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Effect of NaCl on the Interaction of Flavor Compounds with Myofibrillar Proteins

LOU Xiaowei, JIANG Yating, PAN Daodong, SUN Yangying, CAO Jinxuan*   

  1. Key Laboratory of Animal Protein Food Deep Processing Technology of Zhejiang Province, School of Marine Sciences, Ningbo University, Ningbo 315211, China
  • Online:2017-03-15 Published:2017-03-28

Abstract: The aim of the present work was to illustrate the effect and mechanism of action of NaCl concentration on the adsorption capacity of myofibrillar proteins (MPs) to flavor compounds. We selected 17 typical flavor compounds including alcohols, aldehydes, ketones and esters as flavor compounds for investigation of their adsorption properties onto MPs in the NaCl concentration range of 0.0?1.0 mol/L, and we also researched the effect of NaCl concentration on the structure of MPs. Our results showed that the hydrophobicity of MPs significantly increased in the NaCl concentration range of 0.0?0.4 mol/L but remarkably decreased as NaCl concentration rose further to 1.0 mol/L. The α-helix and β-sheet turned into β-turn at NaCl concentration of 0.0?0.4 mol/L and the secondary structure of MPs did not significantly change at higher NaCl concentration. MPs exhibited low adsorption efficiency for alcohols. The adsorptivity for alcohols, aldehydes and ketones in general decreased with increasing NaCl concentration, and the adsorptivity for esters tended to decrease at NaCl levels of 0.0?0.4 mol/L and increase with increasing NaCl level up to 1.0 mol/L. The decreased adsorption to aldehydes and ketones was attributed to the shielding of Schiff sites caused by the unfolding of secondary structure at low salt concentration, and the decrease of hydrophobicity at high salt concentration. The adsorption capacity to esters was negatively related to hydrophobicity, since the binding depended on electrostatic interaction.

Key words: myofibrillar proteins (MPs), volatile compounds, sodium chloride, protein structure, adsorption

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