Download Tipo de Comunicación: Comunicación Oral Simposio: INGENIERÍA

Tipo de Comunicación:
Comunicación Oral
Simposio:
INGENIERÍA BIOQUÍMICA: BIOCATÁLISIS, BIORREACTORES, DOWNSTREAM,
BIOSENSORES E INTEGRACIÓN DE PROCESOS
Título:
Could the MOFs materials be the next generation of carriers for enzymes immobilization?
Autores:
GASCON PEREZ VICTORIA, Carucci Cristina, Xiao XinXin, Magner Edmond
Centro de Trabajo:
Department of Chemical and Environmental Sciences, Materials and Surface Science
Institute, University of Limerick
Email:
[email protected]
Palabras Clave:
Alcohol dehydrogenase; biocatalysts; glucose oxidase; immobilization; MOFs
Comunicación:
Enzymes are well known as the natural biocatalysts. Tremendous efforts have been applied
in using enzymes as catalysts for a wide range of reactions. As a consequence, a wide
range of materials have been prepared and characterised as carriers to protect and to
stabilize enzymes [1]. Metal-organic frameworks (MOFs) materials have been used
extensively for the storage of gases and small molecules, a consequence of the pore sizes
of these materials, which are in the micro scale [2]. Thousands of different MOFs with
different structures and composition have been described. Properties such as high surface
area, pore volume, versatility of structure and composition make MOFs attractive as carriers
for biomolecules. However, only a small number are suitable for enzyme immobilization
purposes. The immobilization of small proteins such as cytochrome c and microperoxidase
have been reported very recently [3-4]. The focus of this work is to synthetize specific MOFs
materials with mesopores in the crystal structure [5], enabling immobilization/encapsulation
of different enzymes. Alcohol dehydrogenase, an enzyme used for the production of
enantiomerically pure alcohols, and glucose oxidase, an enzyme that is commonly used in
biosensors, have been utilised as model enzymes for the study. Both enzymes have been
successfully immobilised on a number of MOFs with retention of activity and no loss in
response over a period of three days. These results represent a general route of
immobilising enzymes for a range of applications.
[1] ACS Catal. 2011, 1, 956-968.
[2] Acta Cryst. B. 2014. 70. 3-10.
[3] J. Am. Chem. Soc. 2012, 134, 13188-13191.
[4 J. Am. Chem. Soc. 2011, 133, 10382-10385.
[5] Green Chem., 2015, 17, 1500-1509.