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New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from Psychrophilic Pseudomonas sp. LSK25, Isolated from Signy Island Antarctica

1
Enzyme and Microbial Technology Research Center, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang Selangor 43400, Malaysia
2
National Antarctic Research Centre (NARC) B303, Block B, Level 3, IPS Building, University of Malaya, Kuala Lumpur 50603, Malaysia
3
Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang Selangor 43400, Malaysia
4
British Antarctic Survey, NERC, High Cross, Madingley Road, Cambridge CB3 OET, UK
5
Department of Biochemistry, Faculty of Biotechnology and Biomolecular Science, Universiti Putra Malaysia, Serdang Selangor 43400, Malaysia
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2019, 20(6), 1264; https://doi.org/10.3390/ijms20061264
Received: 12 January 2019 / Revised: 30 January 2019 / Accepted: 10 February 2019 / Published: 13 March 2019
(This article belongs to the Special Issue Industrial Enzymes: Structure, Function and Applications)
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Abstract

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. View Full-Text
Keywords: Antarctica; cold adapted lipase; Pseudomonas sp. LSK25; purification; organic solvent tolerant Antarctica; cold adapted lipase; Pseudomonas sp. LSK25; purification; organic solvent tolerant
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Salwoom, L.; Raja Abd. Rahman, R.N.Z.; Salleh, A.B.; Mohd. Shariff, F.; Convey, P.; Mohamad Ali, M.S. New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from Psychrophilic Pseudomonas sp. LSK25, Isolated from Signy Island Antarctica. Int. J. Mol. Sci. 2019, 20, 1264.

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