Styrene epoxidation with hydrogen peroxide over calcium oxide catalysts prepared from various precursors

A series of CaO samples were prepared by calcination of commercially available and synthesis of calcium salt precursors such as calcium acetate, carbonate, hydroxide and oxalate etc. CaO samples were found to be effective for the epoxidation of styrene using hydrogen peroxide as an oxidant in the presence of acetonitrile. To determine the influence of the physicochemical properties and surface basicity on the catalytic activity, the prepared CaO samples were characterized using thermogravimetry （TG）, X-ray diffraction （XRD）, scanning electron microscopy （SEM）, N2-adsorption and temperature-programmed desorption of CO2 （CO2-TPD）. The results indicate that the amounts of very strong basic sites and high basicity strength on CaO sample are key factors for its excellent catalytic performance. In contrast, the surface area, porosity and the surface structure of CaO sample have a relatively minor effect on the catalytic activity. CaO sample, obtained by the decomposition of Ca（OH）2, prepared by precipitating calcium nitrate with sodium hydroxide in ethylene glycol solution, exhibits the highest amount of very strong basic sites and stronger strength of basic sites, and therefore it catalyses the epoxidation of styrene with the highest rate among the tested CaO samples. Under the selected reaction conditions, the selectivity of 97.5% to styrene oxide at a conversion in excess of 99% could be obtained.

Analysis of the induction of the myelin basic protein binding to the plasma membrane phospholipid monolayer

Myelin basic protein（MBP） is an essential structure involved in the generation of central nervous system（CNS）myelin.Myelin shape has been described as liquid crystal structure of biological membrane.The interactions of MBP with monolayers of different lipid compositions are responsible for the multi-lamellar structure and stability of myelin.In this paper,we have designed MBP-incorporated model lipid monolayers and studied the phase behavior of MBP adsorbed on the plasma membrane at the air/water interface by thermodynamic method and atomic force microscopy（AFM）.By analyzing the pressure–area（π–A） and pressure–time（π–T） isotherms,univariate linear regression equation was obtained.In addition,the elastic modulus,surface pressure increase,maximal insertion pressure,and synergy factor of monolayers were detected.These parameters can be used to modulate the monolayers binding of protein,and the results show that MBP has the strongest affinity for 1,2-dipalmitoyl-sn-glycero-3-phosphoserine（DPPS） monolayer,followed by DPPC/DPPS mixed and1,2-dipalmitoyl-sn-glycero-3-phospho-choline（DPPC） monolayers via electrostatic and hydrophobic interactions.AFM images of DPPS and DPPC/DPPS mixed monolayers in the presence of MBP（5 n M） show a phase separation texture at the surface pressure of 20 m N/m and the incorporation of MBP put into the DPPC monolayers has exerted a significant effect on the domain structure.MBP is not an integral membrane protein but,due to its positive charge,interacts with the lipid head groups and stabilizes the membranes.The interaction between MBP and phospholipid membrane to determine the nervous system of the disease has a good biophysical significance and medical value.