Journal
SCIENTIFIC REPORTS
Volume 11, Issue 1, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41598-020-80489-6
Keywords
-
Categories
Funding
- Xunta de Galicia
- FEDER [ED431C 2020/08]
- Ministerio de Ciencia, Innovacion y Universidades (MICINN) [RTI2018-099249-B-I00]
- FPU fellowship (Ministerio de Educacion Cultura y Deporte) [FPU12/05050]
- Short Term Mobility program of the FPU scholarship
Ask authors/readers for more resources
The study investigated the microbial community inhabiting As Burgas geothermal spring in Spain, revealing a complex community dominated by Bacteria, with Proteobacteria and Aquificae as prevalent phyla. The research also highlighted the potential involvement of important pathways from the nitrogen and sulfur cycle in the hot spring, as well as the challenge of finding novel active enzymes solely based on their sequence.
In the present study we investigate the microbial community inhabiting As Burgas geothermal spring, located in Ourense (Galicia, Spain). The approximately 23 Gbp of Illumina sequences generated for each replicate revealed a complex microbial community dominated by Bacteria in which Proteobacteria and Aquificae were the two prevalent phyla. An association between the two most prevalent genera, Thermus and Hydrogenobacter, was suggested by the relationship of their metabolism. The high relative abundance of sequences involved in the Calvin-Benson cycle and the reductive TCA cycle unveils the dominance of an autotrophic population. Important pathways from the nitrogen and sulfur cycle are potentially taking place in As Burgas hot spring. In the assembled reads, two complete ORFs matching GH2 beta-galactosidases were found. To assess their functional characterization, the two ORFs were cloned and overexpressed in E. coli. The pTsbg enzyme had activity towards o-Nitrophenyl-beta -d-galactopyranoside (ONPG) and p-Nitrophenyl-beta -d-fucopyranoside, with high thermal stability and showing maximal activity at 85 degrees C and pH 6, nevertheless the enzyme failed to hydrolyze lactose. The other enzyme, Tsbg, was unable to hydrolyze even ONPG or lactose. This finding highlights the challenge of finding novel active enzymes based only on their sequence.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available