Fehér E, Major B, Bélafi-Bakó K, Gubicza L
Research Institute of Chemical and Process Engineering, University of Pannonia, Egyetem u. 10, 8200 Veszprém, Hungary.
Biochem Soc Trans. 2007 Dec;35(Pt 6):1624-7. doi: 10.1042/BST0351624.
The ability of ILs (ionic liquids) to provide an environment of increased stability and, in this way, improve the recyclability of enzymes has been studied. The description of this phenomenon is not easy; there are several approaches for explanation. In this mini-review, the results from different research groups are summarized, with the aim of explaining the strong stability effect of ILs on several enzymes. Spectroscopic methods (e.g. fluorescence and CD, IR spectroscopy, mass spectroscopy and NMR) and investigations of polarity and kosmotropicity of ions are promising methods. Since higher stability means that we may be able to reuse enzymes more times, the recyclability of enzymes was also in the focus. From this point of view, the advantages and disadvantages of applying monophasic or biphasic systems are discussed too, presenting the coupled techniques as well.
离子液体(ILs)提供增强稳定性环境并以此提高酶的可回收性的能力已得到研究。对这一现象的描述并不容易;有几种解释方法。在本综述中,总结了不同研究小组的结果,旨在解释离子液体对几种酶的强稳定作用。光谱方法(如荧光和圆二色光谱、红外光谱、质谱和核磁共振)以及对离子极性和向同性的研究是很有前景的方法。由于更高的稳定性意味着我们或许能够更多次地重复使用酶,酶的可回收性也成为了焦点。从这一角度出发,还讨论了应用单相或双相系统的优缺点,并介绍了耦合技术。