旭硝子財団助成研究成果報告2017
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89Uthaiporn SURIYAPRAPHADILOK90Triwit RattanarojpongDesign and Simulation of Methanol Synthesis from Flue Gas: A Techno-Economic Study of a Power Plant in Thailand (Project 2015)Proteomic Analysis of Antigenic Proteins from Campylobacter jejuni for Vaccine Development in Chicken (Project 2015)65Over the past century the greater amount of CO2 is being emitted to the environment by combustion of carbon-containing substances which are mostly fossil fuels. CO2 is not the most severe greenhouse gases (GHGs), but it contributes to the highest GHG emission which makes it the most unavoidable anthropogenic GHG. In order to lessen CO2 emission into the atmosphere and develop renewable energy sources, two novel approaches for mitigating CO2 from a coal-fired power plant including bi- and tri-reforming are investigated for methanol production. With the aid of Aspen Plus, the characteristics of these processes are designed and simulated to assess energy consumption, net CO2 emissions and atom efficiency. In addition, the total direct costs, capital and utility costs are estimated for the two routes to evaluate economic potential for the utilization of captured CO2. Preliminary evaluations pointed out that the bi-reforming can be considered as a hopeful method for CO2 treatment while the tri-reforming is still far from practical applications.Campylobactor jejuni is a causative agent transmitted enteric disease from animal to human. The effective prevention of C. jejuni infection in chicken is needed to control the transmission of this pathogen to human consumed chicken meat. Here, we tried to screen the antigenic proteins from C. jejuni by using 2-DE and immunoblotting technique and hope that some of these proteins might be a promising good antigen to develop the effective recombinant vaccine. We found 5 proteins spot possibly reacted with chicken serum infected with C. jejuni. There were CadF, FlaA and OprF analyzed by LC-nanoESI-MS/MS. Bioinformatics analysis indicated that CadF and FlaA proteins had the B- cell epitopes. Here, we focused on the expression and production of CadF and FlaA in E. coli by cloning CadF and FlaA gene into pET15bThio vector. The partial CadF encoding some surface exposed parts of ϐ-helix and loop region of CadF (amino acid residue 35-320) and the partial FlaA encoding some surface exposed parts of ϐ-sheet and loop region of FlaA (amino acid residue 125-506) were successfully cloned into the vector. The expression of these two recombinant thioredoxin fusion proteins was compared in Escherichia coli BL21 DE3 and BL21 RIL (CodonPlus) and Origami strains. The results revealed that the recombinant thioredoxin fusion CadF was greatly expressed in Escherichia coli BL21 DE3 and Origami strains at 16 h when inducing with 1 mM IPTG with the molecular mass of 43 kDa. Additionally, there was no any difference in the great expression of recombinant thioredoxin fusion FlaA in Escherichia coli BL21 DE3 and Origami strains at 4 and 16 h with the molecular mass of 49 kDa. However, recombinant thioredoxin fusion CadF was instability due to the self-degradation of the protein. Western-blot analysis with anti-His conjgated HRP antibody also confirmed the successful expression of recombinant thioredoxin fusion FlaA in E. coli. Furthermore, the successful expression of these two recombinants thioredoxin fusion proteins in E. coli gains the benefit for sub- unit vaccine development to testing its efficacy for the reduction of C. jejuni in chicken farm in the future.

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