Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 1 de 1
Filtrar
Más filtros











Base de datos
Intervalo de año de publicación
1.
Int J Biol Macromol ; 165(Pt A): 1002-1009, 2020 Dec 15.
Artículo en Inglés | MEDLINE | ID: mdl-33011269

RESUMEN

The aim of this study was to carry out the co-immobilization of α-amylase and glucoamylase in crosslinked gelatin porous supports. For this, two methods of co-immobilization were proposed based on the crosslinking with glutaraldehyde (Ggta) or CaCl2 in presence of alginate (Gcal). The supports characterization revealed a porous microstructure with good interaction between its components according to the FTIR analysis and thermal properties. Optimal pH and temperature of the Gcal co-immobilized enzymes were determined at 60 °C and pH 6.0, present an enzymatic activity of 120 µmol·mL·min-1. Moreover, both supports were reused for up to 8 hydrolysis cycles. In addition, co-immobilized enzymes were more efficient than free enzymes in starch saccharification of starch in the long term. These results reveal that the co-immobilization of amylases in gelatinous supports is a promising approach in enzymatic chain reactions.


Asunto(s)
Enzimas Inmovilizadas/química , Gelatina/química , Almidón/química , alfa-Amilasas/química , Alginatos/química , Biocatálisis , Estabilidad de Enzimas , Glucano 1,4-alfa-Glucosidasa/química , Glutaral/química , Hidrólisis/efectos de los fármacos , Porosidad , Temperatura
SELECCIÓN DE REFERENCIAS
DETALLE DE LA BÚSQUEDA