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 fromSigny Station, SouthOrkney Islands,maritime Antarctic....

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Published in:International Journal of Molecular Sciences
Main Authors: Salwoom, Leelatulasi, Rahman, Raja Noor Zaliha Raja Abd., Salleh, Abu Bakar, Shariff, Fairolniza Mohd., Convey, Peter, Ali, Mohd Shukuri Mohamad
Format: Article in Journal/Newspaper
Language:English
Published: MDPI 2019
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Online Access:http://nora.nerc.ac.uk/id/eprint/521996/
https://nora.nerc.ac.uk/id/eprint/521996/1/ijms-20-01264.pdf
https://www.mdpi.com/1422-0067/20/6/1264
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spelling ftnerc:oai:nora.nerc.ac.uk:521996 2023-05-15T13:41:42+02:00 New recombinant cold-adapted and organic solvent tolerant lipase from psychrophilic Pseudomonas sp. LSK25, isolated from Signy Island Antarctica Salwoom, Leelatulasi Rahman, Raja Noor Zaliha Raja Abd. Salleh, Abu Bakar Shariff, Fairolniza Mohd. Convey, Peter Ali, Mohd Shukuri Mohamad 2019-03 text http://nora.nerc.ac.uk/id/eprint/521996/ https://nora.nerc.ac.uk/id/eprint/521996/1/ijms-20-01264.pdf https://www.mdpi.com/1422-0067/20/6/1264 en eng MDPI https://nora.nerc.ac.uk/id/eprint/521996/1/ijms-20-01264.pdf Salwoom, Leelatulasi; Rahman, Raja Noor Zaliha Raja Abd.; Salleh, Abu Bakar; Shariff, Fairolniza Mohd.; Convey, Peter orcid:0000-0001-8497-9903 Ali, Mohd Shukuri Mohamad. 2019 New recombinant cold-adapted and organic solvent tolerant lipase from psychrophilic Pseudomonas sp. LSK25, isolated from Signy Island Antarctica. International Journal of Molecular Sciences, 20 (6), 1264. https://doi.org/10.3390/ijms20061264 <https://doi.org/10.3390/ijms20061264> cc_by_4 CC-BY Publication - Article PeerReviewed 2019 ftnerc https://doi.org/10.3390/ijms20061264 2023-02-04T19:47:38Z 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 fromSigny Station, SouthOrkney 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 Natural Environment Research Council: NERC Open Research Archive Antarctic Signy Island ENVELOPE(-45.595,-45.595,-60.708,-60.708) International Journal of Molecular Sciences 20 6 1264
institution Open Polar
collection Natural Environment Research Council: NERC Open Research Archive
op_collection_id ftnerc
language English
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 fromSigny Station, SouthOrkney 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 Salwoom, Leelatulasi
Rahman, Raja Noor Zaliha Raja Abd.
Salleh, Abu Bakar
Shariff, Fairolniza Mohd.
Convey, Peter
Ali, Mohd Shukuri Mohamad
spellingShingle Salwoom, Leelatulasi
Rahman, Raja Noor Zaliha Raja Abd.
Salleh, Abu Bakar
Shariff, Fairolniza Mohd.
Convey, Peter
Ali, Mohd Shukuri Mohamad
New recombinant cold-adapted and organic solvent tolerant lipase from psychrophilic Pseudomonas sp. LSK25, isolated from Signy Island Antarctica
author_facet Salwoom, Leelatulasi
Rahman, Raja Noor Zaliha Raja Abd.
Salleh, Abu Bakar
Shariff, Fairolniza Mohd.
Convey, Peter
Ali, Mohd Shukuri Mohamad
author_sort Salwoom, Leelatulasi
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
publishDate 2019
url http://nora.nerc.ac.uk/id/eprint/521996/
https://nora.nerc.ac.uk/id/eprint/521996/1/ijms-20-01264.pdf
https://www.mdpi.com/1422-0067/20/6/1264
long_lat ENVELOPE(-45.595,-45.595,-60.708,-60.708)
geographic Antarctic
Signy Island
geographic_facet Antarctic
Signy Island
genre Antarc*
Antarctic
Antarctica
Signy Island
genre_facet Antarc*
Antarctic
Antarctica
Signy Island
op_relation https://nora.nerc.ac.uk/id/eprint/521996/1/ijms-20-01264.pdf
Salwoom, Leelatulasi; Rahman, Raja Noor Zaliha Raja Abd.; Salleh, Abu Bakar; Shariff, Fairolniza Mohd.; Convey, Peter orcid:0000-0001-8497-9903
Ali, Mohd Shukuri Mohamad. 2019 New recombinant cold-adapted and organic solvent tolerant lipase from psychrophilic Pseudomonas sp. LSK25, isolated from Signy Island Antarctica. International Journal of Molecular Sciences, 20 (6), 1264. https://doi.org/10.3390/ijms20061264 <https://doi.org/10.3390/ijms20061264>
op_rights cc_by_4
op_rightsnorm CC-BY
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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