and acetic acid mutants in batch fermentation
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Project description:Improved growth of Clostridium thermocellum AG553 via medium supplementation with formate and strain evolution
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