Ultrasound treatment enhanced the ability of the porcine myofibrillar protein to bind furan compounds: Investigation of underlying mechanisms.

This study was designed to explore the effects of different ultrasound power levels (0-600 W) on the ability of myofibrillar protein (MP) to bind furan compounds by analyzing the results of SDS-PAGE, particle size, Raman spectra, fluorescence intensity, solubility, turbidity, zeta potential, surface hydrophobicity, sulfhydryl content, solid-phase microextraction (SPME) and gas chromatography-mass spectrometry (GC-MS). As ultrasound power levels were increased from 0 to 500 W, the hydrophobic bonding sites, hydrogen-bonding sites, and electrostatic effects increased due to the unfolding and depolymerization of MP, thus enhancing the ability of MP to bind furan (flavor-enhancing) compounds. Consistent with these results, the positive effect of ultrasound resulted in ability of MP to bind furan compounds increased by 19.00 % to 33.32 %. However, after 600-W ultrasound treatment, the MP aggregated again and the bonding sites were re-embedded, which decreased the furan-binding ability.