New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from Psychrophilic Pseudomonas sp. LSK25, Isolated from Signy Island Antarctica
In recent years, studies on psychrophilic lipases have become an emerging area of research in the field of enzymology. The study described here focuses on the cold-adapted organic solvent tolerant lipase strain Pseudomonas sp. LSK25 isolated from Signy Station, South Orkney Islands, maritime Antarct...
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ftdoajarticles:oai:doaj.org/article:4507d4684a744a8dafa3ac97f759736c 2023-05-15T13:51:26+02:00 New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from Psychrophilic Pseudomonas sp. LSK25, Isolated from Signy Island Antarctica Leelatulasi Salwoom Raja Noor Zaliha Raja Abd. Rahman Abu Bakar Salleh Fairolniza Mohd. Shariff Peter Convey Mohd Shukuri Mohamad Ali 2019-03-01T00:00:00Z https://doi.org/10.3390/ijms20061264 https://doaj.org/article/4507d4684a744a8dafa3ac97f759736c EN eng MDPI AG http://www.mdpi.com/1422-0067/20/6/1264 https://doaj.org/toc/1422-0067 1422-0067 doi:10.3390/ijms20061264 https://doaj.org/article/4507d4684a744a8dafa3ac97f759736c International Journal of Molecular Sciences, Vol 20, Iss 6, p 1264 (2019) Antarctica cold adapted lipase Pseudomonas sp. LSK25 purification organic solvent tolerant Biology (General) QH301-705.5 Chemistry QD1-999 article 2019 ftdoajarticles https://doi.org/10.3390/ijms20061264 2022-12-31T05:17:39Z In recent years, studies on psychrophilic lipases have become an emerging area of research in the field of enzymology. The study described here focuses on the cold-adapted organic solvent tolerant lipase strain Pseudomonas sp. LSK25 isolated from Signy Station, South Orkney Islands, maritime Antarctic. Strain LSK25 lipase was successfully cloned, sequenced, and over-expressed in an Escherichia coli system. Sequence analysis revealed that the lipase gene of Pseudomonas sp. LSK25 consists of 1432 bp, lacks an N-terminal signal peptide and encodes a mature protein consisting of 476 amino acids. The recombinant LSK25 lipase was purified by single-step purification using Ni-Sepharose affinity chromatography and had a molecular mass of approximately 65 kDa. The final recovery and purification fold were 44% and 1.3, respectively. The LSK25 lipase was optimally active at 30 °C and at pH 6. Stable lipolytic activity was reported between temperatures of 5–30 °C and at pH 6–8. A significant enhancement of lipolytic activity was observed in the presence of Ca2+ ions, the organic lipids of rice bran oil and coconut oil, a synthetic C12 ester and a wide range of water immiscible organic solvents. Overall, lipase strain LSK25 is a potentially desirable candidate for biotechnological application, due to its stability at low temperatures, across a range of pH and in organic solvents. Article in Journal/Newspaper Antarc* Antarctic Antarctica Signy Island South Orkney Islands Directory of Open Access Journals: DOAJ Articles Antarctic South Orkney Islands ENVELOPE(-45.500,-45.500,-60.583,-60.583) Signy Island ENVELOPE(-45.595,-45.595,-60.708,-60.708) Signy Station ENVELOPE(-45.600,-45.600,-60.717,-60.717) International Journal of Molecular Sciences 20 6 1264 |
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Directory of Open Access Journals: DOAJ Articles |
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English |
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Antarctica cold adapted lipase Pseudomonas sp. LSK25 purification organic solvent tolerant Biology (General) QH301-705.5 Chemistry QD1-999 |
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Antarctica cold adapted lipase Pseudomonas sp. LSK25 purification organic solvent tolerant Biology (General) QH301-705.5 Chemistry QD1-999 Leelatulasi Salwoom Raja Noor Zaliha Raja Abd. Rahman Abu Bakar Salleh Fairolniza Mohd. Shariff Peter Convey Mohd Shukuri Mohamad Ali New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from Psychrophilic Pseudomonas sp. LSK25, Isolated from Signy Island Antarctica |
topic_facet |
Antarctica cold adapted lipase Pseudomonas sp. LSK25 purification organic solvent tolerant Biology (General) QH301-705.5 Chemistry QD1-999 |
description |
In recent years, studies on psychrophilic lipases have become an emerging area of research in the field of enzymology. The study described here focuses on the cold-adapted organic solvent tolerant lipase strain Pseudomonas sp. LSK25 isolated from Signy Station, South Orkney Islands, maritime Antarctic. Strain LSK25 lipase was successfully cloned, sequenced, and over-expressed in an Escherichia coli system. Sequence analysis revealed that the lipase gene of Pseudomonas sp. LSK25 consists of 1432 bp, lacks an N-terminal signal peptide and encodes a mature protein consisting of 476 amino acids. The recombinant LSK25 lipase was purified by single-step purification using Ni-Sepharose affinity chromatography and had a molecular mass of approximately 65 kDa. The final recovery and purification fold were 44% and 1.3, respectively. The LSK25 lipase was optimally active at 30 °C and at pH 6. Stable lipolytic activity was reported between temperatures of 5–30 °C and at pH 6–8. A significant enhancement of lipolytic activity was observed in the presence of Ca2+ ions, the organic lipids of rice bran oil and coconut oil, a synthetic C12 ester and a wide range of water immiscible organic solvents. Overall, lipase strain LSK25 is a potentially desirable candidate for biotechnological application, due to its stability at low temperatures, across a range of pH and in organic solvents. |
format |
Article in Journal/Newspaper |
author |
Leelatulasi Salwoom Raja Noor Zaliha Raja Abd. Rahman Abu Bakar Salleh Fairolniza Mohd. Shariff Peter Convey Mohd Shukuri Mohamad Ali |
author_facet |
Leelatulasi Salwoom Raja Noor Zaliha Raja Abd. Rahman Abu Bakar Salleh Fairolniza Mohd. Shariff Peter Convey Mohd Shukuri Mohamad Ali |
author_sort |
Leelatulasi Salwoom |
title |
New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from Psychrophilic Pseudomonas sp. LSK25, Isolated from Signy Island Antarctica |
title_short |
New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from Psychrophilic Pseudomonas sp. LSK25, Isolated from Signy Island Antarctica |
title_full |
New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from Psychrophilic Pseudomonas sp. LSK25, Isolated from Signy Island Antarctica |
title_fullStr |
New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from Psychrophilic Pseudomonas sp. LSK25, Isolated from Signy Island Antarctica |
title_full_unstemmed |
New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from Psychrophilic Pseudomonas sp. LSK25, Isolated from Signy Island Antarctica |
title_sort |
new recombinant cold-adapted and organic solvent tolerant lipase from psychrophilic pseudomonas sp. lsk25, isolated from signy island antarctica |
publisher |
MDPI AG |
publishDate |
2019 |
url |
https://doi.org/10.3390/ijms20061264 https://doaj.org/article/4507d4684a744a8dafa3ac97f759736c |
long_lat |
ENVELOPE(-45.500,-45.500,-60.583,-60.583) ENVELOPE(-45.595,-45.595,-60.708,-60.708) ENVELOPE(-45.600,-45.600,-60.717,-60.717) |
geographic |
Antarctic South Orkney Islands Signy Island Signy Station |
geographic_facet |
Antarctic South Orkney Islands Signy Island Signy Station |
genre |
Antarc* Antarctic Antarctica Signy Island South Orkney Islands |
genre_facet |
Antarc* Antarctic Antarctica Signy Island South Orkney Islands |
op_source |
International Journal of Molecular Sciences, Vol 20, Iss 6, p 1264 (2019) |
op_relation |
http://www.mdpi.com/1422-0067/20/6/1264 https://doaj.org/toc/1422-0067 1422-0067 doi:10.3390/ijms20061264 https://doaj.org/article/4507d4684a744a8dafa3ac97f759736c |
op_doi |
https://doi.org/10.3390/ijms20061264 |
container_title |
International Journal of Molecular Sciences |
container_volume |
20 |
container_issue |
6 |
container_start_page |
1264 |
_version_ |
1766255297556381696 |