Expression and characterization of thermotolerant lipase with broad pH profiles isolated from an Antarctic Pseudomonassp strain AMS3
A gene encoding a thermotolerant lipase with broad pH was isolated from an Antarctic Pseudomonas strain AMS3. The recombinant lipase AMS3 was purified by single-step purification using affinity chromatography, yielding a purification fold of approximately 1.52 and a recovery of 50%. The molecular we...
| Published in: | PeerJ |
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| Main Authors: | , , , , |
| Other Authors: | |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
PeerJ
2016
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.7717/peerj.2420 https://peerj.com/articles/2420.pdf https://peerj.com/articles/2420.xml https://peerj.com/articles/2420.html |
| Summary: | A gene encoding a thermotolerant lipase with broad pH was isolated from an Antarctic Pseudomonas strain AMS3. The recombinant lipase AMS3 was purified by single-step purification using affinity chromatography, yielding a purification fold of approximately 1.52 and a recovery of 50%. The molecular weight was approximately ∼60 kDa including the strep and affinity tags. Interestingly, the purified Antarctic AMS3 lipase exhibited broad temperature profile from 10–70 °C and stable over a broad pH range from 5.0 to pH 10.0. Various mono and divalent metal ions increased the activity of the AMS3 lipase, but Ni 2+ decreased its activity. The purified lipase exhibited the highest activity in the presence of sunflower oil. In addition, the enzyme activity in 25% v/v solvents at 50 °C particularly to n-hexane, DMSO and methanol could be useful for catalysis reaction in organic solvent and at broad temperature. |
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