Dr. Chunqiang Li’s research focuses on the structural, functional, and physicochemical behavior of food proteins, with particular emphasis on protein oxidation, cross-linking mechanisms, and their role in improving food quality, stability, and functionality. His work extensively explores myofibrillar protein modification, transglutaminase-catalyzed cross-linking, and protein self-assembly under various processing conditions, including oxidation, freeze–thaw cycles, pH shifting, and phosphate regulation. He has significantly advanced understanding of how microstructural transitions—such as β-sheet to α-helix transformations and protein unfolding—impact emulsification, gelation, hydration behavior, and meat product quality. His studies on Pickering emulsions, modified plant proteins, and composite particles provide innovative strategies for developing low-fat and functional meat products with enhanced texture, stability, and nutritional value. Through both experimental and molecular-level investigations, he has clarified oxidative effects on actomyosin, light meromyosin, myosin S2, and other muscle proteins, revealing how controlled oxidation can improve enzymatic cross-linking efficiency. His body of work also examines phosphates, pyrophosphates, and ultrasound-assisted treatments that modulate protein structure and improve water-holding capacity, emulsification behavior, and gel network integrity. Collectively, his research contributes important insights for designing healthier, stable, and high-quality food products through targeted protein modification and processing innovations.