CeO2/Pd Nanoparticles Incorporated Fly Ash Zeolite: An Efficient and Recyclable Catalyst for Csp2-Csp2 Bond Formation Reactions

The catalytic activity of CeO₂ and palladium nanoparticles supported fly ash zeolite (CeO₂/Pd@FAZ) for C_sp²-C_sp² bond formation was studied. CeO₂/Pd@FAZ was characterized by FTIR, XRD, EDAX and TEM studies. In the Suzuki-Miyauracross-coupling reaction, biphenyl derivatives with excellent yields were obtained, and the reaction conditions were optimized. The catalytic activity was explored using a wide variety of diversely substituted aryl bromides and chlorides with aryl boronic acid under optimized reaction conditions. The recyclability of the catalyst was established for three cycles, with the conversion rate from 99 to 40%, which gained the advantage of heterogeneous catalysis.     

Numerical investigation of flow boiling characteristics of water in a rectangular microchannel

Journal of Thermal Analysis and Calorimetry - In the case of flow boiling, the prediction of vapour fraction in the horizontal microchannel is a severe issue using the numerical technique....     

Purification of a Lectin from M. rubra Leaves Using Immobilized Metal Ion Affinity Chromatography and Its Characterization

Lectins represent a heterogeneous group of proteins/glycoproteins with unique carbohydrate specificity, with wide range of biomedical applications. The multi-step purification protocols generally used for purification of lectin result in a significant reduction in the final yield and activity. In the present study, Morus rubra lectin (MRL) was purified to homogeneity from the leaves using a single-step immobilized metal ion affinity chromatography (IMAC) procedure. The approximate molecular weight of purified MRL resolved as a single band on SDS-PAGE was 52?kDa. Final percentage yield of purified lectin by IMAC was calculated as 74.7?%. Purified MRL was specific to three sugars, galactose, d-galactosamine and N-acetyl-d-galactosamine, and rendered haemagglutination (HA) activity towards different human blood group RBCs. MRL showed stability over a wide range of temperature (up to 80?°C) and pH (4?C11). Chelation of the lectin with EDTA did not alter HA which indicates that metal ion is not required for activity. In the presence of Fe²⁺, Ca²⁺, Zn²⁺, Ni²⁺, Mn²⁺, Na⁺ and K⁺, HA activity was reduced to 50?%, whereas the presence of trivalent metal ions (Fe3⁺ and Al³⁺) and Cu²⁺ did not affect the activity. In the presence of Mg²⁺ and Hg²⁺, only 25?% of HA activity remained.