Abstract:In this study, to understand the effect of heat treatment time on the absorption capacity of myofibrillar protein gel on flavor compounds, a myofibrillar protein gel-flavor compound (alcohols, aldehydes, ketones, and esters) interaction system was established, and the changes in the surface hydrophobicity, secondary structure, and absorption capacity of myofibrillar protein gels during the heat treatment at 80?C for 20 min were studied. The results showed that the changes in the absorption capacity of myofibrillar protein gels mainly occurred during the first five minutes of the heat treatment. During this period, the absorption capacities of myofibrillar protein gels on amyl alcohol, hexanol, 2-butanone, 2-heptanone, and ethyl acetate significantly increased (P < 0.05) and the surface hydrophobicity of myofibrillar protein gels markedly increased (P < 0.05). The relative content of α-helix structure decreased significantly (P < 0.05) from 37.48 to 33.44%. The relative content of β- sheet and random coil structure was significantly reduced from 20.54 and 16.12% to 15.52 and 14.78%, respectively (P < 0.05). However, the relative content of β-turn structure increased significantly (P < 0.05) from 31.15 to 36.26% and the content of random coil decreased from 16.12% to 14.78%. The changes in the absorption capacity of myofibrillar protein gels are likely due to the changes in the secondary structures and the exposure of hydrophobic groups by heat treatment.
