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

Stability of enzymes.

M P Tombs

    Journal of Applied Biochemistry
    |February 1, 1985
    PubMed
    Summary

    Enzyme stability, crucial for function, can be predicted by thermal denaturation midpoint temperature (Tm). Tm is a reliable indicator of enzyme turnover and resistance to unfolding, even when amino acid sequence changes are complex.

    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

    Myofibrils, sarcoplasmic reticulum and phosphorylase kinase of Pietrain and Large White-landrace pigs.

    Meat science·2011
    Same author

    Biotechnology of protein and polysaccharide gels.

    Biotechnology & genetic engineering reviews·1997
    Same author

    Predicting the phase diagram for a gelatin-pectin system.

    Biochemical Society transactions·1995
    Same author

    Solution behaviour of Chromobacter viscosum and Pseudomonas sp. lipases. No evidence of self-association.

    The Biochemical journal·1991
    Same author

    Hydrodynamic characterization of Chromobacter viscosum lipase.

    Biochemical Society transactions·1990
    Same author

    Preparation of fluorescent derivatives of lipases and their use in fluorescence energy transfer studies in hydrocarbon/water interfaces.

    Biochimica et biophysica acta·1987

    Area of Science:

    • Biochemistry and Molecular Biology
    • Protein Chemistry
    • Enzyme Kinetics

    Background:

    • Enzymes lose activity via covalent and noncovalent structural changes, including protease attack and oxidation.
    • Enzyme conformational stability is critical for maintaining biological activity and in vivo turnover.
    • Thermal denaturation midpoint temperature (Tm) is a key metric for assessing protein stability.

    Purpose of the Study:

    • To explore the relationship between enzyme structure, stability, and activity.
    • To evaluate Tm as a predictive measure for enzyme stability and in vivo performance.
    • To investigate the thermodynamic parameters governing enzyme unfolding.

    Main Methods:

    • Measurement of Tm, the midpoint temperature of thermal denaturation curves.
    • Analysis of heat capacity changes (delta Cp) to determine thermodynamic parameters (delta H, T delta S, delta G).
    • Correlation of Tm with in vivo enzyme turnover and guanidine unfolding concentration ([G]1/2).

    Main Results:

    • Tm directly correlates with in vivo enzyme turnover.
    • Thermodynamic analysis of unfolding provides insights into stability (delta G).
    • Tm is identified as the most reliable predictor of enzyme stability, outperforming predictions based solely on amino acid sequence.

    Conclusions:

    • Tm is a robust and practical measure for predicting enzyme stability and performance.
    • While amino acid sequence influences stability, predicting the precise impact of mutations remains challenging.
    • Understanding enzyme unfolding thermodynamics, particularly Tm, is essential for enzyme engineering and applications.

    Related Experiment Videos