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...
Published in: | International Journal of Molecular Sciences |
---|---|
Main Authors: | , , , , , |
Format: | Text |
Language: | English |
Published: |
Multidisciplinary Digital Publishing Institute
2019
|
Subjects: | |
Online Access: | https://doi.org/10.3390/ijms20061264 |
id |
ftmdpi:oai:mdpi.com:/1422-0067/20/6/1264/ |
---|---|
record_format |
openpolar |
spelling |
ftmdpi:oai:mdpi.com:/1422-0067/20/6/1264/ 2023-08-20T04:00:55+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 agris 2019-03-13 application/pdf https://doi.org/10.3390/ijms20061264 EN eng Multidisciplinary Digital Publishing Institute Molecular Biophysics https://dx.doi.org/10.3390/ijms20061264 https://creativecommons.org/licenses/by/4.0/ International Journal of Molecular Sciences; Volume 20; Issue 6; Pages: 1264 Antarctica cold adapted lipase Pseudomonas sp. LSK25 purification organic solvent tolerant Text 2019 ftmdpi https://doi.org/10.3390/ijms20061264 2023-07-31T22:06:41Z 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. Text Antarc* Antarctic Antarctica Signy Island South Orkney Islands MDPI Open Access Publishing Antarctic Signy Island ENVELOPE(-45.595,-45.595,-60.708,-60.708) Signy Station ENVELOPE(-45.600,-45.600,-60.717,-60.717) South Orkney Islands ENVELOPE(-45.500,-45.500,-60.583,-60.583) International Journal of Molecular Sciences 20 6 1264 |
institution |
Open Polar |
collection |
MDPI Open Access Publishing |
op_collection_id |
ftmdpi |
language |
English |
topic |
Antarctica cold adapted lipase Pseudomonas sp. LSK25 purification organic solvent tolerant |
spellingShingle |
Antarctica cold adapted lipase Pseudomonas sp. LSK25 purification organic solvent tolerant 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 |
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 |
Text |
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 |
Multidisciplinary Digital Publishing Institute |
publishDate |
2019 |
url |
https://doi.org/10.3390/ijms20061264 |
op_coverage |
agris |
long_lat |
ENVELOPE(-45.595,-45.595,-60.708,-60.708) ENVELOPE(-45.600,-45.600,-60.717,-60.717) ENVELOPE(-45.500,-45.500,-60.583,-60.583) |
geographic |
Antarctic Signy Island Signy Station South Orkney Islands |
geographic_facet |
Antarctic Signy Island Signy Station South Orkney Islands |
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; Volume 20; Issue 6; Pages: 1264 |
op_relation |
Molecular Biophysics https://dx.doi.org/10.3390/ijms20061264 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
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_ |
1774721339533295616 |