Expression and characterization of thermotolerant lipase with broad pH profiles isolated from an Antarctic Pseudomonas sp strain AMS3

• Published in: PeerJ
• Main Authors: Wahhida Latip, Raja Noor Zaliha Raja Abd Rahman, Adam Thean Chor Leow, Fairolniza Mohd Shariff, Mohd Shukuri Mohamad Ali
• Format: Article in Journal/Newspaper
• Language: English
• Published: PeerJ Inc. 2016
• Subjects: Thermotolerant lipase; Expression and characterization; Medicine; R; Biology (General); QH301-705.5; Antarctic; Antarc*
• Online Access: https://doi.org/10.7717/peerj.2420; https://doaj.org/article/d36576dedc834725bbdfb0273b0e86af

A gene encoding a thermotolerant lipase with broad pH was isolated from an Antarctic Pseudomonas strain AMS3. The recombinant lipase AMS3 was purified by single-step purification using affinity chromatography, yielding a purification fold of approximately 1.52 and a recovery of 50%. The molecular weight was approximately ∼60 kDa including the strep and affinity tags. Interestingly, the purified Antarctic AMS3 lipase exhibited broad temperature profile from 10–70 °C and stable over a broad pH range from 5.0 to pH 10.0. Various mono and divalent metal ions increased the activity of the AMS3 lipase, but Ni2+ decreased its activity. The purified lipase exhibited the highest activity in the presence of sunflower oil. In addition, the enzyme activity in 25% v/v solvents at 50 °C particularly to n-hexane, DMSO and methanol could be useful for catalysis reaction in organic solvent and at broad temperature.