Complexation Strategies for Enhancing Water-Soluble Protein Stability and Functionality: A Comprehensive Review

Area of Science:

• Food Science
• Protein Chemistry
• Material Science

Background:

• Water-soluble proteins are valuable food ingredients but often lack sufficient stability and functionality.
• Current applications are limited by these inherent shortcomings.
• Complexation with ligands presents a viable strategy to improve protein properties.

Purpose of the Study:

• To review interaction mechanisms between water-soluble proteins and ligands.
• To summarize the enhancement of protein stability and functionalities through complexation.
• To discuss factors influencing these interactions and their outcomes, and to explore applications of protein-ligand complexes.

Main Methods:

• Literature review focusing on protein-ligand interactions.
• Analysis of studies detailing stability and functionality enhancements.
• Synthesis of information on influencing factors (protein/ligand nature, conditions).
• Compilation of current and potential applications of protein-based complexes.

Main Results:

• Detailed mechanisms of protein-ligand interactions have been elucidated.
• Significant improvements in protein stability (e.g., thermal, pH) and functionalities (e.g., emulsification, gelling) are achievable.
• Protein and ligand characteristics, alongside complexation conditions, critically impact the resulting complex properties.
• Diverse applications in food systems, including improved texture, shelf-life, and nutritional delivery, are demonstrated.

Conclusions:

• Complexation is a powerful tool for enhancing water-soluble protein performance.
• Understanding interaction parameters allows for tailored protein-based ingredient design.
• Further research into novel protein-ligand complexes promises expanded food industry applications.