ArticleBMC bioinformatics2012
Improving the thermostability of alpha-amylase by combinatorial coevolving-site saturation mutagenesis.
Article in BMC bioinformatics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Overcoming cellular secretion bottlenecks: advanced secretion engineering and molecular tailoring for next-generation microbial α-amylases with enhanced industrial performance.World journal of microbiology & biotechnology · 2026Review
- Combing Directed Enzyme Evolution with Metabolic Engineering to Develop Efficient Microbial Cell Factories.Chem & bio engineering · 2025Review
- Enzyme Engineering: Performance Optimization, Novel Sources, and Applications in the Food Industry.Foods (Basel, Switzerland) · 2024Review
- Identification, Characterization, and Computer-Aided Rational Design of a Novel Thermophilic Esterase from Geobacillus subterraneus, and Application in the Synthesis of Cinnamyl Acetate.Applied biochemistry and biotechnology · 2024Article
- Modulating Glycoside Hydrolase Activity between Hydrolysis and Transfer Reactions Using an Evolutionary Approach.Molecules (Basel, Switzerland) · 2021Article
- Review
- Methods and Applications of CRISPR-Mediated Base Editing in Eukaryotic Genomes.Molecular cell · 2017Review
- Correlated positions in protein evolution and engineering.Journal of industrial microbiology & biotechnology · 2017Review
- Co-evolution techniques are reshaping the way we do structural bioinformatics.F1000Research · 2017Review
- HotSpot Wizard 2.0: automated design of site-specific mutations and smart libraries in protein engineering.Nucleic acids research · 2016Article
- Improvement of biocatalysts for industrial and environmental purposes by saturation mutagenesis.Biomolecules · 2013Article
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundThe generation of focused mutant libraries at hotspot residues is an important strategy in directed protein evolution. Existing methods, such as combinatorial active site testing and residual coupling analysis, depend primarily on the evolutionary conserved information to find the hotspot residues. Hardly any attention has been paid to another important functional and structural determinants, the functionally correlated variation information--coevolution.
resultsIn this paper, we suggest a new method, named combinatorial coevolving-site saturation mutagenesis (CCSM), in which the functionally correlated variation sites of proteins are chosen as the hotspot sites to construct focused mutant libraries. The CCSM approach was used to improve the thermal stability of α-amylase from Bacillus subtilis CN7 (Amy7C). The results indicate that the CCSM can identify novel beneficial mutation sites, and enhance the thermal stability of wild-type Amy7C by 8°C ( T5030), which could not be achieved with the ordinarily rational introduction of single or a double point mutation.
conclusionsOur method is able to produce more thermostable mutant α-amylases with novel beneficial mutations at new sites. It is also verified that the coevolving sites can be used as the hotspots to construct focused mutant libraries in protein engineering. This study throws new light on the active researches of the molecular coevolution.
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