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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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Main Authors: Salwoom, Leelatulasi, Raja Abdul Rahman, Raja Noor Zaliha, Salleh, Abu Bakar, Mohd Shariff, Fairolniza, Convey, Peter, Mohamad Ali, Mohd Shukuri
Format: Article
Language:English
Published: MDPI 2019
Online Access:http://psasir.upm.edu.my/id/eprint/38418/1/38418.pdf
http://psasir.upm.edu.my/id/eprint/38418/
https://www.mdpi.com/1422-0067/20/6/1264
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spelling my.upm.eprints.384182020-05-04T16:53:30Z http://psasir.upm.edu.my/id/eprint/38418/ New recombinant cold-adapted and organic solvent tolerant lipase from psychrophilic Pseudomonas sp. LSK25, isolated from Signy Island Antarctica Salwoom, Leelatulasi Raja Abdul Rahman, Raja Noor Zaliha Salleh, Abu Bakar Mohd Shariff, Fairolniza Convey, Peter Mohamad Ali, Mohd Shukuri 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. MDPI 2019 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/38418/1/38418.pdf Salwoom, Leelatulasi and Raja Abdul Rahman, Raja Noor Zaliha and Salleh, Abu Bakar and Mohd Shariff, Fairolniza and Convey, Peter and Mohamad Ali, Mohd Shukuri (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). art. no. 1264. pp. 1-21. ISSN 1661-6596; ESSN: 1422-0067 https://www.mdpi.com/1422-0067/20/6/1264 10.3390/ijms20061264
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
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 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
author Salwoom, Leelatulasi
Raja Abdul Rahman, Raja Noor Zaliha
Salleh, Abu Bakar
Mohd Shariff, Fairolniza
Convey, Peter
Mohamad Ali, Mohd Shukuri
spellingShingle Salwoom, Leelatulasi
Raja Abdul Rahman, Raja Noor Zaliha
Salleh, Abu Bakar
Mohd Shariff, Fairolniza
Convey, Peter
Mohamad Ali, Mohd Shukuri
New recombinant cold-adapted and organic solvent tolerant lipase from psychrophilic Pseudomonas sp. LSK25, isolated from Signy Island Antarctica
author_facet Salwoom, Leelatulasi
Raja Abdul Rahman, Raja Noor Zaliha
Salleh, Abu Bakar
Mohd Shariff, Fairolniza
Convey, Peter
Mohamad Ali, Mohd Shukuri
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://psasir.upm.edu.my/id/eprint/38418/1/38418.pdf
http://psasir.upm.edu.my/id/eprint/38418/
https://www.mdpi.com/1422-0067/20/6/1264
_version_ 1665895984403578880
score 13.211869

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