title: Reversible changes of canavalin solubility controlled by divalent cation concentration in crude sword bean extract.
abstract: Canavalin is a vicilin-class (7S) storage protein found in sword bean (Canavalia gladiata). Our previous report indicated that canavalin is precipitated by the addition of 20 mM MgCl2to crude sword bean extract. Here, we examined the solubility changes induced by the addition of Mg2+and Ca2+at various concentrations. Canavalin tended to be insolubilized at relatively low concentrations of MgCl2(< 20 mM) and solubilized at relatively high concentrations (> 20 mM). In addition, canavalin was slightly insolubilized in the presence of NaCl. Overall, the results revealed that solubility changes are reversible and depend on the concentration of divalent cations. Therefore, we suggested a reaction scheme that describes the effects of divalent cations on the solubility of canavalin, which would facilitate the study of its physiological function and the application of canavalin in the food processing industry.
authors: a Department of Food Science and Nutrition , School of Human Environmental Sciences, Mukogawa Women's University , Nishinomiya , Japan.
authors: Kaho
authors: K
authors: Nishizawa
authors: a Department of Food Science and Nutrition , School of Human Environmental Sciences, Mukogawa Women's University , Nishinomiya , Japan.|b Research Institute for Nutrition Sciences , Mukogawa Women's University , Nishinomiya , Japan.
authors: Yasuhiro
authors: Y
authors: Arii
mesh_terms: D002413:Cations, Divalent / Q000494:pharmacology*; D004305:Dose-Response Relationship, Drug; D007887:Fabaceae / Q000737:chemistry*; D019649:Food Industry; D010940:Plant Proteins / Q000737:chemistry*; D012995:Solubility / Q000187:drug effects
chemical_list: D002413:Cations, Divalent; D010940:Plant Proteins
keywords: 7S globulin; canavalin; divalent cation; reversible solubility change; sword bean