Description:
Reducing the capital cost of post combustion CO2 capture by eliminating flue gas desulfurisation (FGD) pre-treatment, requires management of the amines preferential SO2 absorption. Novel technologies such as CS-Cap restrict the impact of SO2 to only a small fraction of the amine inventory resulting in high sulfate burden amines. Traditional thermal reclamation of these spent absorbents has advantages regarding simplicity, but ranks poorly for industrial ecology around PCC. These amines require low energy regeneration technologies compatible with their physico-chemical properties that also maximise the potential for valorising by-products. This review summarises the sulfur chemistry and outlines several amine reclamation processes. It assesses the status of established and novel regeneration technologies for their applicability to high sulfur loaded amines. Should deep sulfur removal be required, a hybrid approach with initial bulk removal (as product) followed by a polishing step to further reduce sulfur is prospective. A preliminary estimation of the relative cost of using standard reclamation methods for treating Sulfur loaded CS-Cap absorbent revealed the cost would increase due to its higher sulfate burden despite comparable treatment volumes. Research gaps are identified which would enable better comparison between the costs of traditional FGD versus higher reclamation costs for combined capture technologies.
Description:
Two cDNA clones, encoding Aluminum-responsive wali1 and wali5, were identified in dehydration stress-specific cDNA library from wheat. Their sequence variations and structural dissimilarities indicated them to be non-homologous genes. Expression of both genes was induced by various abiotic stresses as well as in response to plant hormones and oxidative molecules. Further, they were expressed differentially in shoot and root tissues of wheat seedlings, their transcripts being specifically abundant in roots. Previously characterized as being only Aluminum treatment induced, this report proposes them as novel candidates for stress-responsive studies.
Description:
Dipeptide (Leu-Leu) and nitrate transport activities of 26 Arabidopsis NPF (NRT1/PTR Family) proteins were screened in Saccharomyces cerevisiae and Xenopus laevis oocytes, respectively. Dipeptide transport activity has been confirmed for 2 already known dipeptide transporters (AtNPF8.1 and AtNPF8.3) but none of the other tested NPFs displays dipeptide transport. The nitrate transport screen resulted in the identification of two new nitrate transporters, AtNPF5.5 and AtNPF5.10. The localization of the mRNA coding for NPF5.5 demonstrates that it is the first NPF transporter reported to be expressed in Arabidopsis embryo. Two independent homozygous npf5.5 KO lines display reduced total nitrogen content in the embryo as compared to WT plants, demonstrating an effect of NPF5.5 function on the embryo nitrogen content. Finally, NPF5.5 gene produces two different transcripts (AtNPF5.5a and AtNPF5.5b) encoding proteins with different N-terminal ends. Both proteins are able to transport nitrate in xenopus oocytes.
Description:
Dipeptide (Leu-Leu) and nitrate transport activities of 26 Arabidopsis NPF (NRT1/PTR Family) proteins were screened in Saccharomyces cerevisiae and Xenopus laevis oocytes, respectively. Dipeptide transport activity has been confirmed for 2 already known dipeptide transporters (AtNPF8.1 and AtNPF8.3) but none of the other tested NPFs displays dipeptide transport. The nitrate transport screen resulted in the identification of two new nitrate transporters, AtNPF5.5 and AtNPF5.10. The localization of the mRNA coding for NPF5.5 demonstrates that it is the first NPF transporter reported to be expressed in Arabidopsis embryo. Two independent homozygous npf5.5 KO lines display reduced total nitrogen content in the embryo as compared to WT plants, demonstrating an effect of NPF5.5 function on the embryo nitrogen content. Finally, NPF5.5 gene produces two different transcripts (AtNPF5.5a and AtNPF5.5b) encoding proteins with different N-terminal ends. Both proteins are able to transport nitrate in xenopus oocytes.