title: Surface functional properties of native, acid-treated, and reduced soy glycinin. 1. Foaming properties.
abstract: Foaming properties of native and chemically modified glycinin were evaluated. Effects of ionic strength and glycinin composition and concentration on foam formation and stabilization were studied. Glycinin was modified by means of combined treatments: cold or hot acidic treatments, with or without later disulfide bridges reduction. Modified proteins obtained from glycinin present different degrees of dissociation, deamidation, and as consequence, varied surface hydrophobicity and molecular size. Parameters of forming and stabilizing of foam were correlated with both deamidation and dissociation degrees of modified and native glycinin samples. A positive relationship was observed between surface behavior and foaming properties of different protein species. Results show that dissociation, deamidation, and reduction have produced structural changes on glycinin (increased surface hydrophobicity, increased net charge, decreased molecular size) which enhance the adsorption and anchorage of proteins at the air-water interface and, consequently, improve the foam forming and stabilizing capacities.
authors.affiliation: Centro de Investigación y Desarrollo en Criotecnología de Alimentos (CIDCA), Universidad Nacional de La Plata, Argentina. jrwagner@nahuel.biol.unlp.edu.ar
authors.forename: J R
authors.initials: JR
authors.lastname: Wagner
authors.forename: J
authors.initials: J
authors.lastname: Guéguen
mesh_terms: D005433:Flour; D005916:Globulins / Q000737:chemistry* / Q000302:isolation & purification; D006863:Hydrogen-Ion Concentration; D010084:Oxidation-Reduction; D030262:Soybean Proteins; D013025:Glycine max; D013499:Surface Properties; D014867:Water
chemical_list: D005916:Globulins; D030262:Soybean Proteins; D014867:Water; C011474:glycinin