A new thermophilic nitrilase from an antarctic hyperthermophilic microorganism.
Several environmental samples from Antarctica were collected and enriched to search for microorganisms with nitrilase activity. A new thermostable nitrilase from a novel hyperthermophilic archaea Pyrococcus sp. M24D13 was purified and characterized. The activity of this enzyme increased as the temp...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2016-02-01
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| Series: | Frontiers in Bioengineering and Biotechnology |
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| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fbioe.2016.00005/full |
| _version_ | 1811227702189883392 |
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| author | Geraldine V. Dennett Geraldine V. Dennett Jenny M. Blamey Jenny M. Blamey |
| author_facet | Geraldine V. Dennett Geraldine V. Dennett Jenny M. Blamey Jenny M. Blamey |
| author_sort | Geraldine V. Dennett |
| collection | DOAJ |
| description | Several environmental samples from Antarctica were collected and enriched to search for microorganisms with nitrilase activity. A new thermostable nitrilase from a novel hyperthermophilic archaea Pyrococcus sp. M24D13 was purified and characterized. The activity of this enzyme increased as the temperatures rise from 70 up to 85 °C. Its optimal activity occurred at 85 °C and pH 7.5. This new enzyme shows a remarkable resistance to thermal inactivation retaining more than 50% of its activity even after 8 h of incubation at 85 °C.In addition, this nitrilase is highly versatile demonstrating activity towards different substrates such as benzonitrile (60 mM, aromatic nitrile) and butyronitrile (60 mM, aliphatic nitrile), with a specific activity of 3286.7 U mg-1 of protein and 4008.2 U mg-1 of protein respectively. Moreover the enzyme NitM24D13 also presents cyanidase activity.The apparent Michaelis-Menten constant (Km) and Vmáx of this Nitrilase for benzonitrile were 0.3 mM and 333.3 µM min-1, respectively, and the specificity constant (kcat/Km) for benzonitrile was 2.05×105 s-1 M-1. |
| first_indexed | 2024-04-12T09:46:19Z |
| format | Article |
| id | doaj.art-2453fd70ad634fa6813546bcd4a7eb88 |
| institution | Directory Open Access Journal |
| issn | 2296-4185 |
| language | English |
| last_indexed | 2024-04-12T09:46:19Z |
| publishDate | 2016-02-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Bioengineering and Biotechnology |
| spelling | doaj.art-2453fd70ad634fa6813546bcd4a7eb882022-12-22T03:37:56ZengFrontiers Media S.A.Frontiers in Bioengineering and Biotechnology2296-41852016-02-01410.3389/fbioe.2016.00005148480A new thermophilic nitrilase from an antarctic hyperthermophilic microorganism.Geraldine V. Dennett0Geraldine V. Dennett1Jenny M. Blamey2Jenny M. Blamey3Fundación BiocienciaUniversidad de Santiago de ChileFundación BiocienciaUniversidad de Santiago de ChileSeveral environmental samples from Antarctica were collected and enriched to search for microorganisms with nitrilase activity. A new thermostable nitrilase from a novel hyperthermophilic archaea Pyrococcus sp. M24D13 was purified and characterized. The activity of this enzyme increased as the temperatures rise from 70 up to 85 °C. Its optimal activity occurred at 85 °C and pH 7.5. This new enzyme shows a remarkable resistance to thermal inactivation retaining more than 50% of its activity even after 8 h of incubation at 85 °C.In addition, this nitrilase is highly versatile demonstrating activity towards different substrates such as benzonitrile (60 mM, aromatic nitrile) and butyronitrile (60 mM, aliphatic nitrile), with a specific activity of 3286.7 U mg-1 of protein and 4008.2 U mg-1 of protein respectively. Moreover the enzyme NitM24D13 also presents cyanidase activity.The apparent Michaelis-Menten constant (Km) and Vmáx of this Nitrilase for benzonitrile were 0.3 mM and 333.3 µM min-1, respectively, and the specificity constant (kcat/Km) for benzonitrile was 2.05×105 s-1 M-1.http://journal.frontiersin.org/Journal/10.3389/fbioe.2016.00005/fullNitrilesN-glycosylationThermostablecyanidasePyroccocus |
| spellingShingle | Geraldine V. Dennett Geraldine V. Dennett Jenny M. Blamey Jenny M. Blamey A new thermophilic nitrilase from an antarctic hyperthermophilic microorganism. Frontiers in Bioengineering and Biotechnology Nitriles N-glycosylation Thermostable cyanidase Pyroccocus |
| title | A new thermophilic nitrilase from an antarctic hyperthermophilic microorganism. |
| title_full | A new thermophilic nitrilase from an antarctic hyperthermophilic microorganism. |
| title_fullStr | A new thermophilic nitrilase from an antarctic hyperthermophilic microorganism. |
| title_full_unstemmed | A new thermophilic nitrilase from an antarctic hyperthermophilic microorganism. |
| title_short | A new thermophilic nitrilase from an antarctic hyperthermophilic microorganism. |
| title_sort | new thermophilic nitrilase from an antarctic hyperthermophilic microorganism |
| topic | Nitriles N-glycosylation Thermostable cyanidase Pyroccocus |
| url | http://journal.frontiersin.org/Journal/10.3389/fbioe.2016.00005/full |
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