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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. The solubility changes of canavalin are reversible and depend on the concentration of divalent cations. [ABSTRACT FROM AUTHOR]

Effects of zinc sulphate (ZnSO4) and zinc chloride (ZnCl2) at various levels (0–80µmol/kg) on the properties of gels from yellow stripe trevally (Selaroides leptolepis) surimi were investigated. Both kamaboko (40/90°C) and modori (60/90°C) gels added with ZnSO4 or ZnCl2 up to 60µmol/kg had the increases in breaking force and deformation (P<0.05), compared with the control. The higher breaking force and deformation were generally found in kamaboko gels added with ZnSO4, compared with ZnCl2 (P<0.05). Whiteness of both kamaboko and modori gels increased with increasing levels of zinc salts (P<0.05). Salt bridge and ionic interactions played a major role in cross-linking of proteins. Kamaboko gel had highly interconnected, denser and finer network with smaller voids when zinc salts, especially ZnSO4 at 60µmol/kg, was incorporated. Therefore, ZnSO4 at an appropriate level could improve gel strength and whiteness of surimi from dark fleshed fish. [ABSTRACT FROM AUTHOR]

Abstract: It was reported that the circulating blood cells, including neutrophils, were more likely adherent to the curved micro-vessels than the straight ones. Our previous work indicated that the vessel curvature, cell-cell interaction, and wall shear stress variation would greatly affect this preferential adhesion. It was also found that the affinity state of integrins would be influenced by different divalent cations, which provides an opportunity to explore the particular importance of integrins activation in neutrophils adhesion. In this study, we aim at numerically investigating the effects of divalent cations, i.e. Mn2+, Mg2+ plus EGTA, and Ca2+, on VLA-4/VCAM-1 adhesion under flow condition. The blood dynamics was carried out by the lattice Boltzmann method (LBM), the neutrophil dynamics was governed by the Newton''s law of translation and rotation, and a refined neutrophil adhesive dynamics model that taken into account the effect of wall shear stress gradient on receptor-ligand bonds was applied to solve the VLA-4/VCAM-1 adhesion. The simulation results indicated that the divalent cations significantly influenced neutrophils adhesion under hydrodynamic condition. It was found that the capability of stimulating affinity state of VLA-4 to VCAM-1 was larger in Mg2+ plus EGTA than in Ca2+, and largest in the presence of Mn2+. Our results would be helpful to understand the β1-integrin-mediated neutrophils adhesion in real physiological situations. [Copyright &y& Elsevier]