CAJ | 학술논문

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(~(17)O-NMR)对经静磁场(MF)处理不同有效时间(t_(eff))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t_(eff)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t_(eff)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.
위탐토단백질재자화수중적수합작용,수선이용점도측정급양17핵자공진(~(17)O-NMR)대경정자장(MF)처리불동유효시간(t_(eff))후적순수진행료분석,진일보우이용차시소묘열량계(DSC)급NMR대용해우자화수적β-유구단백(β-Lg)적수합특성진행료분석.수t_(eff)적증가,수분자적내능불단감소,처우경건결합상태적수분자적비례불단증가.결과표명MF처리촉진료수분자체합결구적형성,저일점가능여경건적형성유관.수t_(eff)적증가,β-Lg표면수분자적운동성몰유명현변화,단β-Lg용액중비자유결합수적함량불단증가.설명β-Lg적수합작용여수분자적체합분포유관,해분포의존우수분자적경건상태병가통과자장처리가이개변.
To investigate the hydration of proteins in magnetized water, pure water was treated with a static magnetic field (MF) over different effective treatment time (t_(eff)). Viscosimetry and oxygen nuclear magnetic resonance (~(17)0-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 t_(eff), 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 t_(eff) 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.