Exploring succinylation in proteins: A comprehensive review from functional improvements to application potential.

As global populations grow and economic levels rise, the demand for high-quality proteins and their products is increasing. However, natural proteins generally suffer from poor solubility, low thermal stability, limited emulsifying and foaming properties, and undesirable flavors, severely restricting their industrial application. Succinylation, a chemical modification method involving the introduction of succinyl groups onto specific amino acid residues (particularly lysine), has shown considerable promise in improving protein functionalities. This review systematically summarizes recent research advances in protein succinylation, thoroughly discussing key factors affecting reaction efficiency, such as pH, temperature, reaction time, reagent concentration, amino acid composition, and protein structure. Moreover, the review analyzes the influence of succinylation on protein secondary and tertiary structures and resultant changes in solubility, emulsification, foaming, and gelation properties. While succinylation generally enhances protein functionality, it may negatively impact specific functional properties in certain proteins. Reasons underlying these functional differences are also discussed. Furthermore, the review explores potential applications of succinylated proteins in food preservation, bioactive compound encapsulation, and drug delivery systems. Finally, key challenges, including precise control over modification degree, insufficient long-term chemical stability, and limited toxicological assessments, are identified. Future research should focus on protein structure-function relationships, optimization of modification conditions, and comprehensive safety evaluations to facilitate broader industrial acceptance and regulatory compliance of succinylation technology.