Zinc Oxide is widely used in many industrial sectors, ranging from photocatalysis, rubber, ceramics, pharmaceuticals, and pigments, food additives and cream. The global market is estimated USD annual 3600M, with global production of 10 Mt.
In the new application, the size and shape can be wise increase efficiency and market new nano-ZnO is taking the lead (USD annual 2000M with a capacity of 1 Mt and the expected compound annual growth rate of 20% / year). The purpose of this study was to investigate the possibility of producing nanoparticles of zinc oxide by way of the spinning disc reactor (SDR). A lab-scale spinning disc reactor, which was previously used to produce other nanomaterials such as hydroxyapatite or titania, has been investigated with the aim of producing a needle-shaped zinc oxide nanoparticles.
At the nanoscale and with this form, the zinc oxide particles showed their biggest photoactivity and active area, either increasing the efficiency photocatalysis and ultraviolet (UV) absorbance. Working on different operating conditions, such as on a different disk rotational speed, distance inlet from the center of the disk, the initial concentration of Zn precursor and an alkaline solution, and inlet solution reagent flow, under certain conditions, the size distribution of the unimodal and dimensions of an average of about 56 nm obtained.
Spinning disk reactor allowing continuous production of nanoparticles with a capacity of 57 kg / d, adopting the Zn-precursor concentration of 0.5 M and the inlets early discharge a total of 1 L / min. size of the product seems to be controlled, and the dimensions of the lower average (47 nm), adopted the initial precursor concentration of Zn-0.02 M and a total inlet flow-rate of 0.1 L / min, can be obtained, scarifying productivity (0.23 kg / d). In the end, spinning disk reactor qualify as an equipment-intensive processes for the production of zinc oxide nanoparticles targeted in terms of size.
ZnO Nano-Particles Production Intensification by Means of a Spinning Disk Reactor
intensification solubility studies and extraction of phenolic compounds and anthocyanins from Oryza sativa L. ‘Violet Nori’
Oryza sativa L. ‘Violet Nori’ is a spontaneous plant rice cultivars Italy purple aromatic very rich polyphenolic compounds, especially anthocyanins, that confer excellent antioxidant capacity.
This study aims to improve the extraction of antioxidant compounds in green strategy and it is divided into two steps. The first step is concerned solubility studies targeted polyphenols in different ethanol: water mixture by means of the theoretical prediction method, using a simulation program COSMO-RS, and then confirmation of the results of calculations by practical experiments.
After the best extraction mixture is identified, the second step of the work is done, with the aim of intensifying the extraction results. Therefore, various green innovative extraction techniques, including ultrasound, using both systems probes and ultrasonic bath, milling beads, microwave and accelerated solvent extraction tested and compared with conventional maceration.
Description: A polyclonal antibody for detection of IgD from Human. This IgD antibody is for IHC-P, ELISA. It is affinity-purified from rabbit serum by affinity-chromatography using the specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from part region of human IgD protein at amino acid sequence of 111-160
Description: A polyclonal antibody for detection of IgD from Human. This IgD antibody is for IHC-P, ELISA. It is affinity-purified from rabbit serum by affinity-chromatography using the specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from part region of human IgD protein at amino acid sequence of 111-160
Description: A polyclonal antibody for detection of IgD from Human. This IgD antibody is for IHC-P, ELISA. It is affinity-purified from rabbit serum by affinity-chromatography using the specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from part region of human IgD protein at amino acid sequence of 111-160
Description: Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through interchain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin D (IgD) exists as a monomer with light chains. It plays a biological role as a transmembrane receptor molecule, co-expressed with IgM on the surface of mature/naive B cells. In particular, it is found on spleen B cell surfaces. Compared to IgM, IgD exists in much lower numbers and is not expressed on immature B cells. IgD surface expression on B cells is regulated in part by IL-27. In mice, the inhibition of this immunoglobulin isotype does not cause a significant change to the immune system.
Description: Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through interchain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin D (IgD) exists as a monomer with light chains. It plays a biological role as a transmembrane receptor molecule, co-expressed with IgM on the surface of mature/naive B cells. In particular, it is found on spleen B cell surfaces. Compared to IgM, IgD exists in much lower numbers and is not expressed on immature B cells. IgD surface expression on B cells is regulated in part by IL-27. In mice, the inhibition of this immunoglobulin isotype does not cause a significant change to the immune system.
Description: Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through interchain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin D (IgD) exists as a monomer with light chains. It plays a biological role as a transmembrane receptor molecule, co-expressed with IgM on the surface of mature/naive B cells. In particular, it is found on spleen B cell surfaces. Compared to IgM, IgD exists in much lower numbers and is not expressed on immature B cells. IgD surface expression on B cells is regulated in part by IL-27. In mice, the inhibition of this immunoglobulin isotype does not cause a significant change to the immune system.
Description: A polyclonal antibody against ATF2 (Ab-69 or 51). Recognizes ATF2 (Ab-69 or 51) from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;WB:1:500-1:1000, IHC:1:50-1:200
Description: A polyclonal antibody against ATF2 (Ab-69 or 51). Recognizes ATF2 (Ab-69 or 51) from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;WB:1:500-1:1000, IHC:1:50-1:200
Description: A polyclonal antibody against ATF2 (Ab-73 or 55). Recognizes ATF2 (Ab-73 or 55) from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;WB:1:500-1:1000, IHC:1:50-1:200
Description: A polyclonal antibody against ATF2 (Ab-73 or 55). Recognizes ATF2 (Ab-73 or 55) from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;WB:1:500-1:1000, IHC:1:50-1:200
Description: A polyclonal antibody against ATF2 (Ab-62 or 44). Recognizes ATF2 (Ab-62 or 44) from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC, IF;WB:1:500-1:1000, IHC:1:50-1:200, IF:1:100-1:200
Description: A polyclonal antibody against ATF2 (Ab-62 or 44). Recognizes ATF2 (Ab-62 or 44) from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC, IF;WB:1:500-1:1000, IHC:1:50-1:200, IF:1:100-1:200
Description: A polyclonal antibody against ATF2 (Ab-71 or 53). Recognizes ATF2 (Ab-71 or 53) from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC, IF;WB:1:500-1:1000, IHC:1:50-1:200, IF:1:100-1:200
Description: A polyclonal antibody against ATF2 (Ab-71 or 53). Recognizes ATF2 (Ab-71 or 53) from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC, IF;WB:1:500-1:1000, IHC:1:50-1:200, IF:1:100-1:200
Description: A polyclonal antibody against ATF2 (Ab-112 or 94). Recognizes ATF2 (Ab-112 or 94) from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;WB:1:500-1:1000, IHC:1:50-1:200
Description: A polyclonal antibody against ATF2 (Ab-112 or 94). Recognizes ATF2 (Ab-112 or 94) from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;WB:1:500-1:1000, IHC:1:50-1:200
The results, expressed in terms of total phenolic and anthocyanin content of total monomers, indicates that the best extracting solvent for rice ‘Violet Nori’ is a mixture of ethanol: water (60:40 v / v), become COSMO-RS predictions of computing in a good correlation with the experimental results. In addition, the most efficient technique to extract the antioxidant compound resulted to be the investigation of ultrasound-assisted extraction and milling beads, which is only 5 minutes got the same extractive efficiency is obtained after 3 hours of conventional maceration.
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