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1.
Electron. j. biotechnol ; 38: 49-57, Mar. 2019. tab, graf, ilus
Article in English | LILACS | ID: biblio-1051388

ABSTRACT

BACKGROUND: This paper presents micro- and nano-fabrication techniques for leachable realgar using the extremophilic bacterium Acidithiobacillus ferrooxidans (A. ferrooxidans) DLC-5. RESULTS: Realgar nanoparticles of size ranging from 120 nm to 200 nm were successfully prepared using the highenergy ball mill instrument. A. ferrooxidans DLC-5 was then used to bioleach the particles. The arsenic concentration in the bioleaching system was found to be increased significantly when compared with that in the sterile control. Furthermore, in the comparison with the bioleaching of raw realgar, nanoparticles could achieve the same effect with only one fifth of the consumption. CONCLUSION: Emphasis was placed on improving the dissolvability of arsenic because of the great potential of leachable realgar drug delivery in both laboratory and industrial settings


Subject(s)
Arsenic/metabolism , Sulfides/metabolism , Acidithiobacillus/metabolism , Mining/methods , Arsenic/chemistry , Solubility , Sulfides/chemistry , Temperature , Nanotechnology , Nanoparticles/chemistry , Extremophiles
2.
Biol. Res ; 51: 55, 2018. tab, graf
Article in English | LILACS | ID: biblio-1011399

ABSTRACT

BACKGROUND: The Antarctic continent is a source of extreme microorganisms. Millions of years of isolation have produced unique biodiversity with adaptive responses to its extreme environment. Although the Antarctic climate is mainly cold, the presence of several geothermal sites, including thermal springs, fumaroles, hot soils and hydrothermal vents, provides ideal environments for the development of thermophilic and hyperthermophilic microorganisms. Their enzymes, called thermoenzymes, are the focus of interest in both academic and industrial research, mainly due to their high thermal activity and stability. Glutamate dehydrogenase, is an enzyme that plays a key role in the metabolism of carbon and nitrogen catalyzing reversibly the oxidative deamination of glutamate to alpha-ketoglutarate and ammonium. It belongs to the family of oxidoreductases, is widely distributed and it has been highly regarded for use as biosensors, particularly for their specificity and ability to operate in photochemical and electrochemical systems. However, the use of enzymes as biosensors is relatively problematic due to their instability to high temperatures, organic solvents and denaturing agents. The purpose of this study is to present the partial characterization of a thermophilic microorganism isolated from Deception Island, Antarctica, that displays glutamate dehydrogenase activity. RESULTS: In this work, we report the isolation of a thermophilic microorganism called PID15 from samples of Deception Island collected during the Antarctic Scientific Expedition ECA 46. This microorganism is a thermophile that grows optimally at 50 °C and pH 8.0. Scanning electron microscopy shows rod cells of 2.0 to 8.0 µm of length. Phylogenetic analysis of 16S rRNA gene revealed that this microorganism is closely related to Bacillus gelatini. This microorganism contains a thermostable glutamate dehydrogenase with optimal activity at pH 8.0 and temperatures for its activity from 37 to 50 °C, range of temperature of interest for biotechnological applications. This glutamate dehydrogenase is a highly thermostable enzyme. CONCLUSION: This is the first report of a microorganism from Antarctica containing a thermostable glutamate dehydrogenase that maintains its activity in a broad range of temperatures making it of potential interest for biotechnological applications.


Subject(s)
Animals , Bacteria/enzymology , Extremophiles/enzymology , Glutamate Dehydrogenase/analysis , Phylogeny , Time Factors , Bacteria/growth & development , Bacteria/genetics , RNA, Ribosomal, 16S/genetics , Microscopy, Electron, Scanning , Polymerase Chain Reaction , Microscopy, Electron, Transmission , Islands , Extremophiles/growth & development , Extremophiles/genetics , Antarctic Regions
3.
Electron. j. biotechnol ; 29: 1-6, sept. 2017. graf, tab
Article in English | LILACS | ID: biblio-1016090

ABSTRACT

Background: During salt stress, the yeast Debaryomyces hansenii synthesizes tyrosine as a strategy to avoid the oxidation of proteins. Tyrosine reacts with nitrogen radicals to form 3-nitrotyrosine. 3-nitrotyrosine prevents the effects of associated oxidative stress and thus contributes to the high halotolerace of the yeast. However, the mechanism of how D. hansenii counteracts the presence of this toxic compound is unclear. In this work, we evaluated D. hansenii's capacity to assimilate 3-nitrotyrosine as a unique nitrogen source and measured its denitrase activity under salt stress. To identify putative genes related to the assimilation of 3-nitrotyrosine, we performed an in silico search in the promoter regions of D. hansenii genome. Results: We identified 15 genes whose promoters had binding site sequences for transcriptional factors of sodium, nitrogen, and oxidative stress with oxidoreductase and monooxygenase GO annotations. Two of these genes, DEHA2E24178g and DEHA2C00286g, coding for putative denitrases and having GATA sequences, were evaluated by RT-PCR and showed high expression under salt and nitrogen stress. Conclusions: D. hansenii can grow in the presence of 3-nitrotyrosine as the only nitrogen source and has a high specific denitrase activity to degrade 3-nitrotyrosine in 1 and 2 M NaCl stress conditions. The results suggest that given the lack of information on transcriptional factors in D. hansenii, the genes identified in our in silico analysis may help explain 3-nitrotyrosine assimilation mechanisms.


Subject(s)
Tyrosine/analogs & derivatives , Tyrosine/metabolism , Debaryomyces/genetics , Debaryomyces/metabolism , Tyrosine/genetics , Transcription, Genetic , Yeasts , Regulatory Sequences, Nucleic Acid , Promoter Regions, Genetic , Oxidative Stress , Real-Time Polymerase Chain Reaction , Osmoregulation , Extremophiles , Salt Stress , Nitrogen/metabolism
4.
Electron. j. biotechnol ; 25: 58-63, ene. 2017. tab, graf, ilus
Article in English | LILACS | ID: biblio-1008708

ABSTRACT

Background: Sulphur-oxidizing microorganisms are widely used in the biofiltration of total reduced sulphur compounds (odorous and neurotoxic) produced by industries such as the cellulose and petrochemical industries, which include high-temperature process steps. Some hyperthermophilic microorganisms have the capability to oxidize these compounds at high temperatures (N60°C), and archaea of this group, for example, Sulfolobus metallicus, are commonly used in biofiltration technology. Results: In this study, a hyperthermophilic sulphur-oxidizing strain of archaea was isolated from a hot spring (Chillán, Chile) and designated as M1. It was identified as archaea of the genus Sulfolobus (99% homology with S. solfataricus 16S rDNA). Biofilms of this culture grown on polyethylene rings showed an elemental sulphur oxidation rate of 95.15 ± 15.39 mg S l-1 d-1, higher than the rate exhibited by the biofilm of the sulphur-oxidizing archaea S. metallicus (56.8 ± 10.91 mg l-1 d-1). Conclusions: The results suggest that the culture M1 is useful for the biofiltration of total reduced sulphur gases at high temperatures and for other biotechnological applications.


Subject(s)
Sulfides/metabolism , Archaea/metabolism , Biofilms , Oxidation-Reduction , Phylogeny , Polymerase Chain Reaction , Sulfolobus , Archaea/isolation & purification , Archaea/genetics , Polyethylene , Hot Springs/microbiology , Electrophoresis , Filtration , Extremophiles , Hot Temperature
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