Department of Chemical and Environmental Engineering, Technical University of Cartagena (UPCT), Campus La Muralla, C/Doctor Fleming S/N, E-30202 Cartagena, Murcia, Spain.
Department of Chemical Engineering, Faculty of Chemistry, University of Murcia (UMU), P.O. Box 4021, Campus de Espinardo, E-30100 Murcia, Spain.
Molecules. 2020 Jul 15;25(14):3233. doi: 10.3390/molecules25143233.
New lipase B derivatives with higher activity than the free enzyme were obtained by occlusion in an organogel of an ionic liquid (ionogel) based on the ionic liquid [Omim][PF] and polyvinyl chloride. The inclusion of glutaraldehyde as a crosslinker improved the properties of the ionogel, allowing the enzymatic derivative to reach 5-fold higher activity than the free enzyme and also allowing it to be reused at 70 °C. The new methodology allows enzymatic derivatives to be designed by changing the ionic liquid, thus providing a suitable microenvironment for the enzyme. The ionic liquid may act on substrates to increase their local concentration, while reducing water activity in the enzyme's microenvironment. All this allows the activity and selectivity of the enzyme to be improved and greener processes to be developed. The chemical composition and morphology of the ionogel were also studied by scanning electron microscopy-energy dispersive X-ray spectroscopy, finding that porosity, which was related with the chemical composition, was a key factor for the enzyme activity.
通过将脂肪酶包埋在基于离子液体 [Omim][PF] 和聚氯乙烯的离子凝胶中,得到了比游离酶活性更高的新型脂肪酶衍生物。加入戊二醛作为交联剂可以改善离子凝胶的性能,使酶衍生物的活性比游离酶提高了 5 倍,并且可以在 70°C 下重复使用。这种新方法可以通过改变离子液体来设计酶衍生物,从而为酶提供合适的微环境。离子液体可以作用于底物来增加其局部浓度,同时降低酶微环境中的水活度。所有这些都可以提高酶的活性和选择性,并开发出更环保的工艺。通过扫描电子显微镜-能谱分析研究了离子凝胶的化学组成和形态,发现与化学组成有关的孔隙率是影响酶活性的关键因素。