48 research outputs found
Comparison of experimental results from three dual fluidized bed test facilities capturing CO2 with CaO
10th International Conference on Greenhouse Gas Control Technologies[EN] Postcombustion CO2 capture technologies using CaO as a regenerable solid sorbent have emerged as a promising route to reduce the electricity penalty and the cost of CO2 capture from flue gases of both new and existing fossil fuelled power plants. Rapid progress is taking place in the understanding of these processes at different levels. However, experimental information, validating the concept under continuous operating conditions similar to those expected for large-scale application, remain scarce. We present here a comparative analysis of the results obtained in three laboratory-scale dual fluidized bed (DFB) test facilities in Spain, Germany and Canada. The test facilities range from 10 to 75 kWth with riser heights between 4.5 and 12.4 m. They have been operated to capture CO2 with CaO from simulated flue gases in the bubbling, turbulent and fast fluidization fluid-dynamic regimes. The carbonator reactors are interconnected with regenerators, where the CaCO3 decomposition has been conducted continuously and semi-continuously, operated in both air-combustion and oxy-combustion modes. Many stationary and non-stationary states have been achieved at different combinations of the key operating parameters (e.g. calcium looping ratio). All DFB test facilities showed a carbon balance closure of high quality in most tests. The trends of CO2 capture efficiency with respect to operating conditions and sorbent characteristics are compared and a discussion is made on the most appropriate methodology to conduct future tests under a joint new FP7 project (CaOling) that aims at the rapid scaling up of the calcium looping technology.This work is being funded by the European Commision 7th Framework Programme under the CaOling Project.Peer reviewe
Biotransformation of benzonitrile herbicides via the nitrile hydratase–amidase pathway in rhodococci
Abstract
The aim of this work was to determine the ability of rhodococci to transform 3,5-dichloro-4-hydroxybenzonitrile (chloroxynil), 3,5-dibromo-4-hydroxybenzonitrile (bromoxynil), 3,5-diiodo-4-hydroxybenzonitrile (ioxynil) and 2,6-dichlorobenzonitrile (dichlobenil); to identify the products and determine their acute toxicities. Rhodococcus erythropolis A4 and Rhodococcus rhodochrous PA-34 converted benzonitrile herbicides into amides, but only the former strain was able to hydrolyze 2,6-dichlorobenzamide into 2,6-dichlorobenzoic acid, and produced also more of the carboxylic acids from the other herbicides compared to strain PA-34. Transformation of nitriles into amides decreased acute toxicities for chloroxynil and dichlobenil, but increased them for bromoxynil and ioxynil. The amides inhibited root growth in Lactuca sativa less than the nitriles but more than the acids. The conversion of the nitrile group may be the first step in the mineralization of benzonitrile herbicides but cannot be itself considered to be a detoxification
The effects of liraglutide in mice with diet-induced obesity studied by metabolomics
Liraglutide is the glucagon-like peptide-1 receptor agonist widely used for the treatment of type 2 diabetes mellitus. Recently, it has been demonstrated to decrease cardiovascular morbidity and mortality in patients with type 2 diabetes and high cardiovascular risk. Although the major modes of liraglutide action are well-known, its detailed action at the metabolic level has not been studied. To this end, we explored the effect of 2-week liraglutide treatment in C57BL/6 male mice with obesity and diabetes induced by 13 weeks of high-fat diet using NMR spectroscopy to capture the changes in urine metabolic profile induced by the therapy. The liraglutide treatment decreased body and fat pads weight along with blood glucose and triglyceride levels. NMR spectroscopy identified 11 metabolites significantly affected by liraglutide treatment as compared to high-fat diet-fed control group. These metabolites included ones involved in nicotinamide adenine dinucleotide metabolism, β-oxidation of fatty acids and microbiome changes. Although majority of the metabolites changed after liraglutide treatment were similar as the ones previously identified after vildagliptin administration in a similar mouse model, the changes in creatinine, taurine and trigonelline were specific for liraglutide administration. The significance of these changes and its possible use in the personalization of antidiabetic therapy in humans requires further research
Tailored Multivalent Neo-Glycoproteins: Synthesis, Evaluation, and Application of a Library of Galectin-3-Binding Glycan Ligands
The β-<i>N</i>-Acetylhexosaminidase in the Synthesis of Bioactive Glycans: Protein and Reaction Engineering
N-Acetylhexosamine oligosaccharides terminated with GalNAc act as selective ligands of galectin-3, a biomedically important human lectin. Their synthesis can be accomplished by β-N-acetylhexosaminidases (EC 3.2.1.52). Advantageously, these enzymes tolerate the presence of functional groups in the substrate molecule, such as the thiourea linker useful for covalent conjugation of glycans to a multivalent carrier, affording glyconjugates. β-N-Acetylhexosaminidases exhibit activity towards both N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) moieties. A point mutation of active-site amino acid Tyr into other amino acid residues, especially Phe, His, and Asn, has previously been shown to strongly suppress the hydrolytic activity of β-N-acetylhexosaminidases, creating enzymatic synthetic engines. In the present work, we demonstrate that Tyr470 is an important mutation hotspot for altering the ratio of GlcNAcase/GalNAcase activity, resulting in mutant enzymes with varying affinity to GlcNAc/GalNAc substrates. The enzyme selectivity may additionally be manipulated by altering the reaction medium upon changing pH or adding selected organic co-solvents. As a result, we are able to fine-tune the β-N-acetylhexosaminidase affinity and selectivity, resulting in a high-yield production of the functionalized GalNAcβ4GlcNAc disaccharide, a selective ligand of galectin-3
Two-Step Enzymatic Synthesis of β-d-N-Acetylgalactosamine-(1→4)-d-N-acetylglucosamine (LacdiNAc) Chitooligomers for Deciphering Galectin Binding Behavior
Towards Keratan Sulfate - Chemoenzymatic Cascade Synthesis of Sulfated N-Acetyllactosamine (LacNAc) Glycan Oligomers
Chemo-Enzymatic Synthesis of Branched N -Acetyllactosamine Glycan Oligomers for Galectin-3 Inhibition
Identifying Efficient Clostridium difficile Toxin A Binders with a Multivalent Neo-Glycoprotein Glycan Library
Biocatalyzed Reactions towards Functional Food Components 4-Alkylcatechols and Their Analogues
Catechols are antioxidants and radical scavengers with a broad medical potential. 4-Methylcatechol (1b) and 4-ethylcatechol (2b) (occurring in some traditional fermented and smoked foods) activate the cell defense against oxidative stress. We examined the biocatalyzed reactions towards 4-n-alkylcatechols with different side chains length, which is a factor important for the biological activities of catechols. 4-n-Alkylcatechols with methyl through heptyl side chains (1b–7b) were obtained in one pot by (i) oxidation of phenols 1a–7a with tyrosinase from Agaricus bisporus followed by (ii) reduction of ortho-quinones (intermediates) with L-ascorbic acid sodium salt. The conversions decreased with increasing side chain length. The preparative reactions were carried out with substrates 1a–5a. The isolated yields of the purified products decreased from 59% in 2b to 10% in 5b in correlation with logP of the substrates. Homology modeling indicated that the affinities of two tyrosinase isoforms (PPO3 and PPO4) to the substrates with side chains longer than C2 decreased with increasing side chain length. This was probably due to steric limitations and to missing interactions of the extended side chains in the active sites. We envisage using the model to predict further substrates of tyrosinase and testing the products, catechols, for radical-scavenging and biological activities