In this work, heat transfer of a fluid containing nanoparticles of aluminum oxide with the water volume fraction (0.1-0.3) percent has been reported. Heat transfer of the fluid containing nano water aluminum oxide with a diameter of about 20 nm in a horizontal double pipe counter flow heat exchanger under turbulent flow conditions was studied. The results showed that the heat transfer of nanofluid in comparison with the heat transfer of fluid is slightly higher than 12 percent.

A novel nanocatalyst was developed based on covalent surface functionalization of MCM‐41 with polyethyleneimine (PEI) using [3‐(2,3‐Epoxypropoxy)propyl] trimethoxysilane (EPO) as a cross‐linker. Amine functional groups on the surface of MCM‐41 were then conjugated with iodododecane to render an amphiphilic property to the catalyst. Palladium (II) was finally immobilized onto the MCM‐41@PEI‐dodecane and the resulted MCM‐41@aPEI‐Pd nanocatalyst was characterized by FT‐IR, TEM, ICP‐AES and XPS. Our designed nanocatalyst with a distinguished core‐shell structure and Pd2+ ions as catalytic centers was explored as an efficient and recyclable catalyst for Heck and oxidative boron Heck coupling reactions. In Heck coupling reaction, the catalytic activity of MCM‐41@aPEI‐Pd in the presence of triethylamine as base led to very high yields and selectivity. Meanwhile, the MCM‐41@aPEI‐Pd as the first semi‐heterogeneous palladium catalyst was examined in the C‐4 regioselective arylation of coumarin via the direct C‐H activation and the moderate to excellent yields were obtained toward different functional groups. Leaching test indicated the high stability of palladium on the surface of MCM‐41@aPEI‐Pd as it could be recycled for several runs without significant loss of its catalytic activity.

This paper refers to the Overall Heat Transfer Coefficient of Nano Fluids (OHTCNF) in heat exchangers and the relevant effective parameters. An improvement in Heat Transfer (HT) and OHTCNF containing nanoaluminum oxide with ca. 20 nm particle size and particular volume fraction in the range of 0.001-0.002 has been reported. The effects of temperature and concentration of nanoparticles on HT variation as well as Overall Heat Transfer Coefficient (OHTC) in a countercurrent double tube heat exchanger with turbulent flow have been studied. The experimental results show a remarkable 8%–10% rise in the mean HT and the OHTC. Accordingly, with an increase in the processing temperature and/or particle concentration the OHTC was observed to increase.

Recombinant human factor VII (rh-FVII) is produced by engineered BHK cells at low dose. Accordingly, establishment of a precise method is crucial to reliably measuring expression level of this protein during manufacturing pro-cesses. We developed and established a reproducible sandwich enzyme-linked immunosorbent assay (ELISA) method for measuring amount of FVII during biopharmaceutical in upstream and downstream processes of Aryo-Seven. A sandwich ELISA was designed using two different high affinity mon-oclonal antibodies (mAb1 and mAb2) against h-FVII. The bounded FVII to the first antibody was revealed by the use of a second mouse anti-FVII monoclo-nal antibody (1F1-B11), labeled with HRP that binds to another antigenic determinant of the FVII. Then, validation was done by determination of spec-ificity, linearity, accuracy, precision, reproducibility, detection and quantifica-tion limit and robustness according to ICH Q2 (R1) guideline. In developed ELISA, no interference was found between FVII and proteins derived from BHK which commonly exist in the supernatant. Linear range of detection was from 25-1.56 ng/mL with P-Value <0.001. In accuracy, spiked samples showed 109±2% recovery. Intra and intermediate precision assays showed %RSD not more than20. Detection limit of this assay was 0.99 ng /mL and limit of quantification was 2.99 ng/ml. The sandwich ELISA was found to be useful tool for measuring FVII/ FVIIa. The ELISA approach was precise, repro-ducible, and accurate. The ELISA therefore, is offered as an assured kit for detection of recombinant human factor.