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ISSN: 2169-0111

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Research Article

Engineering of A Lipase towards Thermostability: Studies on Additive Effect of the two Thermo-Stabilising Mutations at Protein Surface

Rakesh K1, Nisha C2, Ranvir S2, Pushpender KS2, Jagdeep K2*
1Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore-560012, India
2Department of biotechnology Panjab University Chandigarh, India
Corresponding Author : Jagdeep Kaur
Department Of Biotechnology, BMS Block-1
Panjab University, South Campus, Sector 25
Chandigarh 160014, India
Tel: 91-172-2534085
Fax: +91-172-2541409
E-mail: [email protected]
Received: June 17, 2015 Accepted: July 29, 2015 Published: August 3, 2015
Citation: Rakesh K, Nisha C, Ranvir S, Pushpender K, Jagdeep K (2015) Engineering of A Lipase towards Thermostability: Studies on Additive Effect of the two Thermo-Stabilising Mutations at Protein Surface. Adv Genet Eng 4:126. doi:10.4172/2169-0111.1000126
Copyright: © 2015 Rakesh, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Abstract

In this study we have showed combined effect of two single point mutations S311C (LipR2) and R214C (LipR3) on the protein stability and overall change in biochemical properties. We found that both of these mutations are near the surface and individually enhanced the thermal stability of the protein (T1/2 for S311C=4.5 h & R214C=7 h at 60°C). But, their combined effect was not additive on thermostability. T1/2 of double mutant (LipR2 + LipR3) was 4 h at 60°C. Circular dichroism (CD) and fluorescence studies also supported our findings. Homology modelling studies demonstrated that in double mutant (LipR4) side chain of Cys311 is protruding towards the bulk solvent and is easily available for oxidation of sulfahydril group. This might be the reason for its low thermostability as compared to LipR3. We also observed that, side chains of Cys 214 didn’t changed. Here, one of the Cystein (Cys311) is behaving like a hydrophilic residue while the other (Cys 214) is behaving like hydrophobic residue.

Keywords:

Lipase; Thermostability; Mutations; Enzyme; Nucleotide sequence

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