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1.
ChemSusChem ; 11(5): 881-887, 2018 03 09.
Artigo em Inglês | MEDLINE | ID: mdl-29446547

RESUMO

Cu is a unique catalyst for CO2 electroreduction, since it can catalyze CO2 reduction to a series of hydrocarbons, alcohols, and carboxylic acids. Nevertheless, such Cu catalysts suffer from poor selectivity. High pressure of CO2 is considered to facilitate the activity and selectivity of CO2 reduction. Herein, a new strategy is presented for CO2 reduction with improved C2 H4 selectivity on a Cu catalyst by using CO2 capture materials as the support at ambient pressure. N-doped carbon (Nx C) was synthesized through high-temperature carbonization of melamine and l-lysine. We observed that the CO2 uptake capacity of Nx C depends on both the microporous area and the content of pyridinic N species, which can be controlled by the carbonization temperature (600-800 °C). The as-prepared CuO/Nx C catalysts exhibit a considerably higher C2 H4 faradaic efficiency (36 %) than CuO supported on XC-72 carbon black (19 %), or unsupported CuO (20 %). Moreover, there is a good linear relationship between the C2 H4 faradaic efficiency and CO2 uptake capacity of the supports for CuO. The local high CO2 concentration near Cu catalysts, created by CO2 capture materials, was proposed to increase the coverage of CO intermediate, which is favorable for the coupling of two CO units in the formation of C2 H4 . This study demonstrates that pairing Cu catalysts with CO2 capture supports is a promising approach for designing highly effective CO2 reduction electrocatalysts.


Assuntos
Dióxido de Carbono/química , Cobre/química , Técnicas Eletroquímicas/métodos , Álcoois/síntese química , Ácidos Carboxílicos/síntese química , Catálise , Etilenos/química , Hidrocarbonetos/síntese química , Oxirredução , Temperatura
2.
J Zhejiang Univ Sci B ; 15(2): 143-52, 2014 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-24510707

RESUMO

This study investigated the effect of heat treatment combined with acid and alkali on the angiotensin-I-converting enzyme (ACE) inhibitory activity of peptides derived from bovine casein. The free amino group content, color, and cytotoxicity of the peptides were measured under different conditions. When heated at 100 °C in the pH range from 9.0 to 12.0, ACE inhibitory activity was reduced and the appearance of the peptides was significantly darkened. After thermal treatment in the presence of acid and alkali, the free amino group content of ACE inhibitory peptides decreased markedly. High temperature and prolonged heating also resulted in the loss of ACE inhibitory activity, the loss of free amino groups, and the darker coloration of bovine casein-derived peptides. However, ACE inhibitory peptides, within a concentration range of from 0.01 to 0.2 mg/ml, showed no cytotoxicity to Caco-2 and ECV-304 cell lines after heat treatment. This indicated that high temperature and alkaline heat treatment impaired the stability of bovine casein-derived ACE inhibitory peptides.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/química , Caseínas/química , Peptídeos/química , Peptidil Dipeptidase A/química , Animais , Células CACO-2 , Bovinos , Linhagem Celular Tumoral , Sobrevivência Celular , Temperatura Alta , Humanos , Concentração de Íons de Hidrogênio , Hidrólise
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