Enzyme-Decorated Covalent Organic Frameworks as Nanoporous Platforms for Heterogeneous Biocatalysis.
Chemistry
; 25(69): 15863-15870, 2019 Dec 10.
Article
en En
| MEDLINE
| ID: mdl-31596001
ABSTRACT
Sustainability in chemistry heavily relies on heterogeneous catalysis. Enzymes, the main catalyst for biochemical reactions in nature, are an elegant choice to catalyze reactions due to their high activity and selectivity, although they usually suffer from lack of robustness. To overcome this drawback, enzyme-decorated nanoporous heterogeneous catalysts were developed. Three different approaches for Candida antarctica lipaseâ
B (CAL-B) immobilization on a covalent organic framework (PPF-2) were employed physical adsorption on the surface, covalent attachment of the enzyme in functional groups on the surface and covalent attachment into a linker added post-synthesis. The influence of the immobilization strategy on the enzyme uptake, specific activity, thermal stability, and the possibility of its use through multiple cycles was explored. High specific activities were observed for PPF-2-supported CAL-B in the esterification of oleic acid with ethanol, ranging from 58 to 283â
U mg-1 , which was 2.6 to 12.7â
times greater than the observed for the commercial Novozyme 435.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas Fúngicas
/
Enzimas Inmovilizadas
/
Estructuras Metalorgánicas
/
Lipasa
Idioma:
En
Revista:
Chemistry
Asunto de la revista:
QUIMICA
Año:
2019
Tipo del documento:
Article
País de afiliación:
Brasil