ArticleProtein science : a publication of the Protein Society2012
Biophysical characterization of mutants of Bacillus subtilis lipase evolved for thermostability: factors contributing to increased activity retention.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 60 citations in OpenAlex.
- Molecular Adaptations of Thermophilic Proteins-From Mechanistic Understanding to Machine Learning Approaches.ChemistryOpen · 2026Review
- Exploring the phylogeny, molecular and genomic adaptations of thermophilic microalgae and cyanobacteria.Planta · 2026Review
- FACS-Sortable Triple Emulsion Picoreactors for Screening Reactions in Biphasic Environments.Advanced materials interfaces · 2025Article
- Accurate Prediction of Enzyme Thermostabilization with Rosetta Using AlphaFold Ensembles.Journal of chemical information and modeling · 2023Article
- Thermostable lipases and their dynamics of improved enzymatic properties.Applied microbiology and biotechnology · 2021Review
- Machine Learning Enables Selection of Epistatic Enzyme Mutants for Stability Against Unfolding and Detrimental Aggregation.Chembiochem : a European journal of chemical biology · 2021Article
- Stabilizing AqdC, a Pseudomonas Quinolone Signal-Cleaving Dioxygenase from Mycobacteria, by FRESCO-Based Protein Engineering.Chembiochem : a European journal of chemical biology · 2021Article
- Direct production of a genetically-encoded immobilized biodiesel catalyst.Scientific reports · 2018Article
- The Lid Domain in Lipases: Structural and Functional Determinant of Enzymatic Properties.Frontiers in bioengineering and biotechnology · 2017Review
- Fluorescence spectroscopic analysis of the structure and dynamics of Bacillus subtilis lipase A governing its activity profile under alkaline conditions.European biophysics journal : EBJ · 2015Article
- Structural Rigidity and Protein Thermostability in Variants of Lipase A from Bacillus subtilis.PloS one · 2015Article
- Characterization of flavin-based fluorescent proteins: an emerging class of fluorescent reporters.PloS one · 2013Article
- Lipase improvement: goals and strategies.Computational and structural biotechnology journal · 2012Review
- Recent advances in rational approaches for enzyme engineering.Computational and structural biotechnology journal · 2012Review
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Previously, Lipase A from Bacillus subtilis was subjected to in vitro directed evolution using iterative saturation mutagenesis, with randomization sites chosen on the basis of the highest B-factors available from the crystal structure of the wild-type (WT) enzyme. This provided mutants that, unlike WT enzyme, retained a large part of their activity after heating above 65 °C and cooling down. Here, we subjected the three best mutants along with the WT enzyme to biophysical and biochemical characterization. Combining thermal inactivation profiles, circular dichroism, X-ray structure analyses and NMR experiments revealed that mutations of surface amino acid residues counteract the tendency of Lipase A to undergo precipitation under thermal stress. Reduced precipitation of the unfolding intermediates rather than increased conformational stability of the evolved mutants seems to be responsible for the activity retention.
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