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Emulsions of peanut and soy proteins, including their major components (arachin, conarachin, glycinin and β−conglycinin), were prepared by ultrasonication (300 W, 20 min) at a constant protein concentration (4%, w/v) and oil fraction (30%, v/v). These emulsions were then induced by CaCl2, transglutaminase (TGase) and glucono-δ-lactone (GDL) to form emulsion gels. The optimum coagulant concentrations were obtained for peanut and soy protein-stabilized emulsion gels, such as CaCl2 (0.15 and 0.25 g/dL, respectively), TGase (25 U/mL) and GDL (0.3% and 0.5%, w/v, respectively). For the CaCl2-induced emulsion gels, the hardness of the β−conglycinin gel was the highest, whereas that of the conarachin gel was the lowest. However, when TGase and GDL were used as coagulants, the strength of the conarachin emulsion gel was the best. For the GDL-induced emulsion gels, microstructural analysis indicated that the conarachin gel showed more homogeneous and compact structures. The gelation kinetics showed that the storage modulus (G′) of all the GDL-induced emulsions increased sharply except for the arachin-stabilized emulsion. The interactive force nature varied between conarachin and arachin emulsion gels. This work reveals that peanut conarachin could be used as a good protein source to produce emulsion gels when suitable coagulants are selected.

Physical Properties of Peanut and Soy Protein-Based Emulsion Gels Induced by Various Coagulants