Effects of different ultrasound frequencies on the structure, rheological and functional properties of myosin: Significance of quorum sensing.

Structure and rheological properties of myosin in myofibrillar protein (MP) after single frequency pulsed ultrasound (SFPU, G1-G2) and dual frequency pulsed ultrasound (DFPU, G3) were compared for the first time. Results showed SFPU and DFPU induced "stress response" through the action of cavitation on multiple myosin. In addition, there may be a certain quorum sensing among myosin, inducing a more stable β-antiparallel structure to resist negative effects of cavitation force. Results of particle size and synchronous fluorescence indicated that structure of myosin in MPs changed through stress. The increase in pH also assisted in the ultrasound process (G5-G7). Notably, DFPU induced stronger quorum sensing and formed a more stable structure. More so, effects of (-)-epigallocatechin-3-gallate (EGCG) and baicalein (BN) on the emulsion and gel properties of DFPU treated and non-treated MPs were also investigated. Results showed that ultrasound increased the stability of emulsion. Additionally, the texture and expressible moisture content (EMOC) of the gel were also improved after treatment.