NYOBE Emilienne Carine; MINKA Samuel René;
The knowledge on how food processing conditions and protein composition can modulate individual or food matrix protein functionality is crucial for designing new protein ingredients. In this regard, we investigated how heat treatment and protein composition influence physicochemical and functional properties of Moringa oléifera seed protein isolate. Results showed that the change of temperature induced conformational modifications affecting the hydrophobic core of proteins. Protein isolate was more soluble at room temperature whereas prolamins had high solubility at 70°C. The glutelins showed higher emulsifying properties at all temperatures. The surface hydrophobicity of albumin and prolamin improved significantly the surface hydrophobicity of the protein isolate. The solubility and emulsion capacity of glutelin improved significantly those of the protein isolate, while emulsion stability of the protein isolate improved the emulsion stability of albumin and globulin. These findings indicate that the protein composition modulates significantly their physicochemical and functional properties.
Keywords: Moringa oléifera; protein isolate; storage proteins; secondary structure; Functional properties.