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7 results for “Alcohol dehydrogenase”
Heterogeneous Biocatalytic Reduction of 5-(Hydroxy)methyl Furfural Using two Co-immobilised Alcohol Dehydrogenases
<p>Biocatalyst heterogenisation may enable robust processes that can be applied in biorefineries to selectively valorise highly functionalised platform chemicals. In this work, we co-immobilise two dehydrogenases and successfully apply them in the selective reduction of 5-hydroxymethylfurfural (HMF) to 2,5-bis(hydroxymethyl) furan (BHMF) with efficient <em>in situ</em> cofactor regeneration. First, we select the best enzyme candidates (an alcohol dehydrogenase from <em>Escherichia coli</em> together with a thermostable glucose dehydrogenase from <em>Bacillus subtilis</em>) and then screen a variety of carriers and chemistries to find the optimal individual immobilisation protocols for each dehydrogenase. As a result, methacrylate carriers (Purolite™) functionalised with either aldehydes or with epoxy and cobalt-chelate groups co-immobilise both enzymes in high yields with a sufficient activity recovery (>20%). These optimal heterogeneous biocatalysts enable the quantitative bio-reduction of HMF to BHMF with >99% selectivity in only fifteen minutes, exhibiting an outstanding reusability of >15 batch cycles with a total volumetric productivity of ∼5 g L<sup>−1</sup> h<sup>−1</sup> of BHMF. Preliminary experiments on a semipreparative scale with HMF loadings of 40 mM also reach high product conversions (86%). Overall, the judicious selection of enzymes, carriers and reaction conditions enables the design of robust biocatalysts that may contribute to paving the way to the valorisation of highly functionalised chemicals in biorefineries.</p>
Computational Studies of Human Class V Alcohol Dehydrogenase - The Odd Sibling
<p>A number of class I-VI ADH protein sequences were obtained from the UniProt, NCBI protein database, and Ensembl databases in October 2015. The sequences were aligned using the L-INS-i approach of MAFFT 7.266.</p> <p>The tree was generated using Phyml release 20151210. In the published figure, the tree was visualised as a radial phylogram in Dendroscope 3.</p>
Alcohol dehydrogenase 1B emerged prominent in the carcinogenesis of oro- and hypopharyngeal cancers in Genome-Wide Study in areca-quid endemic area
GEO Series GSE218224. Homo sapiens. 698 samples. Type: SNP genotyping by SNP array.
Contrasting in vitro and in vivo methanol oxidation activities of lanthanide-dependent alcohol dehydrogenases XoxF1 and ExaF from Methylobacterium extorquens AM1
GEO Series GSE125593. Methylorubrum extorquens AM1. 5 samples. Type: Expression profiling by high throughput sequencing.
Interaction Between a Natural Aldehyde Dehydrogenase 2 (ALDH2) Inhibitor and Alcohol
ClinicalTrials.gov study NCT02309801. IPD Sharing: Not stated. Countries: 1. Publications: 0.
Comparison between wild type E. coli and adhE (alcohol dehydrogenase) mutants, grown under anaerobic condition
GEO Series GSE46455. Escherichia coli O157:H7 str. EDL933; Escherichia coli CFT073; Escherichia coli O157:H7 str. Sakai; Escherichia coli str. K-12 substr. MG1655; Escherichia coli BW25113; Escherichia coli BL21(DE3). 4 samples. Type: Expression profiling by array.
Paracardial fat remodeling affects systemic metabolism through alcohol dehydrogenase 1.
GEO Series GSE162779. Mus musculus. 7 samples. Type: Expression profiling by array.
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