ArticleMolecular biotechnology2014
Hydrophobic substitution of surface residues affects lipase stability in organic solvents.
Article in Molecular biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Solvent Tolerance Improvement of Lipases Enhanced Their Applications: State of the Art.Molecules (Basel, Switzerland) · 2024Review
- Ion-Pair Interaction and Hydrogen Bonds as Main Features of Protein Thermostability in Mutated T1 Recombinant Lipase Originating fromMolecules (Basel, Switzerland) · 2020Article
- Filling the Void: Introducing Aromatic Interactions into Solvent Tunnels To Enhance Lipase Stability in Methanol.Applied and environmental microbiology · 2018Article
- From Protein Features to Sensing Surfaces.Sensors (Basel, Switzerland) · 2018Review
- Sortase A-mediated crosslinked short-chain dehydrogenases/reductases as novel biocatalysts with improved thermostability and catalytic efficiency.Scientific reports · 2017Article
- Recombinant Lipases and Phospholipases and Their Use as Biocatalysts for Industrial Applications.International journal of molecular sciences · 2015Review
- Adsorption/desorption and bioavailability of methamphetamine in simulated gastrointestinal fluids under the presence of multiwalled carbon nanotubes.Environmental science and pollution research international · 2015Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
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 site-directed 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 wild-type. 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 wild-type 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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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.