1.
Performance and mechanism of carbon dioxide fixation by a newly isolated chemoautotrophic strain Paracoccus denitrificans PJ-1.
Ye, J, An, N, Chen, H, Ying, Z, Zhang, S, Zhao, J
Chemosphere. 2020;:126473
Abstract
CO2 is regarded as a major contributor to the global warming. CO2 utilization is promising to reduce the CO2 emissions. Currently, the biofixation of CO2 using chemoautotrophs has markedly gain interest in CO2 utilization. In this study, a newly isolated chemoautotroph, Paracoccus denitrificans PJ-1, was used for the biofixation of CO2 under anaerobic condition. Experimental results revealed that Paracoccus denitrificans PJ-1 achieved a high carbon fixation rate (13.25 mg·L-1·h-1) which was ∼10 times faster than the previous reported chemotrophic bacteria using thiosulfate as electron donor. The best CO2 fixation activity of Paracoccus denitrificans PJ-1 was achieved at the pH value of 9.0 and CO2 concentration of 20 vol%. Meanwhile, a high CO2 fixation yield of 106.03 mg·L-1 was reached. The presence of oxygen was adverse to the biofixation, indicating that strain PJ-1 was more suitable for CO2 fixation in anaerobic environments. Carbon mass balance analysis revealed that the carbon from CO2 was mainly fixed into the extracellular organic carbon rather than the biomass. GC-MS analysis and cbbL gene test revealed that Paracoccus denitrificans PJ-1 fixed CO2 through the Calvin-Benson-Bassham cycle and mainly converted CO2 to oxalic acid and succinic acid. Overall, the excellent CO2 fixation capacity of Paracoccus denitrificans PJ-1 suggests that it had potential for CO2 utilization.
2.
Enhanced stability and chemical resistance of a new nanoscale biocatalyst for accelerating CO2 absorption into a carbonate solution.
Zhang, S, Lu, H, Lu, Y
Environmental science & technology. 2013;(23):13882-8
Abstract
A novel potassium-carbonate-based absorption process is currently being developed to reduce the energy consumption when capturing CO2 from coal combustion flue gas. The process employs the enzyme carbonic anhydrase (CA) as a catalyst to accelerate the rate of CO2 absorption. This study focused on the immobilization of a new variant of the CA enzyme onto a new group of nonporous nanoparticles to improve the enzyme's thermal stability and its chemical resistance to major impurities from the flue gas. The CA enzyme was manufactured at the pilot scale by a leading enzyme company. As carrier materials, two different batches of SiO2-ZrO2 composite nanoparticles and one batch of silica nanoparticle were synthesized using a flame spray pyrolysis method. Classic Danckwerts absorption theory with reaction was applied to determine the kinetics of the immobilized enzymes for CO2 absorption. The immobilized enzymes retained 56-88% of their original activity in a K2CO3/KHCO3 solution over a 60-day test period at 50 °C, compared with a 30% activity retention for their free CA enzyme counterpart. The immobilized CA enzymes also revealed improved chemical stability. The inactivation kinetics of the free and immobilized CA enzymes in the K2CO3/KHCO3 solution were experimentally quantified.