Amaranth proteins foaming properties: Adsorption kinetics and foam formation—Part 1

• Published in: Colloids and surfaces, B, Biointerfaces Vol. 105; pp. 319 - 327
• Main Authors: Bolontrade, Agustín J., Scilingo, Adriana A., Añón, María C.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.05.2013
• Subjects: Adsorption; Air; Amaranth proteins; Amaranthus - chemistry; Calorimetry, Differential Scanning; Circular Dichroism; colloids; Electrophoresis; Foam formation; foaming; foaming capacity; foams; hydrolysis; Interface air/water; ionic strength; Peptide Fragments - chemistry; Plant Proteins - chemistry; protein aggregates; Seeds - chemistry; surfactants; Water - chemistry; Interface air/water; Amaranth proteins; Foam formation
• ISSN: 0927-7765; 1873-4367
• DOI: 10.1016/j.colsurfb.2012.12.039

[Display omitted] ► Amaranth proteins were treated at two pHs and two ionic strength, that modified their structures. ► Treatment at pH 2 induces dissociation, unfolding and a partial hydrolysis of amaranth proteins. ► Treatment at pH 2 significantly improves the rate of protein adsorption, increases the surface pressure and reduces the need for rearrangement of protein at the interface. ► The modification of structural properties and interfacial behavior has a favorable impact in the foaming properties of amaranth proteins. This work has focused on the study of the relationships between the structural changes in proteins of amaranth under different conditions of pH and ionic strength and the ability to form foam, also taking into consideration the kinetics of adsorption of proteins at the interface. Results showed that treatment at pH 2.0 significantly improves the foaming properties of amaranth proteins. The structural studies performed indicate that amaranth proteins at acidic pH are denatured, dissociated and undergo partial hydrolysis due to the existence of an endoprotease. They also present a lower content of β-sheet and random coil secondary structures. Diffusion–adsorption studies of proteins at the air:water interface allowed to determine that the acidic pH favors adsorption thereof (higher values of kdiff and ka) and reduces the need for a rearrangement (higher values of γr). The interfacial behavior of amaranth proteins is a direct consequence of the structural changes they undergo at acidic pH, changes that also were reflected on the increased foaming capacity (higher vo) thus forming more dense and homogeneous foams. The behavior of the soluble proteins as surfactants was not altered by the presence of protein aggregates and insoluble proteins.