RESUMO
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.
Assuntos
Enzimas/química , Líquidos Iônicos/química , Estabilidade Enzimática , Ligação de Hidrogênio , Propriedades de SuperfícieRESUMO
Thermostability of Candida rugosa lipase in organic solvents and ionic liquids was studied. During our experiments the aim was to determine if the conversion degree and enzyme half-life are changed, i.e. how to tolerate the enzyme the elevated temperature in various solvents. It was found that the enzyme kept its activity and enantioselectivity much better in ionic liquids than in the traditional organic solvents.
Assuntos
Candida/enzimologia , Lipase/metabolismo , Estabilidade Enzimática , Temperatura Alta , Indicadores e Reagentes , Cinética , Lipase/química , Solventes , Especificidade por SubstratoRESUMO
A new, large-scale process was developed for the enzymatic production of low molecular weight flavour esters in organic solvent. Solutions for the elimination of substrate and product inhibitions are presented. The excess water produced during the process was continuously removed by hetero-azeotropic distillation and esters were produced at yields of over 90%.
