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In order to clarify the influence of curing agents on the flavor of duck, the effect of pH on the surface hydrophobicity, secondary structures, and adsorption capacity of myofibrillar proteins to alcohols, aldehydes, ketones, and esters was assessed using Raman spectroscopy, gas chromatography-mass spectrometer, and other methodologies. The hydrophobicity decreased as pH increased from 5.0 to 8.0; β-turn turned into α-helix and random coil as pH increased from 5.0 to 7.0, while α-helix and random coil turned into β-sheet and β-turn as pH increased from 7.0 to 8.0. With the increase of pH, the decreased adsorbing of alcohols could depend on hydrogen bonds. As pH increased from 5.0 to 8.0, the increase of aldehydes and esters was attributed to the unfolding of myofibrillar proteins and decreased hydrophobicity. The decreased adsorbing of ketones was due to the decreased hydrophobicity as pH increased from 5.0 to 8.0. The present work provided information about the correlation between structure and adsorption capacity of myofibrillar proteins to flavor compounds.