摘要
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.
To investigate the hydration of proteins in magnetized water, pure water was treated with a static magnetic field （MF） over different effective treatment time （teff）. Viscosimetry and oxygen nuclear magnetic resonance （170-NMR） spectra were recorded. The hydration properties of β-lactoglobulin （β-Lg） in magnetized water were examined by differential scanning calorimetry （DSC） and NMR. By increasing teff, the internal energy of the water decreased and the concentration of ＂hydrogen-bonded＂ water increased. This result indicates that MF treatment promotes the formation of water clusters, which can be attributed to an increase in hydrogen bonding. For the β-Lg solution prepared in magnetized water, the mobility of water molecules around the β-Lg surface did not change significantly with an increase in teff but the quantity of non-freezable bound water increased. This suggests that β-Lg hydration is related to the formation of water clusters, which depends on the hydrogen-bonding structure of water and can be varied by MF treatment.
出处
《物理化学学报》
SCIE
CAS
CSCD
北大核心
2010年第2期304-310,共7页
Acta Physico-Chimica Sinica
基金
国家自然科学基金(50608046)资助项目~~
关键词
磁化
氢键
水分子缔合
蛋白质水合
Magnetization
Hydrogen bond
Water molecule cluster
Protein hydration
