Related Experiment Video
Updated: Jul 13, 2026

Comparison of Tobacco Host Cell Protein Removal Methods by Blanching Intact Plants or by Heat Treatment of Extracts
Published on: August 8, 2016
Interfacial properties of heat-treated ovalbumin
Thomas Croguennec1, Anne Renault, Sylvie Beaufils
1INRA-Agrocampus, UMR1253, Science & Technologie du lait et de l'oeuf, 65 rue St Brieuc, F-35000 Rennes, France. thomas.croguennec@agrocampus-rennes.fr
Abstract:
The interfacial properties (kinetics of adsorption at the air/water interface, rheology of the interfacial layer) of ovalbumin molecules, unheated or previously heat-denatured in solution (10 g L(-1), pH 7, NaCl 50 mM) under controlled conditions (up to 40 min at 80 degrees C), were investigated. Heat treatments induced the formation of covalent aggregates which surface exhibits a higher hydrophobicity and an increased exposition of sulfhydryl groups when compared to native ovalbumin (unheated). Although they have a larger hydrodynamic size, aggregates adsorb as fast as native ovalbumin at the air/water interface. However, aggregates are able to established rapid contacts in the interfacial layer as shown by the fast increase of both surface pressure and shear elastic constant. In contrast, native ovalbumin needs longer time to developed intermolecular contacts and exhibits lower foam stability even if the shear elastic constant on aging reached higher value than for ovalbumin aggregates.
More Related Videos
10:20In vitro Digestion of Emulsions in a Single Droplet via Multi Subphase Exchange of Simulated Gastrointestinal Fluids
Published on: November 18, 2022
06:02Cationic Nanoemulsion-Encapsulated Retinoic Acid as an Adjuvant to Promote OVA-Specific Systemic and Mucosal Responses
Published on: February 23, 2024
Related Concept Videos
Aqueous Solutions and Heats of Hydration
When ionic compounds dissolve in water, the ions in the solid separate and disperse uniformly throughout the solution because water molecules surround and solvate the ions, reducing the strong electrostatic forces between them. This process...
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...
Globular Proteins
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...