酶
生化工程
化学
固定化酶
纳米技术
计算机科学
工程类
生物化学
材料科学
作者
Nazzoly Rueda,José Cleiton Sousa dos Santos,Claudia Ortíz,Rodrigo Torres,Oveimar Barbosa,Rafael C. Rodrigues,Ángel Berenguer‐Murcia,Roberto Fernández‐Lafuente
标识
DOI:10.1002/tcr.201600007
摘要
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.
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