Related Experiment Video
Updated: May 27, 2026
10:50
Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
Published on: March 9, 2010
Crosslinking food proteins for improved functionality
Johanna Buchert1, Dilek Ercili Cura, Hairan Ma
1VTT Technical Research Center of Finland, Espoo, FI-02044 Finland. johanna.buchert@vtt.fi
Annual Review of Food Science and Technology
|December 2, 2011
Summary
This review explores enzymatic protein crosslinking, focusing on transglutaminase (TG) and oxidative enzymes. These enzymes enhance food texture in cereal, dairy, meat, and fish products, with TG being commercially dominant.
Area of Science:
- Food Science
- Biochemistry
- Protein Chemistry
Background:
- Protein crosslinking is crucial for modifying food structure and texture.
- Enzymatic methods offer targeted approaches to protein modification.
- Transglutaminase (TG) is a key enzyme in current food applications.
Purpose of the Study:
- To review enzymatic protein crosslinking methods.
- To emphasize the impact of enzymatic crosslinking on food structure.
- To compare different crosslinking enzymes and their properties.
Main Methods:
- Literature review of protein crosslinking techniques.
- Focus on enzymatic crosslinking mechanisms.
- Analysis of enzyme applications in various food industries.
Main Results:
- Enzymatic crosslinking, particularly with transglutaminase (TG) and oxidative enzymes, significantly impacts food texture.
- TG is the most common enzyme in commercial food processing.
- Different enzymes exhibit distinct reaction mechanisms and technological properties.
Conclusions:
- Enzymatic crosslinking is a valuable tool for improving food product quality.
- Understanding enzyme mechanisms is key to optimizing their application.
- Further research into diverse oxidative enzymes could expand applications beyond TG.
Related Concept Videos
01:57Protein Complexes with Interchangeable Parts
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
01:57Protein Complexes with Interchangeable Parts
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
00:49Ligand Binding and Linkage
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
01:24Tagging and Fusion Proteins
Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
02:26Protein Networks
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
02:04Protein-protein Interfaces
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...