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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Published in:International Journal of Molecular Sciences
Main Authors: Leelatulasi Salwoom, Raja Noor Zaliha Raja Abd. Rahman, Abu Bakar Salleh, Fairolniza Mohd. Shariff, Peter Convey, Mohd Shukuri Mohamad Ali
Format: Article in Journal/Newspaper
Language:English
Published: MDPI AG 2019
Subjects:
Online Access:https://doi.org/10.3390/ijms20061264
https://doaj.org/article/4507d4684a744a8dafa3ac97f759736c
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spelling 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
institution Open Polar
collection Directory of Open Access Journals: DOAJ Articles
op_collection_id ftdoajarticles
language English
topic Antarctica
cold adapted lipase
Pseudomonas sp. LSK25
purification
organic solvent tolerant
Biology (General)
QH301-705.5
Chemistry
QD1-999
spellingShingle 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
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