5 research outputs found

    Table1_Porous single-crystalline molybdenum nitride enhances electroreduction of nitrogen to ammonia.DOCX

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    The industrial ammonia synthesis reaction has the disadvantage of large energy consumption; thus, the electrochemical reduction method of ammonia synthesis characterized by its clean nature and environmental protectiveness has received extensive attention. Molybdenum nitride is a commonly used electrocatalyst for ammonia synthesis, and its Faraday efficiency is low, which may be due to many internal grain boundaries and few active sites. In this work, we grow microscale porous Mo2N single crystals and polycrystalline Mo2N from non-porous MoO3 single crystals. Porous molybdenum nitride materials facilitate charge transport in grain boundaries due to their single-crystal nature and enhance the catalytic properties of ammonia synthesis reactions. Compared with polycrystalline Mo2N, the porous Mo2N single crystal shows better performance, with a high NH4+ yield of 272.56 μg h−1 mg−1 and a Faradaic efficiency of 7.3%. In addition, the porous Mo2N single crystal exhibits superior long-term stability with little attenuation after 16 h electrolysis reaction. It provides a new method for the catalyst of ammonia synthesis.</p

    Quantitative Phosphoproteome of Infant Formula: New Insights into the Difference of Phosphorylation in Milk Proteins between Bovine and Goat Species

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    Phosphorylation is a broad post-translational protein modification, and the level of phosphorylation of milk proteins is associated with lactation, coagulation properties, and digestibility. However, phosphoproteins in bovine milk-based and goat milk-based infant formula have not been systematically explored. Here, we have analyzed six bovine and six goat milk-based infant formula using a quantitative phosphoproteomics approach, from which we identified 200 phosphoproteins with 276 phosphorylation sites and 156 phosphorylation sites from 75 phosphoproteins, respectively. Of these, 99 phosphorylation sites from 26 shared phosphoproteins were differentially expressed between bovine and goat milk-based infant formula. Especially, CSN1S1 was the most phosphoprotein with 25 quantified phosphorylation sites. Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) analyses showed that the identified phosphoproteins not only provide nutrition to the infant but also have anti-inflammatory, antipathogenic, and other biological functions. Our results shed light on the composition, phosphorylation sites, and biological functions of phosphoproteins in bovine milk and goat milk-based infant formula, which provide new insights into the key role of protein modifications during infant development. It also helps us to better understand the differences in digestibility of infant formula from different animal milk sources and thus guides the choice of milk source for infant formula

    Quantitative Phosphoproteome of Infant Formula: New Insights into the Difference of Phosphorylation in Milk Proteins between Bovine and Goat Species

    No full text
    Phosphorylation is a broad post-translational protein modification, and the level of phosphorylation of milk proteins is associated with lactation, coagulation properties, and digestibility. However, phosphoproteins in bovine milk-based and goat milk-based infant formula have not been systematically explored. Here, we have analyzed six bovine and six goat milk-based infant formula using a quantitative phosphoproteomics approach, from which we identified 200 phosphoproteins with 276 phosphorylation sites and 156 phosphorylation sites from 75 phosphoproteins, respectively. Of these, 99 phosphorylation sites from 26 shared phosphoproteins were differentially expressed between bovine and goat milk-based infant formula. Especially, CSN1S1 was the most phosphoprotein with 25 quantified phosphorylation sites. Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) analyses showed that the identified phosphoproteins not only provide nutrition to the infant but also have anti-inflammatory, antipathogenic, and other biological functions. Our results shed light on the composition, phosphorylation sites, and biological functions of phosphoproteins in bovine milk and goat milk-based infant formula, which provide new insights into the key role of protein modifications during infant development. It also helps us to better understand the differences in digestibility of infant formula from different animal milk sources and thus guides the choice of milk source for infant formula

    Highly Efficient CO<sub>2</sub> Electrolysis on Cathodes with Exsolved Alkaline Earth Oxide Nanostructures

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    The solid oxide CO<sub>2</sub> electrolyzer has the potential to provide storage solutions for intermittent renewable energy sources as well as to reduce greenhouse gas emissions. One of the key challenges remains the poor adsorption and activity toward CO<sub>2</sub> reduction on the electrolyzer cathode at typical operating conditions. Here, we show a novel approach in tailoring a perovskite titanate (La, Sr)­TiO<sub>3+δ</sub> cathode surface, by the <i>in situ</i> growing of SrO nanoislands from the host material through the control of perovskite nonstoichiometry. These nanoislands provide very enhanced CO<sub>2</sub> adsorption and activation, with stability up to 800 °C, which is shown to be in an intermediate form between carbonate ions and molecular CO<sub>2</sub>. The activation of adsorbed CO<sub>2</sub> molecules results from the interaction of exsolved SrO nanoislands and the defected titanate surface as revealed by DFT calculations. These cathode surface modifications result in an exceptionally high direct CO<sub>2</sub> electrolysis performance with current efficiencies near 100%
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