College of Light Industry and Food Sciences, South China University of Technology, Guangzhou 510640, China.
School of Chemistry and Chemical Engineering, Henan University of Technology, Zhengzhou 450001, China.
Food Chem. 2017 Feb 15;217:560-567. doi: 10.1016/j.foodchem.2016.09.012. Epub 2016 Sep 6.
In this study, the natural deep eutectic solvents (NADESs) based on trehalose and choline chloride have been prepared to enhance the protein thermostability. The results of fourier transform infrared spectroscopy and (1)H nuclear magnetic resonance spectroscopy suggested that there were intensive hydrogen-bonding interactions between trehalose and choline chloride in TCCL3-DES and TCCL3-DES75. The physicochemical properties of TCCL3-DES and TCCL3-DES75 were investigated in the temperature range of 293.15-363.15K. Our results revealed that the thermostability of lysozyme, a model protein used in this study was dramatically increased in TCCL3-DES75, as evidenced by the disappearance of the denaturing peak from their Differential Scanning Calorimetry (DSC) traces. The results of circular dichroism (CD) experiments further demonstrated that the lysozyme in TCCL3-DES75 unfolded partially at 90°C and recovered to the initial structure at 20°C. The study suggests that TCCL3-DES75 might be a potential solvent for stabilizing proteins.
在这项研究中，制备了基于海藻糖和氯化胆碱的天然深共熔溶剂（NADESs），以提高蛋白质的热稳定性。傅里叶变换红外光谱和（1）H 核磁共振光谱的结果表明，在 TCCL3-DES 和 TCCL3-DES75 中，海藻糖和氯化胆碱之间存在强烈的氢键相互作用。在 293.15-363.15K 的温度范围内，研究了 TCCL3-DES 和 TCCL3-DES75 的物理化学性质。我们的结果表明，作为本研究中使用的模型蛋白的溶菌酶的热稳定性在 TCCL3-DES75 中显著提高，这可以从它们的差示扫描量热法（DSC）曲线上变性峰的消失得到证明。圆二色性（CD）实验的结果进一步表明，TCCL3-DES75 中的溶菌酶在 90°C 下部分展开，并在 20°C 下恢复到初始结构。该研究表明，TCCL3-DES75 可能是一种稳定蛋白质的潜在溶剂。
