Structural transitions of sword bean canavalin in response to different salt concentrations

Canavalin is the major storage protein in sword beans (Canavalia gladiata) and belongs to the 7S seed globulin class. Canavalin solubility can be reversibly altered via the addition of MgCl₂ and CaCl₂ at different concentrations; specifically, it is insoluble at lower concentrations and soluble at higher concentrations. However, the addition of NaCl does not induce the insolubilization of canavalin. In this study, it was determined that the addition of NaCl causes the nearly complete solubilization of MgCl₂-precipitated canavalin in the presence of high concentrations. Moreover, using gel filtration we examined the quaternary structures of soluble canavalin in the bean extract and in the presence of high-concentration salts. Results indicated that canavalin was present in the monomer form within crude extracts with distilled water. Alternatively, we identified trimeric soluble canavalin in the presence of high concentrations of NaCl or MgCl₂. Our study revealed that the quaternary structures of sword bean soluble proteins differ in crude extract compared to those in high-concentration salt solutions. The three-dimensional structure of β-conglycinin, which is a typical 7S-seed globulin in soybean, has a trimer form in the presence of high concentrations of NaCl. However, it remains unclear whether β-conglycinin is present as trimers in soybean seed. Our findings serve as an important reference to analyze 7S globulin characteristics.