Ammonium Sulfate Co-precipitation of SSB and Interacting Proteins

Author(s):  
Aimee H. Marceau
2018 ◽  
Vol 36 (9) ◽  
pp. 981-985 ◽  
Author(s):  
Jinsheng Li ◽  
Zhifa Liu ◽  
Lei Wu ◽  
Xiumei Han ◽  
Xiwei Qi ◽  
...  

2012 ◽  
Vol 04 (08) ◽  
pp. 536-543 ◽  
Author(s):  
Chuner Cai ◽  
Chunxia Li ◽  
Shuxian Wu ◽  
Qing Wang ◽  
Ziye Guo ◽  
...  

2021 ◽  
Vol 2117 (1) ◽  
pp. 012038
Author(s):  
N P Asri ◽  
R Saraswati ◽  
R R Yogasuara ◽  
D A Puspitasari ◽  
Y W Mirzayanti ◽  
...  

Abstract Biodiesel is an alternative energy obtained through the trasesterification of vegetable oil in the presence of a catalyst. The catalyst plays a very important role in the success of the transesterification process. One way to increase the activity of the catalyst is through chemical modification called functionalization, which generally using SO3 group as a sulfonating agent is known as the sulfonation process. However, the disadvantage of this process is that it uses strong acids which are corrosive, require high temperatures and are not environmentally friendly. This study aims to increase the activity of zinc oxide catalyst supported by multi-wall carbon nano tube (Z/MWCNTs) sulfonated using (NH4)2SO4 as sulfonating agent. The synthesis route includes co-precipitation, sulfonation and precipitation time. The effect of concentration of ammonium sulfate, co-precipitation time, and sulfonating time on yield of biodiesels of kesambi (Schleichera oleosa L) oil (OSOBD) was investigated. The result showed that the activity functionalized Z/MWCNTS catalyst (Z/s-MWCCNTs) could enhance significantly. The results of the catalyst activity test on transesterification of OSO into biodiesel showed that Z/s-MWCNTs gave a high yield of 91% for the functionalized catalyst using ammonium sulfate with a concentration of 35%, co-precipitation time 12 hours and sulfonation time 4 hours. The functionalization of MWCNTS with the sulfonation process using ammonium sulfate has the potential to increase catalyst activity and can increase the efficiency of the transesterification process for non-edible oils, especially kesambi oil.


2003 ◽  
Vol 107 ◽  
pp. 945-948 ◽  
Author(s):  
P. M. Nicolaysen ◽  
E. Steinnes ◽  
T. E. Sjobakk

1968 ◽  
Vol 20 (03/04) ◽  
pp. 457-464 ◽  
Author(s):  
L Gonyea ◽  
R Herdman ◽  
R. A Bridges

SummaryAn anticoagulant occurring in 4 of 6 patients with SLE has been demonstrated by a sensitive assay utilizing an ammonium sulfate fraction of serum. The anticoagulant functions as an inhibitor of the activation of prothrombin. No species specificity was demonstrable. The inhibitor behaves clinically and chromatographically as an immunoglobulin, although an attempt to demonstrate directly the antibody nature of the inhibitor was not successful.A severe, apparently independent, decrease in the level of prothrombin was observed in the patient with hemorrhagic symptoms. In contrast to the anticoagulant activity, the low prothrombin has persisted during treatment.


2013 ◽  
Vol 10 (2) ◽  
pp. 29
Author(s):  
Normah Ismail ◽  
Nur' Ain Mohamad Kharoe

Unripe and ripe bilimbi (Averrhoa bilimbi L.) were ground and the extracted juices were partially purified by ammonium sulfate precipitation at the concentrations of 40 and 60% (w/v). The collected proteases were analysed for pH, temperature stability, storage stability, molecular weight distribution, protein concentration and protein content. Protein content of bilimbi fruit was 0.89 g. Protease activity of both the unripe and ripe fruit were optimum at pH 4 and 40°C when the juice were purified at 40 and 60% ammonium sulfate precipitation. A decreased in protease activity was observed during the seven days of storage at 4°C. Molecular weight distribution indicated that the proteases protein bands fall between IO to 220 kDa. Protein bands were observed at 25, 50 and 160 kDa in both the unripe and ripe bilimbi proteases purified with 40% ammonium sulfate, however, the bands were more intense in those from unripe bilimbi. No protein bands were seen in proteases purified with 60% ammonium sulfate. Protein concentration was higher for proteases extracted with 40% ammonium sulfate at both ripening stages. Thus, purification using 40% ammonium sulfate precipitation could be a successful method to partially purify proteases from bilimbi especially from the unripe stage. 


2015 ◽  
Vol 7 (2) ◽  
pp. 1393-1403
Author(s):  
Dr R.P VIJAYALAKSHMI ◽  
N. Manjula ◽  
S. Ramu ◽  
Amaranatha Reddy

Single crystalline nano-sized multiferroic BiFeO3 (BFO) powders were synthesized through simple chemical co-precipitation method using polyethylene glycol (PEG) as capping agent. We obtained pure phase BiFeO3 powder by controlling pHand calcination temperature. From X-ray diffraction studies the nanoparticles were unambiguously identified to have a rhombohedrally distorted perovskite structure belonging to the space group of R3c. No secondary phases were detected. It indicates single phase structure. EDX spectra indicated the appearance of three elements Bi, Fe, O in 1:1:3. From the UV-Vis diffuse reflectance spectrum, the absorption cut-off wavelength of the BFO sample is around 558nm corresponding to the energy band gap of 2.2 eV. The size (60-70 nm) and morphology of the nanoparticles have been analyzed using transmission electron microscopy (TEM).   Linear M−H behaviour and slight hysteresis at lower magnetic field is observed for BiFeO3 nanoparticles from Vibrating sample magnetometer studies. It indicates weak ferromagnetic behaviour at room temperature. From dielectric studies, the conductivity value is calculated from the relation s = L/RbA Sm-1 and it is around 7.2 x 10-9 S/m.


1973 ◽  
Vol 36 (6) ◽  
pp. 1186-1190 ◽  
Author(s):  
K. K. Bolsen ◽  
Walter Woods ◽  
Terry Klopfenstein
Keyword(s):  

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