Effect of myofibrillar protein structure changes mediated by NaCl on the binding capacity of volatile compounds in Cantonese sausage

Sodium chloride (NaCl) has an indispensable effect on Cantonese sausage flavor, while its mechanism is far from clear. This study examined how NaCl affects the flavor of Cantonese sausage by altering myofibrillar protein (MP) structure and its binding to key volatile compounds. The results showed that NaCl concentration most affected the esters in Cantonese sausage. At 3.5 %, myosin degradation shifted α-helix to β-sheets and β-turns. Ionic bonding, hydrophobic interactions and surface hydrophobicity peaked due to the solubilization of proteins as well as the exposure of hydrophobic groups. MP adsorption capacity showed that 3.5 % NaCl concentration adsorbed ethyl hexanoate, octanol, octanal, and 2-nonanone most strongly. The adsorption driving force originates from the exposure of hydrophobic sites, which reduces surface tension and subsequently promotes the adsorption of flavor compounds. This study provides theoretical and data support for optimizing processing conditions and improving the flavor of Cantonese sausages.