Project description:Cyanuric acid, a metabolic intermediate in the degradation of many s-triazine compounds, is further metabolized by cyanuric acid hydrolase. Cyanuric acid also accumulates in swimming pools due to the breakdown of the sanitizing agents di- and trichloroisocyanuric acid. Structurally stable cyanuric acid hydrolases are being considered for usage in pool water remediation. In this study, cyanuric acid hydrolase from the thermophile Moorella thermoacetica ATCC 39073 was cloned, expressed in Escherichia coli, and purified to homogeneity. The recombinant enzyme was found to have a broader temperature range and greater stability, at both elevated and low temperatures, than previously described cyanuric acid hydrolases. The enzyme had a narrow substrate specificity, acting only on cyanuric acid and N-methylisocyanuric acid. The M. thermoacetica enzyme did not require metals or other discernible cofactors for activity. Cyanuric acid hydrolase from M. thermoacetica is the most promising enzyme to use for cyanuric acid remediation applications.
Project description:Moorella thermoacetica-CdS hybrid system have been proven capable of efficiently harnessing solar energy into chemical energy. This project aims to make clear the concrete electron transport pathway, CO2 fixation process and energy production for this photosynthetic biobybrid system with the help of quanlitative and label free quantitative proteomics.
Project description:Moorella thermoacetica spores are the most heat-resistant so far retrieved in food industry and we previously showed that the resistance properties of these spores to wet- heat and biocides were lower when spores were produced at low limit temperature than at optimal temperature. By electron microcopy, we observed that the ultrastructure of the spore coat differed according to the sporulation temperature, with spores produced at 55 °C mainly exhibiting lamellar inner coat tightly associated to diffuse outer coat, while spores produced at 45 °C showing an inner and outer coat separated by a less electron- dense zone. Moreover, misarranged coat structures were more frequently observed when spores were produced at low limit temperature. We analyzed the proteome of spore ob- tained at 45° and 55 °C and focused our data analysis on putative spore coat, exosporium proteins or proteins playing a role in spore resistance. Some putative spore coat proteins, such as CotSA, were only identified in spores produced at 55 °C, while some other puta- tive exosporium and coat proteins were significantly less abundant in spores produced at 45 °C. Altogether, our results suggest that sporulation temperature affects the structure and the protein composition of M. thermoacetica spores.