Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Engineering an enzyme to resist boiling

B Van den Burg1, G Vriend, O R Veltman

  • 1Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren The Netherlands. burgb@biol.rug.nl

Proceedings of the National Academy of Sciences of the United States of America
|April 16, 1998
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Citius, Altius, Fortius.

Proteins·2020
Same author

Bio-knowledge-based filters improve residue-residue contact prediction accuracy.

Bioinformatics (Oxford, England)·2018
Same author

Forecasting residue-residue contact prediction accuracy.

Bioinformatics (Oxford, England)·2017
Same author

Correlated mutations select misfolded from properly folded proteins.

Bioinformatics (Oxford, England)·2017
Same author

Novel IRF6 Mutations Detected in Orofacial Cleft Patients by Targeted Massively Parallel Sequencing.

Journal of dental research·2016
Same author

GPCRdb: the G protein-coupled receptor database - an introduction.

British journal of pharmacology·2016
Same journal

Chemotactic self-organization captures the dynamics of mammalian hair follicle patterning.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Tomographic imaging of superconducting order using particle-hole interference.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Inhibitory potential of autologous neutralizing antibodies sets quantitative limits on the rebound-competent HIV-1 reservoir.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Inferring epidemiological parameters under an infectious phylogeography model with visitor dynamics.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Analytical modeling for suction cup designs for skin-interfaced wearable devices.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Improving cell-free metabolism through direct integration of artificial respiratory chains.

Proceedings of the National Academy of Sciences of the United States of America·2026
See all related articles

Researchers engineered a hyperstable enzyme, a thermolysin-like protease (TLP-ste), through targeted mutations. This enhanced enzyme functions at 100°C and retains activity at 37°C, offering a robust biocatalyst.

Area of Science:

  • Biochemistry
  • Enzymology
  • Protein Engineering

Background:

  • Enzymes from extremophiles offer insights into hyperstability.
  • Developing hyperstable biocatalysts is a key research goal.

Purpose of the Study:

  • To engineer a hyperstable enzyme from a moderately stable precursor.
  • To investigate the structural basis of enzyme hyperstability through mutagenesis.

Main Methods:

  • Site-directed mutagenesis of a thermolysin-like protease (TLP-ste).
  • Incorporation of mutations from naturally thermostable variants.
  • Rational design of mutations to enhance stability.

Main Results:

  • An 8-fold mutant TLP-ste enzyme exhibiting hyperstability was created.

Related Experiment Videos

  • The mutant enzyme functions effectively at 100°C and in denaturing conditions.
  • The engineered enzyme maintained wild-type-like activity at 37°C, unlike many natural hyperstable enzymes.

    • Conclusions:

    • Limited, strategic mutations can confer hyperstability to enzymes.
    • Engineered hyperstable enzymes can possess broad operational temperature ranges.
    • This approach yields robust biocatalysts with retained functionality.