| Literature DB >> 27664672 |
Ruipu Xin1, Suijian Qi1, Chaoxi Zeng1, Faez Iqbal Khan2, Bo Yang3, Yonghua Wang4.
Abstract
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.Entities:
Keywords: Choline chloride; Choline chloride (PubChem CID: 6209); Deep eutectic solvents; Lysozyme; Physicochemical properties; Thermostability; Trehalose; Trehalose (PubChem CID: 7427)
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Year: 2016 PMID： 27664672 DOI： 10.1016/j.foodchem.2016.09.012
Source DB: PubMed Journal: Food Chem ISSN： 0308-8146 Impact factor: 7.514