title: Contribution of Long Fibrils and Peptides to Surface and Foaming Behavior of Soy Protein Fibril System.
abstract: When soy glycinin (11S) is heated for a prolonged time at pH 2 (20 h at 85 °C), a mixture is formed consisting of long semiflexible 11S fibrils and small peptides. The surface and foaming properties of this mixture were investigated at different pHs, and compared to the behavior of pure fibrils and pure peptides, to determine the individual contributions of these two factions to the behavior of the mixture. The adsorption of these three systems at air-water interfaces and the resulting surface rheological properties were studied by combining drop shape analysis tensiometry, ellipsometry, and surface large amplitude oscillatory dilatational (LAOD) rheology. Lissajous plots of surface pressure versus deformation were used to analyze the surface rheological response in terms of interfacial microstructure. Our results show that the adsorption kinetics, dilatational rheological properties, and the foaming behavior of the mixture were mainly dominated by the small peptides in the fibril system. Compared to pH 2, the fibril mixture at pH 5 and 7 provides much better foam stability and appears to be a very promising protein material to make stable foams, even at low protein concentration (0.1 wt %). The presence of fibril clusters and peptide aggregates at pH 5 and 7 contributed to foam stability of the mixture. In contrast, pure fibril formed an interface with a highly pH-responsive adsorption and rheological behavior, and the foamability and foam stability of the pure fibrils were very poor.
authors.affiliation: Research and Development Center of Food Proteins, Department of Food Science and Technology, South China University of Technology , Guangzhou 510640, People's Republic of China.|Laboratory of Physics and Physical Chemistry of Foods, Wageningen University , Bornse Weilanden 9, 6708WG Wageningen, The Netherlands.
authors.forename: Zhili
authors.initials: Z
authors.lastname: Wan
authors.affiliation: Research and Development Center of Food Proteins, Department of Food Science and Technology, South China University of Technology , Guangzhou 510640, People's Republic of China.
authors.forename: Xiaoquan
authors.initials: X
authors.lastname: Yang
authors.affiliation: Laboratory of Physics and Physical Chemistry of Foods, Wageningen University , Bornse Weilanden 9, 6708WG Wageningen, The Netherlands.|Department of Materials, Polymer Physics, ETH Zürich , Leopold-Ruzicka-Weg 4, 8093 Zurich, Switzerland.
authors.forename: Leonard M C
authors.initials: LM
authors.lastname: Sagis
mesh_terms: D006863:Hydrogen-Ion Concentration; D010455:Peptides / Q000737:chemistry*; D030262:Soybean Proteins / Q000737:chemistry*; D013025:Glycine max / Q000737:chemistry*
chemical_list: D010455:Peptides; D030262:Soybean Proteins