Literature DB >> 27562119

Reversible changes of canavalin solubility controlled by divalent cation concentration in crude sword bean extract.

Kaho Nishizawa1, Yasuhiro Arii1,2.   

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 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.

Entities:  

Keywords:  7S globulin; canavalin; divalent cation; reversible solubility change; sword bean

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Year:  2016        PMID: 27562119     DOI: 10.1080/09168451.2016.1224642

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN: 0916-8451            Impact factor:   2.043


  2 in total

1.  Honey-mediated aggregation of soymilk proteins.

Authors:  Yasuhiro Arii; Kaho Nishizawa
Journal:  Heliyon       Date:  2020-04-12

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

Authors:  Kaho Nishizawa; Yasuhiro Arii
Journal:  Heliyon       Date:  2019-12-18
  2 in total

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