ReviewApplied microbiology and biotechnology2022
Thermostability engineering of industrial enzymes through structure modification.
Review in Applied microbiology and biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 29 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
29 citing papers in PubMed.
- Rational Engineering of AKR13B3 fromInternational journal of molecular sciences · 2026Article
- Designing Novel Aspartic Protease (NAP) Using Ancestral Sequence Reconstruction (ASR) for Cheesemaking.Molecular biotechnology · 2026Article
- Deep Learning-Guided Engineering ofMicroorganisms · 2026Article
- Proteome-wide analysis of protein stability in Escherichia coli under acid stress.Journal of industrial microbiology & biotechnology · 2026Article
- In Silico Structural Insights into a Glucanase from Clostridium perfringens and Prediction of Structural Stability Improvement Through Hydrophobic Interaction Network and Aromatic Interaction.Molecular biotechnology · 2026Article
- DDGWizard: Integration of feature calculation resources for analysis and prediction of changes in protein thermostability upon point mutations.PLoS computational biology · 2025Article
- Thermostable Proteases fromMicroorganisms · 2025Review
- Engineering a novel carbaryl-degrading esterase from Bacillus velezensis for enhanced degradability via semi-rational design and whole-cell biocatalysis.World journal of microbiology & biotechnology · 2025Article
- Enzyme miniaturization: Revolutionizing future biocatalysts.Biotechnology advances · 2025Review
- Improving the thermostability and substrate affinity of3 Biotech · 2025Article
- Recent advances on protein engineering for improved stability.Biodesign research · 2025Review
- Improving the hydrophilic microenvironment surrounding the catalytic site of fructosyltransferase enhances its catalytic ability.Biotechnology letters · 2025Article
- Recent advances in phytase thermostability engineering towards potential application in the food and feed sectors.Food science and biotechnology · 2025Review
- Optimizing enzyme thermostability by combining multiple mutations using protein language model.mLife · 2024Article
- Enhancement of tryptophan 2-monooxygenase thermostability by semi-rational enzyme engineering: a strategic design to minimize experimental investigation.RSC chemical biology · 2024Article
- Synthetic co-culture in an interconnected two-compartment bioreactor system: violacein production with recombinant E. coli strains.Bioprocess and biosystems engineering · 2024Article
- Automated in vivo enzyme engineering accelerates biocatalyst optimization.Nature communications · 2024Review
- Application of an alchemical free energy method for the prediction of thermostable DuraPETase variants.Applied microbiology and biotechnology · 2024Article
- A novel thermotolerant L-rhamnose isomerase variant for biocatalytic conversion of D-allulose to D-allose.Applied microbiology and biotechnology · 2024Article
- A Bibliometric Analysis: Current Perspectives and Potential Trends of Enzyme Thermostability from 1991-2022.Applied biochemistry and biotechnology · 2024Article
Corrections and comments
- Erratum issued
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thermostability is an essential requirement of enzymes in the industrial processes to catalyze the reactions at high temperatures; thus, enzyme engineering through directed evolution, semi-rational design and rational design are commonly employed to construct desired thermostable mutants. Several strategies are implemented to fulfill enzymes' thermostability demand including decreasing the entropy of the unfolded state through substitutions Gly → Xxx or Xxx → Pro, hydrogen bond, salt bridge, introducing two different simultaneous interactions through single mutant, hydrophobic interaction, filling the hydrophobic cavity core, decreasing surface hydrophobicity, truncating loop, aromatic-aromatic interaction and introducing positively charged residues to enzyme surface. In the current review, horizons about compatibility between secondary structures and substitutions at preferable structural positions to generate the most desirable thermostability in industrial enzymes are broadened. KEY POINTS: • Protein engineering is a powerful tool for generating thermostable industrial enzymes. • Directed evolution and rational design are practical approaches in enzyme engineering. • Substitutions in preferable structural positions can increase thermostability.
Indexed as
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35804158What OpenQuestion holds
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.