Amine absorption processes are widely used in the industry to purify refinery gases, process gases or natural gas. Recently, amine absorption has also been considered for CO2 removal from flue gases. It has a number of advantages, but there is one major disadvantage - high energy consumption. This can be reduced by using an appropriate sorbent. From a group of several dozen solutions, three amine sorbents were selected based on primary, tertiary and sterically hindered amines. The solutions were used to test CO2 absorption capacity, absorption kinetics and heat of CO2 absorption. Additional tests were performed on the actual absorber-desorber system to indicate the most appropriate sorbent for capturing CO2 from flue gases.
:This paper provides a discussion concerning results of CO2 removal from a gas mixture by the application of aqueous solutions of ethanoloamine (MEA) and 2-amino-2-methyl-1-propanol (AMP) promoted with piperazine (PZ). The studies were conducted using a process development unit. Research of such a scale provides far more reliable representation of the actual industrial process than modelling and laboratory tests. The studies comprised comparative analyses entailing identical energy supplied to a reboiler as well as tests conducted at similar process efficiencies for both solvents. The results thus obtained imply that using AMP/PZ enables reduction of the solvent heat duty. Moreover, while using AMP/PZ temperature decrease was also observed in the columns.
Phosphorylated fructose-1,6-bisphosphatase (FBPase) was isolated from rabbit muscle in an SDS/PAGE homogeneous form. Its dephosphorylation with alkaline phosphatase revealed 2.8 moles of inorganic phosphate per mole of FBPase. The phosphorylated FBPase (P-FBPase) differs from the dephosphorylated enzyme in terms of its kinetic properties like Km and kcat, which are two times higher for the phosphorylated FBPase, and in the affinity for aldolase, which is three times lower for the dephosphorylated enzyme. ephosphorylated FBPase can be a substrate for protein kinase A and the amount of phosphate incorporated per FBPase monomer can reach 2-3 molecules. Since interaction of muscle aldolase with muscle FBPase results in desensitisation of the latter toward AMP inhibition (Rakus & Dzugaj, 2000, Biochem. Biophys. Res. Commun. 275, 611-616), phosphorylation may be considered as a way of muscle FBPase activity regulation.
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