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Interfacial and Emulsifying Characteristics of Acid-treated Pea Protein

Abstract : This work presents equilibrium and dynamic aspects for the adsorption at the oil-water interface of pea (Pisum sativum L.) protein isolate (PPI). Dynamic interfacial tension, γ, and surface viscoelasticity modulus, ε, were determined using pendant-drop method. Adsorption kinetics studies revealed that pea proteins adsorb faster at pH 7.0 than at acidic pH (pH 2.4). On the other hand, the measured ε is lower at pH 7.0. This is probably due to fast adsorption, leading to the formation of inhomogeneous film structures. In fact, compared with pHs above the isoelectric point (pI~4.3), acidic conditions slow down the adsorption, but the modulus is increased. Pea-protein-stabilized emulsions are more stable to creaming at acidic pH and their particle-size distributions are more homogeneous in these conditions. Effect of pH on interfacial properties and on properties of oil-in-water emulsions stabilized by PPI was interpreted in terms of pea protein solubility, globulin dissociation, and oil-droplet surface electrostatic charge. We propose that at acidic conditions, adsorbed dissociated globulins form stronger and denser viscoelastic networks when adsorbed at oil-water interface. Consequently, the pH-dependence of pea-globulin-stabilized emulsions properties could be of great interest to tune barrier properties of oil/water interfacial membranes for several applications such as encapsulation and controlled release of lipophilic bioactive components within the food, medical, and pharmaceutical industries.
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Submitted on : Tuesday, September 24, 2019 - 11:58:25 AM
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Adem Gharsallaoui, Eliane Cases, Odile Chambin, Rémi Saurel. Interfacial and Emulsifying Characteristics of Acid-treated Pea Protein. Food Biophysics, Springer Verlag (Germany), 2009, 4 (4), pp.273-280. ⟨10.1007/s11483-009-9125-8⟩. ⟨hal-02295538⟩



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