Departamento de Biocatálisis, ICP-CSIC C/Marie Curie 2, Campus UAM-CSIC, Cantoblanco, 28049, Madrid, Spain.
Escuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM) Edificio Camilo Torres 210, Universidad Industrial de Santander, CEP, 680001, Bucaramanga, Colombia.
Chem Rec. 2016 Jun;16(3):1436-55. doi: 10.1002/tcr.201600007. Epub 2016 May 11.
Chemical modification of enzymes and immobilization used to be considered as separate ways to improve enzyme properties. This review shows how the coupled use of both tools may greatly improve the final biocatalyst performance. Chemical modification of a previously immobilized enzyme is far simpler and easier to control than the modification of the free enzyme. Moreover, if protein modification is performed to improve its immobilization (enriching the enzyme in reactive groups), the final features of the immobilized enzyme may be greatly improved. Chemical modification may be directed to improve enzyme stability, but also to improve selectivity, specificity, activity, and even cell penetrability. Coupling of immobilization and chemical modification with site-directed mutagenesis is a powerful instrument to obtain fully controlled modification. Some new ideas such as photoreceptive enzyme modifiers that change their physical properties under UV exposition are discussed.
酶的化学修饰和固定化曾经被认为是改善酶性质的两种独立方法。本综述展示了这两种工具的耦合使用如何极大地提高最终生物催化剂的性能。与游离酶的修饰相比，对先前固定化酶的化学修饰要简单得多，也更容易控制。此外，如果进行蛋白质修饰以改善其固定化（使酶富含反应基团），则固定化酶的最终特性可能会得到极大改善。化学修饰可以改善酶的稳定性，但也可以提高选择性、特异性、活性，甚至细胞通透性。将固定化和化学修饰与定点突变相结合是获得完全可控修饰的有力工具。还讨论了一些新的想法，例如光响应酶修饰剂，它们在紫外线照射下改变其物理性质。
