Electromagnetic separation of heat stable salt from gas sweetening amine

2018 ◽  
Vol 68 ◽  
pp. 256-268 ◽  
Author(s):  
Fadi Alnaimat ◽  
Emad Alhseinat ◽  
Fawzi Banat
Molecules ◽  
2020 ◽  
Vol 25 (21) ◽  
pp. 4911
Author(s):  
Asma Ghorbani ◽  
Behrouz Bayati ◽  
Teresa Poerio ◽  
Pietro Argurio ◽  
Tavan Kikhavani ◽  
...  

This study presents an efficient and scalable process for removing the heat-stable salts (HSS) ions from amine solution while recovering methyl diethanolamine (MDEA) solution for its reuse in gas sweetening plants. The presence of HSS in the amine solution causes the loss of solvent capacity, foaming, fouling, and corrosion in gas sweetening units so their removal is crucial for a more well-performing process. Furthermore, the recovery of the amine solution can make the sweetening step a more sustainable process. In this study, for the first time, the removal of a multicomponent mixture of HSS from MDEA solution was investigated via a nanofiltration process using flat-sheet NF-3 membranes. The impact of operating parameters on salts and amine rejection, and flux, including the operating pressure, HSS ions concentration, and MDEA concentration in the feed solution was investigated. Results based on the nanofiltration of an amine stream with the same composition (45 wt.% MDEA solution) as that circulating in a local gas refinery (Ilam Gas refinery), demonstrated a removal efficiency of HSS ions in the range from 75 to 80% and a MDEA rejection of 0% indicating the possibility of reusing this stream in the new step of gas sweetening.


2001 ◽  
Vol 120 (5) ◽  
pp. A137-A137
Author(s):  
D CHILDS ◽  
D CROMBIE ◽  
V PRATHA ◽  
Z SELLERS ◽  
D HOGAN ◽  
...  

1984 ◽  
Vol 52 (03) ◽  
pp. 243-249 ◽  
Author(s):  
S Izaki ◽  
T Hibino ◽  
Y Isozaki ◽  
P S Hsu ◽  
M Izaki ◽  
...  

SummaryPlasminogen activator that is associated with the development of hypersensitivity granulomas (gPA) was partially purified from a saline soluble fraction of murine lepromas elicited in “resistant” mice, C57BL/6N. The gPA was shown to consist of two subspecies (23,000 and 48,000 in molecular weight) with essentially identical enzymologic properties. The gPA was found to be a relatively heat stable weakly alkaline serine proteinase with trypsin-like characteristics in the specificity for synthetic substrates and proteinase inhibitors. It showed a high affinity for H- D-Ile-Pro-Arg-pNA (Km = 1.4 × 10-4 M) H-D-Val-Leu-Lys- pNA (Km = 5.2 × 10-4 M), and L-pyroGlu-Gly-Arg-pNA (Km = 9.3 × 10-4 M). The gPA did not demonstrate antigenic cross reaction with urokinase-type or tissue-type plasminogen activator.Two distinct enzymatic regulators of the gPA were also demonstrated in the saline soluble fraction of the hypersensitivity granulomas. The gPA and its regulation are assumed to be correlated with macrophage activation in the hypersensitivity granulomas


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