Improved emulsifying properties of water-soluble myofibrillar proteins at acidic pH conditions: Emphasizing pH-regulated electrostatic interactions with chitosan

Water-soluble muscle protein with enhanced functionalities has attracted great interest for low-salt food design. Electrostatic interactions of chitosan (CS) with myofibrillar proteins (MP) in water-aqueous solution at acidic pHs (4.0–6.5) were investigated, and how pH regulated complex formation, microstructures, conformation changes, and emulsifying capacity was systematically explored. At pH 4.0–4.5, MP and CS were positively charged and displayed a co-soluble system, exhibiting small particles and high solubility. When the pH increased to near the isoelectric point (pI) of MP (pH 5.0–6.0), electrostatic interactions largely inhibited the aggregation of MP by forming smaller particle complexes. The flexible structures and improved amphiphilic properties promoted protein absorption at the oil-water interface, further improving the emulsion stability. When the pH increased to 6.5, large aggregates were formed causing poor functionalities. This study could provide great insights to further exploit meat-protein-based low-salt functional foods in novel food design.