Abstract: Dense phase carbon dioxide (DPCD) is a promising non-thermal food processing technology, which can induce protein denaturation and self-assembly leading to gel formation. In order to clarify the mechanism of gel formation of myosin induced by DPCD, we explored the effects of DPCD treatment at different pressures and temperatures on intermolecular force of myosin from Litopenaeus vannamei. The results showed that compared with the untreated samples, DPCD treatment decreased the contents of hydrogen bonds and ionic bonds in myosin (P < 0.05), and increased the contents of hydrophobic interaction, disulfide bonds and non-disulfide covalent bonds (P < 0.05). In the case of DPCD treatment at the same temperature, pressure (5–25 MPa) had no significant effect on intermolecular force of myosin (P > 0.05). In the case of DPCD treatment at the same pressure, with the increase in temperature (40–60 ℃), hydrogen bonds and disulfide bonds did not change significantly (P > 0.05), non-disulfide covalent bonds increased (P < 0.05), hydrophobic interaction decreased (P < 0.05), and ionic bonds initially decreased followed by an increase (P < 0.05). Therefore, hydrophobic interaction, disulfide bonds and non-disulfide covalent bonds but not hydrogen bonds and ionic bonds are the major intermolecular forces in myosin gelation induced by DPCD. These results will provide useful data for clarifying the mechanism of myosin gelation induced by DPCD.

Key words: dense phase carbon dioxide, intermolecular force, myosin, Litopenaeus vannamei