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

Chemical processing as a tool to generate ovalbumin variants with changed stability.

Hans A Kosters1, Kerensa Broersen, Jolan de Groot

  • 1Wageningen Centre for Food Sciences, Diedenweg 20, 6700 AN Wageningen, The Netherlands.

Biotechnology and Bioengineering
|August 12, 2003
PubMed
Summary

Controlled processing of ovalbumin can significantly alter denaturation temperature by over 23°C without affecting structural fold. Modifications like succinylation and lipophilization offer tunable protein functionality for various applications.

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

Organoids-on-a-chip: microfluidic technology enables culture of organoids with enhanced tissue function and potential for disease modeling.

Frontiers in bioengineering and biotechnology·2025
Same author

Biopurification using non-growing microorganisms to improve plant protein ingredients.

NPJ science of food·2024
Same author

The TNFR1 antagonist Atrosimab reduces neuronal loss, glial activation and memory deficits in an acute mouse model of neurodegeneration.

Scientific reports·2023
Same author

Robust Tissue Fabrication for Long-Term Culture of iPSC-Derived Brain Organoids for Aging Research.

Journal of visualized experiments : JoVE·2023
Same author

Alzheimer's Disease: Treatment Strategies and Their Limitations.

International journal of molecular sciences·2022
Same author

Use of standard U-bottom and V-bottom well plates to generate neuroepithelial embryoid bodies.

PloS one·2022

Area of Science:

  • Protein Chemistry
  • Biophysical Chemistry
  • Food Science

Background:

  • Ovalbumin processing can yield modified proteins with altered thermal stability.
  • Structural integrity is often maintained despite significant changes in denaturation temperature.

Purpose of the Study:

  • To investigate methods for modifying ovalbumin's denaturation temperature.
  • To understand the thermodynamic consequences of protein modifications.
  • To explore potential applications of modified ovalbumin.

Main Methods:

  • Protein modification techniques including succinylation, methylation, glycosylation, lipophilization, and S-ovalbumin processing.
  • Biochemical and spectroscopic analyses to assess structural fold.
  • Differential scanning calorimetry and guanidine-HCl denaturation curves to study thermodynamics.

Related Experiment Videos

  • Monitoring tryptophan fluorescence and ellipticity at 222 nm.

    • Main Results:

    • Modifications altered denaturation temperature by up to 23°C while preserving structural fold.
    • Thermodynamic impact varied based on the nature of the covalently coupled moiety.
    • A free energy change of approximately 1 kJ/mol/K was observed for modifications.
    • Lipophilized ovalbumin showed substantially lowered water-binding properties.

    Conclusions:

    • Controlled processing of ovalbumin enables significant modulation of thermal properties.
    • Protein modification offers a route to tailor protein functionality for specific applications.
    • Modified ovalbumin holds potential as a texturizer in food and medical industries.