Mechanism on the Synergistic Gelation of the Myofibrillar Protein Composite Gel Enhanced by "Clean-Label" Skin Functional Protein Powders.

Abstract

The concept of healthiness and sustainability has promoted the innovation and development of "clean-label" products. Herein, this study aims to explore the influence mechanism of "clean label" skin protein powder (FPP) on the gelation properties of myofibrillar proteins (MPs). Specifically, the addition of FPP (0.2-4.0%) can improve the water holding capability and texture properties of MP composite gels. When the FPP concentration is over 1.0%, the composite gels exhibit no significant water loss during centrifugation. Dynamic rheology and sodium-dodecyl sulfate-polyacrylamide gel electrophoresis results revealed that FPP can slow the aggregation and denaturation of myosin and promote the formation of disulfide bonds between myofibril proteins, thus forming a stable network structure. Structural observation revealed that FPP can fill into the MP gel and lead to the formation of compact gel structures. Besides, with the increase of FPP concentration, the chemical forces involved in structural stabilization change significantly. Specifically, hydrophobic interaction and hydrogen bonding are the dominant forces at a lower FPP concentration (0.2 and 0.4%), while the ionic bond and disulfide bond are the dominant forces at a higher concentration. Overall, this work demonstrated that FPP can significantly improve the gel functionality of MP by altering the gel structure and strengthening the molecular forces.