Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein Organization

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

Protein Organization

Protein Organization

Protein Folding

Protein Folding

Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

Protein and Protein Structures

Protein and Protein Structures

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

You might also read

Related Articles

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

Sort by

Same author

Techno-functional and sensory properties of pigeon pea-rice protein blends for beverage applications.

Journal of food science and technology·2026

Same author

Seed germination improves air classification efficiency of pea and faba bean flours.

Journal of the science of food and agriculture·2026

Same author

Oat protein extraction: The role of oat flourcomposition on extraction yield, purity, and functionality.

Food chemistry·2025

Same author

Effect of Extrusion Conditions on the Characteristics of Texturized Vegetable Protein from a Faba Bean Protein Mix and Its Application in Vegan and Hybrid Burgers.

Foods (Basel, Switzerland)·2025

Same author

Submerged fermentation of lentil protein isolate and its impact on protein functionality, nutrition, and volatile profiles.

Journal of food science·2024

Same author

Effects of extrusion screw speed, feed moisture content, and barrel temperature on the physical, techno-functional, and microstructural quality of texturized lentil protein.

Journal of food science·2024

Search research articles

Related Experiment Video

Updated: May 10, 2026

Real-Time Force Measurement Between Emulsion Droplets During Enzymatic Breakdown

Real-Time Force Measurement Between Emulsion Droplets During Enzymatic Breakdown

Published on: June 27, 2025

Food proteins: a review on their emulsifying properties using a structure-function approach.

Ricky S H Lam¹, Michael T Nickerson

¹Department of Food and Bioproduct Sciences, University of Saskatchewan, 51 Campus Drive, Saskatoon, SK, Canada S7N 5A8.

|June 25, 2013

Summary

Food proteins stabilize oil-in-water or water-in-oil emulsions due to their amphiphilic nature. Factors like protein conformation, pH, and polysaccharides influence emulsion stability for applications in food and drug delivery.

More Related Videos

In vitro Digestion of Emulsions in a Single Droplet via Multi Subphase Exchange of Simulated Gastrointestinal Fluids

In vitro Digestion of Emulsions in a Single Droplet via Multi Subphase Exchange of Simulated Gastrointestinal Fluids

Published on: November 18, 2022

Related Experiment Videos

Last Updated: May 10, 2026

Real-Time Force Measurement Between Emulsion Droplets During Enzymatic Breakdown

Real-Time Force Measurement Between Emulsion Droplets During Enzymatic Breakdown

Published on: June 27, 2025

In vitro Digestion of Emulsions in a Single Droplet via Multi Subphase Exchange of Simulated Gastrointestinal Fluids

In vitro Digestion of Emulsions in a Single Droplet via Multi Subphase Exchange of Simulated Gastrointestinal Fluids

Published on: November 18, 2022

Area of Science:

Food science and technology
Colloid and surface chemistry
Biomaterials science

Background:

Proteins possess amphiphilic properties, enabling them to adsorb at oil-water interfaces and reduce interfacial tension.
This interfacial activity allows proteins to act as emulsifiers, forming stable oil-in-water (O/W) or water-in-oil (W/O) emulsions.
These protein-stabilized emulsions have significant potential in food formulations, drug delivery, and nutrient delivery systems.

Purpose of the Study:

To review the critical factors influencing the stability of food protein-stabilized emulsions.
To explore the role of protein conformation, pH, solvent conditions, and thermal treatments on emulsion stability.
To investigate the synergistic effects of polysaccharides complexed with proteins for enhanced emulsion stabilization.

Main Methods:

Literature review focusing on scientific studies of protein behavior at oil-water interfaces.
Analysis of factors affecting protein conformation and interfacial properties.
Examination of polysaccharide-protein interactions and their impact on emulsion characteristics.

Main Results:

Protein adsorption at the interface is governed by amphiphilicity, leading to emulsion formation.
Emulsion stability is significantly influenced by protein conformation, pH, solvent composition, and thermal history.
Complexation with polysaccharides can further enhance the stability of protein-stabilized emulsions.

Conclusions:

Understanding the factors affecting protein interfacial behavior is crucial for tailoring emulsion properties.
Food proteins are versatile emulsifiers with broad applications, particularly when their stability is optimized.
Polysaccharide-protein complexes offer a promising strategy for developing robust and functional emulsions for various industries.