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为探讨蛋白质在磁化水中的水合作用,首先利用粘度测定及氧17核磁共振(17O-NMR)对经静磁场(MF)处理不同有效时间(teff)后的纯水进行了分析,进一步又利用差示扫描热量计(DSC)及NMR对溶解于磁化水的β-乳球蛋白(β-Lg)的水合特性进行了分析.随teff的增加,水分子的内能不断减小,处于氢键结合状态的水分子的比例不断增加.结果表明MF处理促进了水分子缔合结构的形成,这一点可能与氢键的形成有关.随teff的增加,β-Lg表面水分子的运动性没有明显变化,但β-Lg溶液中非自由结合水的含量不断增加.说明β-Lg的水合作用与水分子的缔合分布有关,该分布依存于水分子的氢键状态并可通过磁场处理加以改变.
In order to investigate the hydration of protein in magnetized water, the pure water after different effective time (teff) by static magnetic field (MF) was first analyzed by viscosity measurement and oxygen 17 nuclear magnetic resonance (17O-NMR) The hydration characteristics of β-lactoglobulin (β-Lg) dissolved in magnetized water were analyzed by differential scanning calorimetry (DSC) and NMR.With the increase of teff, the internal energy of water molecules decreased continuously, The proportion of water molecules in the bound state increased continuously.The results showed that MF treatment promoted the formation of water molecular association structure, which may be related to the formation of hydrogen bonds.With the increase of teff, the mobility of β-Lg surface water molecules was not obvious , But the content of non-free water in β-Lg solution increased continuously, indicating that the hydration of β-Lg is related to the association of water molecules, which depends on the hydrogen bonding status of water molecules and can be treated by magnetic field change.