Reversible changes of canavalin solubility controlled by divalent cation concentration in crude sword bean extract
Reversible changes of canavalin solubility controlled by divalent cation concentration in crude sword bean extract
复制标题
刀豆粗提取物中二价阳离子浓度控制刀豆球蛋白溶解度的可逆变化
DOI：
10.1080/09168451.2016.1224642
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发表时间：
2016
期刊：
影响因子：
--
通讯作者：
Y. Arii
中科院分区：
文献类型：
--
作者：
Kaho Nishizawa;Y. Arii
刀豆球蛋白是刀豆球蛋白类（7S）贮藏蛋白，存在于刀豆（Canavalia gladiata）中。我们之前的报告表明，向粗刀豆提取物中添加20 mM MgCl2会沉淀刀豆球蛋白。在这里，我们研究了在不同浓度下加入Mg 2+和Ca 2+引起的溶解度变化。刀豆球蛋白倾向于在相对低浓度的MgCl 2（< 20 mM）下不溶解，而在相对高浓度（> 20 mM）下溶解。此外，刀豆球蛋白在NaCl存在下轻微不溶。总的来说，结果表明，溶解度的变化是可逆的，并取决于二价阳离子的浓度。因此，我们提出了一个反应方案，描述了二价阳离子对刀豆球蛋白的溶解度的影响，这将有助于其生理功能的研究和刀豆球蛋白在食品加工工业中的应用。图形摘要刀豆球蛋白的溶解度变化是可逆的，并依赖于二价阳离子的浓度。
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 MgCl2 to 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. Graphical abstract The solubility changes of canavalin are reversible and depend on the concentration of divalent cations.