Keywords

Abstract

Abstract The effects of protein concentration, oil content, pH and ionic strength on the emulsification activity and emulsification stability of chickpea protein isolate were studied. At the isoelectric point of the protein, pH 5.0, the emulsification activity is the smallest and the emulsification stability is the highest; ionic strength When the ionic strength is 0.2, the emulsification activity is the lowest and the emulsification stability is the highest. In order to explain this phenomenon, the pH and ion values were studied. The effect of strength on the secondary structure and surface hydrophobicity of proteins. The results show that the secondary structure and surface hydrophobicity of proteins change with changes in the pH and ionic strength of the solution. When the isoelectric point or ionic strength of the protein is low ( For example, when 0.1), the secondary structure of the protein mainly exists in the form of ¦Á-helix, and when the ionic strength is 0.1, the surface hydrophobicity of the protein is the lowest

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