The
thermodynamics on the direct synthesis of dimethyl carbonate
(DMC) from CO2 and CH3OH was calculated and
analyzed. Using Y(NO3)3·6H2O
as the precursor, a series of Y2O3 were prepared
through the one-pot calcination method, which were employed to catalyze
DMC synthesis. The decomposition temperature of Y(NO3)3·6H2O was measured by thermogravimetric analysis,
and Y2O3 was obtained after the precursor calcination
at desired temperatures, denoted as Y2O3-T (°C). The catalysts were characterized by X-ray diffraction,
Brunauer–Emmett–Teller method, transmission electron
microscopy, NH3/CO2 temperature-programmed desorption,
and X-ray photoelectron spectroscopy to detect the crystal phase,
surface property, particle size, acidity–basicity amounts,
and oxidation state, respectively. The characterization results indicated
that Y2O3-750 can favor the formation of moderate
acidic and basic sites and facilitate the activation of CO2 and CH3OH. The catalytic performance evaluation was experimentally
investigated, and Y2O3-750 owned the highest
DMC yield of 1.02 mmol/g·cat under 90 °C, 8 MPa, and 6 h,
which also exhibited reliable recycle ability.
Rotaviruses (RVsR otaviruses (RVs) are the major causative agents of acute gastroenteritis in young children and animals worldwide (1). The RV genome contains 11 segments of double-stranded RNA encoding 12 proteins: six structural proteins (VP1, VP2, VP3, VP4, VP6, and VP7) and six nonstructural proteins (NSP1 to NSP6) (2). RVs are classified into 8 species (A to H) by the antigenicity of the VP6 protein (3). Group A rotavirus (RVA) is a major cause of human RV-associated gastroenteritis (4). RVA can be classified into various G and P types on the basis of glycoprotein VP7 and protease-sensitive VP4, respectively. To date, at least 27 G and 35 P genotypes have been reported (5). The fact that the segmented genome undergoes point mutations, reassortment, and gene rearrangements accounts for the large genetic diversity of RVs (1).VP4 can be cleaved by protease to yield N-terminal VP8* and C-terminal VP5* (6). VP8* includes the VP4 spike head and is reported to bind to cell surface glycans essential for cell invasion (7). The ability of a virus to invade host cells is crucial for its replication, host tropism, and pathogenicity. Notably, VP8* is the most variable domain. VP8* proteins of sialidase-sensitive RVs were reported to interact with sialic acids (Sia) (8); however, most animal RVs and almost all human RVs were sialidase insensitive (9). It was noted that many of the sialidase-insensitive RVA strains interact with Sia at subterminal sites of glycoprotein receptors (10). Recently, histo-blood group antigens (HBGAs) have been reported to be attachment factors for human RVs by interacting with VP8* (11,12). HBGAs are a group of carbohydrates present on the surfaces of red blood cells and mucosal epithelia and as free oligosaccharides in saliva, blood, and milk (13).Previous studies by oligosaccharide and saliva binding assays showed that P
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