RESUMEN
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.
Asunto(s)
Cloruro de Sodio Dietético , Cloruro de Sodio , Animales , Porcinos , Unión Proteica , Interacciones Hidrofóbicas e Hidrofílicas , Proteínas Musculares/químicaRESUMEN
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.