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

Abstract

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.