Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/220539
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Carrier-bound and carrier-free immobilization of type A feruloyl esterase from Aspergillus niger: Searching for an operationally stable heterogeneous biocatalyst for the synthesis of butyl hydroxycinnamates |
Autor: | Grajales-Hernández, Daniel A.; Velasco-Lozano, Susana CSIC ORCID; Armendáriz-Ruiz, Mariana A.; Rodríguez-González, Jorge A.; Camacho-Ruíz, Rosa María; Asaff-Torres, Ali; López-Gallego, Fernando CSIC ORCID; Mateos-Díaz, Juan Carlos | Palabras clave: | Feruloyl esterase Butyl hydroxycinnamates Cross-linked enzyme aggregates Esterification |
Fecha de publicación: | 2020 | Editor: | Elsevier | Citación: | Journal of Biotechnology 316: 6-16 (2020) | Resumen: | Feruloyl esterases synthesize butyl hydroxycinnamates, molecules possessing interesting biological properties, nonetheless, they exhibit a low stability under synthesis conditions in organic solvents, restricting its use. To enhance its operational stability in synthesis, we immobilized type A feruloyl esterase from Aspergillus niger (AnFAEA) using several carrier-bound and carrier-free strategies. The most active biocatalysts were: 1) AnFAEA immobilized on epoxy-activated carriers (protein load of 0.6 mgenzyme x mg−1carrier) that recovered 91 % of the initial hydrolytic activity, and 2) AnFAEA aggregated and cross-linked in the presence of 5 mg of BSA and 15 mM of glutaraldehyde (AnFAEA-amino-CLEAs), which exhibited 385 % of its initial hydrolytic activity; both using 4-nitrophenyl butyrate as substrate. The AnFAEA-amino-CLEAs were 12.7 times more thermostable at 60 °C than the AnFAEA immobilized on epoxy-activated carrier, thus AnFAEA-amino-CLEAs were selected for further characterization. Interestingly, during methyl sinapate hydrolysis (pH 7.2 and 30 °C), AnFAEA-amino-CLEAs KM was 15 % higher, while during butyl sinapate synthesis the KM was reduced in 63 %, both compared with the soluble enzyme. The direct esterification of butyl sinapate at solvent free conditions using sinapic acid 50 mM, reached 95 % conversion after 24 h employing AnFAEA-amino-CLEAs, which could be used for 10 cycles without significant activity losses, demonstrating their outstanding operational stability. | Versión del editor: | https://doi.org/10.1016/j.jbiotec.2020.04.004 | URI: | http://hdl.handle.net/10261/220539 | DOI: | 10.1016/j.jbiotec.2020.04.004 | ISSN: | 0168-1656 |
Aparece en las colecciones: | (ISQCH) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 59,24 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
20
checked on 12-abr-2024
WEB OF SCIENCETM
Citations
17
checked on 28-feb-2024
Page view(s)
112
checked on 22-abr-2024
Download(s)
14
checked on 22-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.