Tracking Protein Aggregation Behavior and Molecular Interactions Induced by Conformational Alterations in the Formation of Myofibrillar Protein-Abelmoschus Manihot Gum Mixed Gels During Heating Process

The present study aimed to systematically investigate the effects of different Abelmoschus manihot gum (AMG) concentrations (0-0.5%, w/w) on the formation of myofibrillar protein (MP) gels during heating process (30-80 degrees C) based on conformational alterations, protein aggregation behavior and molecular interactions. With the increase of temperature, the fluorescence intensity and alpha-helix content significantly decreased, revealing conformational transition of MP molecular. Dynamic rheological results indicated that MP had completely denatured and formed temporary gel at 50 degrees C, and completely formed irreversible cross-linked three-dimensional network structure at 80 degrees C. Moreover, the addition of AMG decreased the fluorescence intensity, as well as induced the transition of MP from alpha-helix to beta-sheet during the whole heating process. Furthermore, AMG addition significantly decreased the turbidity and improved solubility of MP (P < 0.05), especially for at 0.3% AMG concentration, indicating that AMG accelerated the early unfolding and aggregation of MP during heating process. This was verified by the dynamic rheological results. Additionally, hydrophobic interactions and disulfide bonds were the main molecular forces to induce the formation of MP-AMG mixed gel. Therefore, our present results provided the new insights into the formation of MP-AMG mixed thermal-induced gel, and also contributed to the practical application of AMG in meat processing.