Innovative aspects of protein stability in ionic liquid mixtures
- PDF / 1,093,820 Bytes
- 6 Pages / 595.276 x 790.866 pts Page_size
- 70 Downloads / 184 Views
REVIEW
Innovative aspects of protein stability in ionic liquid mixtures Awanish Kumar 1 & Pannuru Venkatesu 1 Received: 1 February 2018 / Accepted: 5 March 2018 # International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature 2018
Abstract Mixtures of ionic liquids (ILs) have attracted our attention because of their extraordinary performances in extraction technologies and in absorbing large amount of CO2 gas. It has been observed that when two or more ILs are mixed in different proportions, a new solvent is obtained which is much better than that of each component of ILs from which the mixture is obtained. Within a mixture of ILs, several unidentified interactions occur among several ions which give rise to unique solvent properties to the mixture. Herein, in this review, we have highlighted the utilization of the advantageous properties of the IL mixtures in protein stability studies. This approach is exceptional and opens new directions to the use of ILs in biotechnology. Keywords Ionic liquids . IL mixtures . Cations and anions
Introduction Over the past years, ionic liquids (ILs) have been considered as novel biocompatible solvents for biotechnology. The ILs are composed of organic ions that have certain characteristics that hinder crystallization, and therefore, these salts are liquid near room temperature (Podgoršek et al. 2016). Due to this reason, they are also termed as room temperature ILs too. ILs are environmentally benign and chemically stable. Their physical properties can be easily tuned based on the experimental requirements. Interestingly, ILs have very low vapor pressure and hence are highly stable (Greaves and Drummond 2015; Smith et al. 2014). Very few of the literature reports that the ILs have very low freezing points in their purest state (Matsumoto et al. 2006; Kareem et al. 2010). Most of the ILs represented themselves as promising candidates for the proteins. An interesting aspect of the ILs is their self-buffering characteristics which have been recently explored in the literature. ILs offer high self-buffering capacity for the protein solutions in the physiological pH range (Taha et al. 2014; Gupta et al. 2016). Overall, ILs can adjust This article is part of a Special Issue on BIonic Liquids and Biomolecules^ edited by Antonio Benedetto and Hans-Joachim Galla. * Pannuru Venkatesu [email protected]; [email protected] 1
Department of Chemistry, University of Delhi, Delhi 110007, India
themselves in any required experimental conditions starting from protein stability, its extraction, crystallization, aggregation control, and enzyme catalysis under non-native environment (Wu et al. 2014; Zhao 2016). Additionally, it has been reported recently that some of the ILs can significantly reduce the viscosities of concentrated mAbs solutions (Weight et al. 2015). Hence, the use of ILs is beneficial not only for controlling protein denaturation but also for reducing the viscosities of highly concentrated protein solutions
Data Loading...
