Bioconversion of cellulosic biomass wastes by Azorean hot spring bacterial consortia

ECO-BIO 2016Enzymatic hydrolysis of cellulose is a fundamental step in the carbon cycle and in the industrial bioconversion of biomass to biofuels. In nature cellulose hydrolysis is often catalysed by enzymes from complex microbial communities, nevertheless these studies are limited to a few isolates. Actually the production of biofuels from biomass became a necessity and novel pre-treatments are mandatory to be discovered. Thereby the study of cellulose hydrolysing bacterial communities is a step in achieving a sustainable future in biofuels development. We propose the stabilization of an aerobic thermophilic bacterial consortia (BC) with the ability to adapt and hydrolyse different cellulose-rich wastes. Decaying cellulosic residues were sampled inside Azorean hot springs. Samples were enriched in cellulosic selective medium at 60ºC with growth monitored quantifying DNA. Hydrolysis efficiency was monitored and enzymatic activity was detected using xylan and carboxymetylcellulose (CMC). 16S rRNA hypervariable regions V3/V4 were amplified for phylogenetic characterization of BC using 454 pyrosequencing. Selected BC was able to hydrolyse 50% of cellulose-rich plant mix material in 4 days. Besides hydrolysing low content lignin material as non-wood plants, newspaper and cardboard, the consortia was able to hydrolyse high lignin content material, with lower efficiency. Celulase and xylanase were present in BC and reducing sugars were shown to be higher, compared with control. The phylogenetic results showed a large diversity in the BC with Thermobacillus representing 44% of the consortia, followed by Symbiobacterium 25%, Brevibacillus 16%, Geobacillus 12% and Hipomicrobium 3%. Three Geobacillus species were identified; G. stearothermophilus, G.thermodenitrificans and G.debilis. Further work will comply the isolation of enzyme producing bacteria isolates from the consortia for the construction of new consortia taking in consideration the efficiency of cellulose rich wastes. These results suggest that bacterial communities can be an alternative pre-treatment method of green wastes to obtain molecules to biofuels production.info:eu-repo/semantics/publishedVersio

The genome, transcriptome, and proteome of the nematode Steinernema carpocapsae: Evolutionary signatures of a pathogenic lifestyle

The entomopathogenic nematode Steinernema carpocapsae has been widely used for the biological control of insect pests. It shares a symbiotic relationship with the bacterium Xenorhabdus nematophila, and is emerging as a genetic model to study symbiosis and pathogenesis. We obtained a high-quality draft of the nematode’s genome comprising 84,613,633 bp in 347 scaffolds, with an N50 of 1.24 Mb. To improve annotation, we sequenced both short and long RNA and conducted shotgun proteomic analyses. S. carpocapsae shares orthologous genes with other parasitic nematodes that are absent in the free-living nematode C. elegans, it has ncRNA families that are enriched in parasites, and expresses proteins putatively associated with parasitism and pathogenesis, suggesting an active role for the nematode during the pathogenic process. Host and parasites might engage in a co-evolutionary arms-race dynamic with genes participating in their interaction showing signatures of positive selection. Our analyses indicate that the consequence of this arms race is better characterized by positive selection altering specific functions instead of just increasing the number of positively selected genes, adding a new perspective to these co-evolutionary theories. We identified a protein, ATAD-3, that suggests a relevant role for mitochondrial function in the evolution and mechanisms of nematode parasitism

Beyond Genetic Factors in Familial Amyloidotic Polyneuropathy: Protein Glycation and the Loss of Fibrinogen's Chaperone Activity

Familial amyloidotic polyneuropathy (FAP) is a systemic conformational disease characterized by extracellular amyloid fibril formation from plasma transthyretin (TTR). This is a crippling, fatal disease for which liver transplantation is the only effective therapy. More than 80 TTR point mutations are associated with amyloidotic diseases and the most widely accepted disease model relates TTR tetramer instability with TTR point mutations. However, this model fails to explain two observations. First, native TTR also forms amyloid in systemic senile amyloidosis, a geriatric disease. Second, age at disease onset varies by decades for patients bearing the same mutation and some mutation carrier individuals are asymptomatic throughout their lives. Hence, mutations only accelerate the process and non-genetic factors must play a key role in the molecular mechanisms of disease. One of these factors is protein glycation, previously associated with conformational diseases like Alzheimer's and Parkinson's. The glycation hypothesis in FAP is supported by our previous discovery of methylglyoxal-derived glycation of amyloid fibrils in FAP patients. Here we show that plasma proteins are differentially glycated by methylglyoxal in FAP patients and that fibrinogen is the main glycation target. Moreover, we also found that fibrinogen interacts with TTR in plasma. Fibrinogen has chaperone activity which is compromised upon glycation by methylglyoxal. Hence, we propose that methylglyoxal glycation hampers the chaperone activity of fibrinogen, rendering TTR more prone to aggregation, amyloid formation and ultimately, disease