Expression and characterization of thermotolerant lipase with broad pH profiles isolated from an AntarcticPseudomonassp strain AMS3

Author:

Latip Wahhida1,Raja Abd Rahman Raja Noor Zaliha12,Chor Leow Adam Thean13,Mohd Shariff Fairolniza12,Mohamad Ali Mohd Shukuri14

Affiliation:

1. Enzyme and Microbial Technology Research Center, Universiti Putra Malaysia, Serdang, Selangor, Malaysia

2. Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang, Selangor, Malaysia

3. Department of Cell and Molecular Biology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, UPM Serdang, Selangor, Malaysia

4. Department of Biochemistry, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang, Selangor, Malaysia

Abstract

A gene encoding a thermotolerant lipase with broad pH was isolated from an AntarcticPseudomonasstrain 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.

Funder

University Putra Malaysia

Publisher

PeerJ

Subject

General Agricultural and Biological Sciences,General Biochemistry, Genetics and Molecular Biology,General Medicine,General Neuroscience

Reference38 articles.

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