Insight into the efficient loading and enhanced activity of enzymes immobilized on functionalized UiO-66.
Int J Biol Macromol
; 279(Pt 4): 135557, 2024 Nov.
Article
en En
| MEDLINE
| ID: mdl-39265898
ABSTRACT
Enzyme immobilization is an effective strategy for achieving efficient and sustainable enzyme catalysis. As a kind of promising enzyme-loading materials, the systematic research on zirconium based metal organic frameworks (Zr-MOFs) about immobilization performance at molecular level is still in its initial stage. In this work, UiO-66 was functionalized with various groups (-H, -NH2, -COOH, -OH, -2OH) for the immobilization of cytochrome c (Cyt c) and antioxidant enzyme catalase (CAT). Then the effects of surface-functionalized UiO-66 derivatives on the loading efficiency, enzyme stability and catalysis kinetics were systematically investigated. In addition, the affinity constants of Cyt c and CAT towards UiO-66-series MOFs carriers were also compared. The results have shown that hydroxyl group functionalized UiO-66 represents the highest enzyme loading capacity, enhanced activity and improved stability for Cyt c and CAT possibly due to high surface area and suitable microenvironments as well as enhanced affinity towards the enzymes provided by the introduction of a single hydroxyl group. Our research would foresee immense potential of MOFs in engineering biocatalysts.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Estabilidad de Enzimas
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Catalasa
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Citocromos c
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Enzimas Inmovilizadas
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Estructuras Metalorgánicas
Idioma:
En
Revista:
Int J Biol Macromol
Año:
2024
Tipo del documento:
Article
País de afiliación:
China