Abstract
The effects of ultrasound (500 W) on the interaction of porcine myofibrillar protein (MP) with furan flavor compounds at different salt concentrations (0.6 %, 1.2 % and 2.4 %) were investigated. With the increase of salt concentration, the particle size of MP decreased, and the surface hydrophobicity and active sulfhydryl content increased due to the unfolding and depolymerization of MP. At the same time, ultrasound promoted the exposure of hydrophobic binding sites and hydrogen bonding sites of MP in different salt concentration systems, thus improving the binding ability of MP with furan compounds by 2 % to 22 %, among which MP had the strongest binding capacity of 2-pentylfuran. In conclusion, ultrasound could effectively promote the unfolding of the secondary structure of MP, which was beneficial to the combination of MP and furan flavor compounds under different salt concentrations.
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