title: Comparison of physicochemical properties of 7S and 11S globulins from pea, fava bean, cowpea, and French bean with those of soybean--French bean 7S globulin exhibits excellent properties.
abstract: Legume seeds contain 7S and/or 11S globulins as major storage proteins. The amino acid sequences of them from many legumes are similar to each other in the species but different from each other, meaning that some of these proteins from some crops exhibit excellent functional properties. To demonstrate this, we compared protein chemical and functional properties (thermal stability, surface hydrophobicity, solubility as a function of pH, and emulsifying properties) of these proteins from pea, fava bean, cowpea, and French bean with those of soybean as a control at the same conditions. The comparison clearly indicated that the 7S globulin of French bean exhibited excellent solubility (100%) at pH 4.2-7.0 even at a low ionic strength condition (mu = 0.08) and excellent emulsion stability (a little phase separation after 3 days) at pH 7.6 and mu = 0.08, although the emulsions from most of the other proteins separated in 1 h. These results indicate that our assumption is correct.
authors.affiliation: Laboratory of Food Quality Design and Development, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011, Japan.
authors.forename: Aiko
authors.initials: A
authors.lastname: Kimura
authors.forename: Takako
authors.initials: T
authors.lastname: Fukuda
authors.forename: Meili
authors.initials: M
authors.lastname: Zhang
authors.forename: Shiori
authors.initials: S
authors.lastname: Motoyama
authors.forename: Nobuyuki
authors.initials: N
authors.lastname: Maruyama
authors.forename: Shigeru
authors.initials: S
authors.lastname: Utsumi
mesh_terms: D002500:Centrifugation, Isopycnic; D007887:Fabaceae / Q000737:chemistry*; D005916:Globulins / Q000737:chemistry* / Q000302:isolation & purification; D006358:Hot Temperature; D057927:Hydrophobic and Hydrophilic Interactions; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D055550:Protein Stability
chemical_list: D005916:Globulins; D010940:Plant Proteins