Investigation in thorium phosphate by NMR II-phosphorus dipolar networks

With through space and through bond experiments in two-dimensional NMR we analyze the transformation from the thorium phosphate-hydrogen phosphate hydrate (TPHPH) to the β form of the thorium phosphate diphosphate (β-TPD) in relation with the phosphorus networks. These techniques are complementary: the through space coupling gives an insight on the dipolar phosphorus networks while the through bond coupling is particularly efficient in the detection of the P₂O₇ groups. With these experiments we show that in a first step, by heating the precursor TPHPH above 250 °C, it transforms into an form of TPD. This transformation is due to the complete condensation of hydrogen phosphate groups HPO₄ into P₂O₇ entities. By heating -TPD above 950 °C it transforms into its well-known β form. The form is characterized by a hygroscopic behavior: some water molecules are present near the P₂O₇ groups that makes non-equivalent their phosphorus nuclei. PO₄ dipolar networks are always present in the form. The main effect of these PO₄ and P₂O₇ units is to give the system a channel structure and the water enters in them.     

Recent developments of metallic nanoparticles and their catalytic activity in organic reactions

During the last two decades, with the development of nanotechnology, various nanomaterials have been designed and generated. Among them, hybrid organic–inorganic nanoparticles as a particular immobilizing carrier of the catalyst active sites have shown an important contribution in the current research studies. This is due to the large area and loads of active sites. This prominent review is focused on the novel various exa about the immobilization of nanoparticles with organic compounds as versatile and efficient catalysts in organic syntheses.     

Thermal Stability of Immobilised α-chymotrypsinogen

The unfolding of α-chymotrypsinogen covalently immobilized on silica beads has been studied by differential scanning calorimetry (DSC). The enzyme undergoes an unfolding transition which, unlike the free protein, cannot be approximated by a single two-state process. After immobilization, the unfolding is characterized by the presence of two partially overlapping transitions, both of them show two-state behavior. The two processes correspond to the separate unfolding of the two domains of the α-chymotrypsinogen molecule. The loss of cooperativity behavior is a consequence of the covalent immobilization. The two domains showed different thermal stability as functions of pH. One of them unfolded with a transition temperature T _m2 higher than T _m of the free enzyme, implying stabilization effect of immobilization. However, below pH 4.5, its native structure is lost. The other transition shows a remarkable pH-independent thermal stability from pH 2.5 to 7.0. This revised version was published online in July 2006 with corrections to the Cover Date.     

Structure and morphology controllable synthesis of Ag/carbon hybrid with ionic liquid as soft-template and their catalytic properties

Ag/carbon hybrids were fabricated by the redox of glucose and silver nitrate (AgNO₃) in the presence of imidazolium ionic liquid ([C₁₄mim]BF₄) under hydrothermal condition. Monodisperse carbon hollow sub-microspheres encapsulating Ag nanoparticles and Ag/carbon cables were selectively prepared by varying the concentration of ionic liquid. Other reaction parameters, such as reaction temperature, reaction time and the mole ratio of silver nitrate to glucose, play important roles in controlling the structures of the products. The products were characterized by XRD, TEM (HRTEM), SEM, energy-dispersive X-ray spectroscopy (EDX), FTIR spectroscopy and a Raman spectrometer. The possible formation mechanism was proposed. The catalytic property of the hybrid in the oxidation of 1-butanol by H₂O₂ was also investigated.     

Targeted Synthesis of Isomeric Naphthalene-Based 2D Kagome Covalent Organic Frameworks

Targeted synthesis of kagome ( kgm ) topologic 2D covalent organic frameworks remains challenging, presumably due to the severe dependence on building units and synthetic conditions. Herein, two isomeric “two-in-one” monomers with different lengths of substituted arms based on naphthalene core (p-Naph and m-Naph) are elaborately designed and utilized for the defined synthesis of isomeric kgm Naph-COFs. The two isomeric frameworks exhibit splendid crystallinity and showcase the same chemical composition and topologic structure with, however, different pore channels. Interestingly, C₆₀ is able to uniformly be encapsulated into the triangle channels of m-Naph-COF via in situ incorporation method, while not the isomeric p-Naph-COF, likely due to the different pore structures of the two isomeric COFs. The resulting stable C₆₀@m-Naph-COF composite exhibits much higher photoconductivity than the m-Naph-COF owing to charge transfer between the conjugated skeletons and C₆₀ guests.     

Size dependence of SiO2 particles enhanced glucose biosensor

A wide size range of SiO₂ particles were synthesized and were used as enzyme immobilization carriers to fabricate glucose biosensors. The size of the particles was in the range of 17-520 nm. These biosensors could be operated under physiological conditions (0.1 M phosphate buffer, pH 7.2). Particle size could affect the performance of SiO₂ modified glucose biosensors drastically. The smaller particles had higher performance. The smallest SiO₂ modified biosensor could work well in the glucose concentration range of 0.02-10 mM with a correlation coefficient of 0.9993. Its sensitivity was 2.08 μA/mM and the detection limit was 1.5 μM glucose.     

Preparation and characterization of mono-valent ion selective polypyrrole composite ion-exchange membranes

Polypyrrole composite cation- and anion-exchange membranes (CEM and AEM), in which polypyrrole (PPY) coated on one surface of the membrane as a thin layer, were prepared by chemical polymerization of pyrrole in the presence of high oxidant concentration (Na₂S₂O₈). Existence of polypyrrole layer on the both types of ion-exchange membranes were confirmed by recording their coating density, SEM images and conductivity. These membranes were extensively characterized by recording their properties such as water uptake, ion-exchange capacity, contact angle, permselectivity and membrane conductivity as a function of polymerization time such as. It was observed that due to coating of PPY for 2 h, membrane permselectivity of CEM for NaCl (0.907) was reduced to 0.873, while it was increased from 0.747 to 0.889 in the case of AEM. Similar behaviors were also obtained for bi-valent electrolytes. Electrodialysis experiments were also conducted with polypyrrole composite ion-exchange membranes using mixed electrolytic systems. Relative dialytic rates for NaCl with respect to other bi-valent electrolyte were varied in between 5 and 8 (depending on bi-valent electrolyte), which suggested the feasible and efficient separation of mono-valent from bi-valent electrolyte. Slower electro-migration of bi-valent electrolyte (CaCl₂, MgCl₂ and CuCl₂) in comparison to NaCl was explained on the basis of synergetic effect of sieving of bulkier bi-valent cations by tight and rigid polypyrrole layer and the difference in electrostatic and hydrophobic–hydrophilic repulsion force between bi-valent cations and mono-valent cation. It was concluded that these composite membranes are suitable for the efficient separation of same type of charged ions by electro-driven separation techniques.     

Development of core–shell structure Fe3O4@Ta2O5 microspheres for selective enrichment of phosphopeptides for mass spectrometry analysis

Protein phosphorylation is one of the most important post-translational modifications. Due to the dynamic nature and low stoichiometry of the protein phosphorylation, enrichment of phosphopeptides from proteolytic mixtures is often necessary prior to their characterization by mass spectrometry. Many metal oxides such as titanium dioxide and zirconium dioxide have been successfully applied to isolation and enrichment of phosphopeptides. Recently, niobium pentoxide was proved to have the ability for selective enrichment of phosphopeptides. Considering the proximity of tantalum to niobium, we supposed that Ta₂O₅ can be used as affinity probes for phosphopeptide enrichment. In the work, we synthesized Fe₃O₄@Ta₂O₅ magnetic microspheres with core–shell structure for selective enrichment of phosphopeptides. To demonstrate its ability for selective enrichment of phosphopeptides, we applied Fe₃O₄@Ta₂O₅ magnetic microspheres to isolation and enrichment of the phosphopeptides from tryptic digestion of standard proteins and real samples, and then the enriched peptides were analyzed by matrix-assisted laser desorption mass spectrometry analysis (MALDI-MS) or liquid chromatography coupled to electrospray ionization mass spectrometry (LC–ESI-MS). Experiment results demonstrate that Ta₂O₅ coated-magnetic microspheres show the excellent potential for selective enrichment of phosphopeptides.     

A mild hydrolysis of esters mediated by lithium salts

When treated with amine bases such as triethylamine and various lithium salts in wet solvents, esters are efficiently hydrolyzed to the corresponding acids in good yields. Esters incorporating an α- or β-heteroatom with respect to the ester carbonyl group are hydrolyzed rapidly even at room temperature. To further demonstrate the usefulness of this method, one example is provided where hydrolysis of acetylated camphorsultam is mediated by LiBr.     

Characterization of immobilized nuclease P1

To improve the efficiency of the use of nuclease P1, enzyme immobilization technology was applied using nuclease P1. Characterization of immobilized nuclease P1 on different supports was studied. The results showed that the optimum pH and temperature of nuclease P1 immobilized via different supports were enhanced. The immobilized enzyme was obviously stable when stored for long periods and was reusable. The best results were obtained when nuclease P1 was immobilized on chitosan nanoparticles. The nanoparticles were applied to protect the activity of nuclease P1 and improved enzyme activity by 13.17% over that of free nuclease P1 at the same conditions. The Michaelis constant Km and V _max were determined for free and immobilized enzyme as well.