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Title of Journal: Mol Biotechnol

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Abbravation: Molecular Biotechnology

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Springer US

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DOI

10.1007/bf00002179

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1559-0305

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Hydrophobic Substitution of Surface Residues Affec

Authors: Maryam Monsef Shokri Shahin Ahmadian Neda Akbari Khosro Khajeh
Publish Date: 2013/10/22
Volume: 56, Issue: 4, Pages: 360-368
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Abstract

A novel lipase has been recently isolated from a local Pseudomonas sp GQ243724 In the present study we have tried to increase the organic solvent stability of this lipase using sitedirected mutagenesis Eight variants N219L N219I N219P N219A N219R N219D S251L and S251K were designed to change the surface hydrophobicity of this enzyme with respect to the wildtype Among these variants the stability of N219L and N219I significantly increased in the presence of all tested organic solvents whereas two mutants N219R and N219D significantly exhibited decreased stabilities in all the organic solvent studied suggesting that improvement of hydrophobic patches on the enzyme surface enhances the stability in organic media Furthermore replacing Ser251 with hydrophobic residues on the enzyme surface dramatically diminished its stability in the tested condition In spite of the distance of the mutated sites from the active site the values of k cat and K m were affected Finally structural analysis of the wildtype and mutated variants was carried out in the presence and absence of some organic solvents using circular dichroism and fluorescence spectroscopy

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