ArticleInternational journal of biological macromolecules2020
Semi-rational design and molecular dynamics simulations study of the thermostability enhancement of cellobiose 2-epimerases.
Article in International journal of biological macromolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.
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Who cites it
12 citing papers in PubMed, 1 synthesis or guideline pooled it, 56 citations in OpenAlex.
- Computer-Aided Lipase Engineering for Improving Their Stability and Activity in the Food Industry: State of the Art.Molecules (Basel, Switzerland) · 2023Pooled it
- Temperature-Dependent Thumb Domain Dynamics of Xylanase TsaGH11: Insights from Molecular Dynamics Simulations.International journal of molecular sciences · 2026Article
- Improving the Thermostability of the Qβ Bacteriophage Coat Protein Through Single-Site Mutation Based on Molecular Dynamics.International journal of molecular sciences · 2026Article
- Synergistic, theoretical, and experimental study of the interaction of a tri-heterometallic polymer with bovine liver catalase.RSC advances · 2025Article
- Activating the d-Tagatose Production Capacity ofJournal of agricultural and food chemistry · 2025Article
- A Bibliometric Analysis: Current Perspectives and Potential Trends of Enzyme Thermostability from 1991-2022.Applied biochemistry and biotechnology · 2024Article
- SERS-based microdroplet platform for high-throughput screening ofFrontiers in bioengineering and biotechnology · 2024Article
- Bioengineered Enzymes and Precision Fermentation in the Food Industry.International journal of molecular sciences · 2023Review
- Thermostability enhancement and insight of L-asparaginase from Mycobacterium sp. via consensus-guided engineering.Applied microbiology and biotechnology · 2023Article
- Zearalenone lactonase: characteristics, modification, and application.Applied microbiology and biotechnology · 2022Review
- Thermostability Improvement of L-Asparaginase fromMolecules (Basel, Switzerland) · 2022Article
- Characterization of a Novel Mannose Isomerase from Stenotrophomonas rhizophila and Identification of Its Possible Catalytic Residues.Molecular biotechnology · 2022Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Directed evolution using random mutation in vast sequence space leads to the low probability of obtaining target proteins. Emerging engineering strategies with computational tools are developed for more trustable outcomes. We used some semi-rational design methods to modify an industrial enzyme, namely cellobiose 2-epimerase (CE). A mutant was selected for its better thermostability and isomerization activity. The tradeoffs between thermostability, epimerization activity and isomerization activity of the CE mutants were different. To investigate the computational prediction performance of protein stability upon point mutations, molecular dynamics (MD) simulation analyses were conducted. The root mean square deviation (RMSD) and hydrogen bond analyses reproduced the correct trends in stability changes of the wild-type and mutated CEs with relatively high accuracy (correlation coefficients r ~ 0.5-0.8). The simulation temperature and time are important factors that influence the prediction performance. Our result shows that thermostability predictors calculated from MD simulation do better in predicting the thermostability changes of the mutated enzymes than the predictors using static-state information of the enzymes.
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