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PubMed | Swissaustral United States and Fundacion Cientifica y Cultural Biociencia
Type: | Journal: Frontiers in bioengineering and biotechnology | Year: 2015

The development of enzymes for industrial applications relies heavily on the use of microorganisms. The intrinsic properties of microbial enzymes, e.g., consistency, reproducibility, and high yields along with many others, have pushed their introduction into a wide range of products and industrial processes. Extremophilic microorganisms represent an underutilized and innovative source of novel enzymes. These microorganisms have developed unique mechanisms and molecular means to cope with extreme temperatures, acidic and basic pH, high salinity, high radiation, low water activity, and high metal concentrations among other environmental conditions. Extremophile-derived enzymes, or extremozymes, are able to catalyze chemical reactions under harsh conditions, like those found in industrial processes, which were previously not thought to be conducive for enzymatic activity. Due to their optimal activity and stability under extreme conditions, extremozymes offer new catalytic alternatives for current industrial applications. These extremozymes also represent the cornerstone for the development of environmentally friendly, efficient, and sustainable industrial technologies. Many advances in industrial biocatalysis have been achieved in recent years; however, the potential of biocatalysis through the use of extremozymes is far from being fully realized. In this article, the adaptations and significance of psychrophilic, thermophilic, and hyperthermophilic enzymes, and their applications in selected industrial markets will be reviewed. Also, the current challenges in the development and mass production of extremozymes as well as future prospects and trends for their biotechnological application will be discussed.


Monsalves M.T.,Fundacion Cientifica y Cultural Biociencia | Monsalves M.T.,University of Technology of Chile | Amenabar M.J.,Fundacion Cientifica y Cultural Biociencia | Ollivet-Besson G.P.,Fundacion Cientifica y Cultural Biociencia | Blamey J.M.,Fundacion Cientifica y Cultural Biociencia
Protein and Peptide Letters | Year: 2013

A thermostable superoxide dismutase from a thermophilic bacterium, called Geobacillus wiegeli (GWE1), isolated from the interior of a sterilization drying oven, was purified by anion-exchange and molecular size-exclusion liquid chromatography. On the basis of SDS-PAGE, the purified enzyme was found to be homogeneous and showed an estimated subunit molecular mass of 23.9 kDa. The holoenzyme is a homotetramer of 97.3 kDa. Superoxide dismutase exhibited maximal activity at pH 8.5 and at temperature around 60 °C. The enzyme was thermostable maintaining 50% of its activity even after 4.5 hours incubation at 60 °C and more than 70% of its activity after 30 min at 80 °C. When the microorganism was irradiated with UVA, an increase in the specific activity of superoxide dismutase was observed which was correlated with decreasing levels of anion superoxide, indicating the direct involvement of this enzyme in the capture of reactive oxygen species. This study reports the effects of UV radiation on a superoxide dismutase from a thermophilic bacterium isolated from an anthropogenic environment. © 2013 Bentham Science Publishers.


Munoz P.A.,Fundacion Cientifica y Cultural Biociencia | Munoz P.A.,University of Santiago de Chile | Correa-Llanten D.N.,Fundacion Cientifica y Cultural Biociencia | Blamey J.M.,Fundacion Cientifica y Cultural Biociencia | Blamey J.M.,University of Santiago de Chile
Lipids | Year: 2013

Four lipases were purified from ID17, a thermophilic bacterium belonging to Geobacillus genus isolated from Deception Island, Antarctica. Lipase activity was detected by opacity test and p-nitrophenyl laurate methods. Lipase production was better in a medium containing tryptone as the carbon and nitrogen source, without non-ionic detergents and pH 7.5. Proteins were ultrafiltered from supernatant and separated using anion exchange and size exclusion chromatography resulting in four distinct fractions with lipase activity (called Lip1-4). Purified lipases showed an optimal pH at 9.0, 9.5, 10.0 and 8.0 and temperature at 65, 70, 75 and 80 C for Lip1-4, respectively. Lip1 and Lip2 showed higher activity using p-nitrophenol decanoate as substrate, whereas Lip3 and Lip4 prefer p-nitrophenol laurate. Based on their molecular weight Lip1 and Lip2 are trimeric and pentameric proteins, respectively, whereas Lip3 and Lip4 are monomeric proteins. Lip1 was exceptionally thermostable maintaining 70 % of its activity after incubating it at 70 C for 8 h. Based on their characteristics, the four lipases obtained from ID17 are good candidates to understand the mechanisms of lipase stability and to be used in different types of industrial applications. © 2013 AOCS.


Correa-Llanten D.N.,Fundacion Cientifica y Cultural Biociencia | Munoz-Ibacache S.A.,Fundacion Cientifica y Cultural Biociencia | Munoz-Ibacache S.A.,University of Technology of Chile | Castro M.E.,Fundacion Cientifica y Cultural Biociencia | And 4 more authors.
Microbial Cell Factories | Year: 2013

Background: The use of microorganisms in the synthesis of nanoparticles emerges as an eco-friendly and exciting approach, for production of nanoparticles due to its low energy requirement, environmental compatibility, reduced costs of manufacture, scalability, and nanoparticle stabilization compared with the chemical synthesis.Results: The production of gold nanoparticles by the thermophilic bacterium Geobacillus sp. strain ID17 is reported in this study. Cells exposed to Au3+ turned from colourless into an intense purple colour. This change of colour indicates the accumulation of intracellular gold nanoparticles. Elemental analysis of particles composition was verified using TEM and EDX analysis. The intracellular localization and particles size were verified by TEM showing two different types of particles of predominant quasi-hexagonal shape with size ranging from 5-50 nm. The mayority of them were between 10-20 nm in size. FT-IR was utilized to characterize the chemical surface of gold nanoparticles. This assay supports the idea of a protein type of compound on the surface of biosynthesized gold nanoparticles. Reductase activity involved in the synthesis of gold nanoparticles has been previously reported to be present in others microorganisms. This reduction using NADH as substrate was tested in ID17. Crude extracts of the microorganism could catalyze the NADH-dependent Au3+ reduction.Conclusions: Our results strongly suggest that the biosynthesis of gold nanoparticles by ID17 is mediated by enzymes and NADH as a cofactor for this biological transformation. © 2013 Correa-Llantén et al.; licensee BioMed Central Ltd.


Munoz P.A.,Fundacion Cientifica y Cultural Biociencia | Munoz P.A.,University of Santiago de Chile | Flores P.A.,Fundacion Cientifica y Cultural Biociencia | Flores P.A.,University of Santiago de Chile | And 2 more authors.
Antarctic Science | Year: 2011

Deception Island, an active stratovolcano located in the South Shetland Islands, Antarctica, provides excellent conditions for the thermophilic bacteria growth because of high ground temperatures in specific areas, such as Fumarole Bay where the temperatures are above the mesophilic range. Denaturing Gradient Gel Electrophoresis (DGGE) was used with the 16S ribosomal gene to analyse cultures of thermophilic bacteria from a soil sample taken from Fumarole Bay. Nine bands were sequenced and analysed from DGGE and they indicated the presence of bacteria from the genera Geobacillus, Bacillus, Brevibacillus, Thermus and uncultured sulphate reducing bacteria. Some of which have been reported in other Antarctic geothermal sites. Geobacillus, Bacillus and Brevibacillus genera were successfully cultivated in an enriched medium. A pure culture of one thermophilic Geobacillus bacterium was obtained closely related to Geobacillus jurassicus. © Copyright Antarctic Science Ltd 2011.


Munoz P.A.,Fundacion Cientifica y Cultural Biociencia | Correa-Llanten D.N.,Fundacion Cientifica y Cultural Biociencia | Blamey J.M.,Fundacion Cientifica y Cultural Biociencia | Blamey J.M.,University of Santiago de Chile
Lipids | Year: 2014

Lipases catalyze the hydrolysis and synthesis of triglycerides and their reactions are widely used in industry. The use of ionic liquids has been explored in order to improve their catalytic properties. However, the effect of these compounds on kinetic parameters of lipases has been poorly understood. A study of the kinetic parameters of Lip1, the most thermostable lipase from the supernatant of the strain ID17, a thermophilic bacterium isolated from Deception Island, Antarctica, and a member of the genus Geobacillus is presented. Kinetic parameters of Lip1 were modulated by the use of ionic liquids BmimPF6 and BmimBF4. The maximum reaction rate of Lip1 was improved in the presence of both salts. The highest effect was observed when BmimPF6 was added in the reaction mix, resulting in a higher hydrolytic activity and in a modulation of the catalytic efficiency of the enzyme. However, the catalytic efficiency did not change in the presence of BmimBF4. The increase of the reaction rates of Lip1 promoted by these ionic liquids could be related to possible changes in the Lip1 structure. This effect was measured by quenching of tryptophan fluorescence of the enzyme, when it was incubated with each liquid salt. In conclusion, the hydrolytic activity of Lip1 is modulated by the ionic liquids BmimBF4 and BmimPF6, improving the reaction rate and the catalytic efficiency of this enzyme when BmimPF6 was used. This effect is probably due to changes in the structure of Lip1 induced by the presence of these ionic liquids, stimulating its catalytic activity. © 2014 AOCS.


Amenabar M.J.,Fundacion Cientifica y Cultural Biociencia | Flores P.A.,Fundacion Cientifica y Cultural Biociencia | Flores P.A.,University of Santiago de Chile | Pugin B.,Fundacion Cientifica y Cultural Biociencia | And 4 more authors.
Polar Biology | Year: 2013

Antarctica is an extreme continent composed of cold environments but also of several geothermal sites, among them is Deception Island, an active stratovolcano located in the South Shetland archipelago. From this island, few microbiological studies have been performed, and the presence of archaea has not been reported. In order to investigate the archaeal diversity in hydrothermalism from Deception Island, different submarine samples were taken from the flooded caldera. Samples were analyzed by denaturing gradient gel electrophoresis (DGGE) of the 16S rRNA gene in conjunction with culture-dependent methods at hyperthermophilic temperatures. Analysis from DGGE band sequencing showed the presence of archaea belonging to the hyperthermophilic genus Thermococcus and different uncultured archaea closely related to environmental clones from hydrothermal vents. Archaea from the psychrotolerant genus Methanococcoides were also detected. Additionally, we have successfully isolated an anaerobic hyperthermophilic archaeon closely related to Thermococcuscelericrescens. Cells were irregular cocci with a diameter between 0. 6 and 2 μm and grew at 50-90 °C and at a NaCl concentration of 1-5 %. Here, we present, based on culture-dependent and culture-independent approaches, the first report on archaea from marine hydrothermal sites of Antarctica. © 2012 Springer-Verlag Berlin Heidelberg.


PubMed | Fundacion Cientifica y Cultural Biociencia
Type: Journal Article | Journal: BMB reports | Year: 2012

Glutamate dehydrogenase from axenic bacterial cultures of a new microorganism, called GWE1, isolated from the interior of a sterilization drying oven, was purified by anion-exchange and molecular-exclusion liquid chromatography. The apparent molecular mass of the native enzyme was 250.5 kDa and was shown to be an hexamer with similar subunits of molecular mass 40.5 kDa. For glutamate oxidation, the enzyme showed an optimal pH and temperature of 8.0 and 70 degrees C, respectively. In contrast to other glutamate dehydrogenases isolated from bacteria, the enzyme isolated in this study can use both NAD(+) and NADP(+) as electron acceptors, displaying more affinity for NADP(+) than for NAD(+). No activity was detected with NADH or NADPH, 2-oxoglutarate and ammonia. The enzyme was exceptionally thermostable, maintaining more than 70% of activity after incubating at 100(o)C for more than five hours suggesting being one of the most thermoestable enzymes reported in the family of dehydrogenases.


PubMed | Fundacion Cientifica y Cultural Biociencia
Type: Journal Article | Journal: Lipids | Year: 2013

Four lipases were purified from ID17, a thermophilic bacterium belonging to Geobacillus genus isolated from Deception Island, Antarctica. Lipase activity was detected by opacity test and p-nitrophenyl laurate methods. Lipase production was better in a medium containing tryptone as the carbon and nitrogen source, without non-ionic detergents and pH 7.5. Proteins were ultrafiltered from supernatant and separated using anion exchange and size exclusion chromatography resulting in four distinct fractions with lipase activity (called Lip1-4). Purified lipases showed an optimal pH at 9.0, 9.5, 10.0 and 8.0 and temperature at 65, 70, 75 and 80C for Lip1-4, respectively. Lip1 and Lip2 showed higher activity using p-nitrophenol decanoate as substrate, whereas Lip3 and Lip4 prefer p-nitrophenol laurate. Based on their molecular weight Lip1 and Lip2 are trimeric and pentameric proteins, respectively, whereas Lip3 and Lip4 are monomeric proteins. Lip1 was exceptionally thermostable maintaining 70% of its activity after incubating it at 70C for 8h. Based on their characteristics, the four lipases obtained from ID17 are good candidates to understand the mechanisms of lipase stability and to be used in different types of industrial applications.


PubMed | Fundacion Cientifica y Cultural Biociencia
Type: Journal Article | Journal: Protein and peptide letters | Year: 2013

A thermostable superoxide dismutase from a thermophilic bacterium, called Geobacillus wiegeli (GWE1), isolated from the interior of a sterilization drying oven, was purified by anion-exchange and molecular size-exclusion liquid chromatography. On the basis of SDS-PAGE, the purified enzyme was found to be homogeneous and showed an estimated subunit molecular mass of 23.9 kDa. The holoenzyme is a homotetramer of 97.3 kDa. Superoxide dismutase exhibited maximal activity at pH 8.5 and at temperature around 60 C. The enzyme was thermostable maintaining 50% of its activity even after 4.5 hours incubation at 60 C and more than 70% of its activity after 30 min at 80 C. When the microorganism was irradiated with UVA, an increase in the specific activity of superoxide dismutase was observed which was correlated with decreasing levels of anion superoxide, indicating the direct involvement of this enzyme in the capture of reactive oxygen species. This study reports the effects of UV radiation on a superoxide dismutase from a thermophilic bacterium isolated from an anthropogenic environment.

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