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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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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.
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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...
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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Protein Glycosylation01:25

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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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Designing Silk-silk Protein Alloy Materials for Biomedical Applications
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Crosslinking Soy Protein: Mechanisms, Functional Modification, Applications in Food, and Future Directions.

Tolulope Joshua Ashaolu1,2

  • 1Institute for Global Health Innovations, Duy Tan University, Da Nang, Vietnam.

Journal of Texture Studies
|February 15, 2026
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Summary

Crosslinking soy protein (SP) improves its solubility, stability, and bioavailability. This review explores methods to enhance SP for advanced food and industrial applications, overcoming current limitations.

Keywords:
crosslinkingenzymatic modificationfunctional foodsgenipinsoy proteintransglutaminase

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Area of Science:

  • Food Science and Technology
  • Biopolymer Chemistry
  • Sustainable Materials

Background:

  • Soy protein (SP) is a nutritious, sustainable biopolymer with limitations in solubility, stability, and bioavailability.
  • These limitations hinder its widespread application in food and industrial products.
  • Crosslinking is a key strategy to modify SP's structure and enhance its functionality.

Purpose of the Study:

  • To review various crosslinking methods for soy protein.
  • To analyze the impact of crosslinking on SP's functional properties.
  • To explore advanced applications of crosslinked soy protein.

Main Methods:

  • Enzymatic crosslinking (transglutaminase, laccases).
  • Chemical crosslinking (genipin, tannins).
  • Physical crosslinking (high-pressure, thermal treatments).

Main Results:

  • Crosslinking significantly enhances SP's emulsion stability, gel strength, and water-holding capacity.
  • Modified SP exhibits improved functional properties for diverse applications.
  • Advanced applications include meat analogs, functional emulsions, packaging films, and bio-adhesives.

Conclusions:

  • Crosslinking effectively overcomes the limitations of native soy protein.
  • Further research is needed to address scalability, cost, and regulatory challenges.
  • Future directions include hybrid techniques, AI optimization, and smart materials for enhanced SP utilization.