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Int J Biol Macromol ; 115: 476-482, 2018 Aug.
Artículo en Inglés | MEDLINE | ID: mdl-29678790

RESUMEN

Enzymatically-active bacterial cellulose (BC) was prepared by non-covalent immobilization of a hybrid enzyme composed by a ß-galactosidase from Thermotoga maritima (TmLac) and a carbohydrate binding module (CBM2) from Pyrococcus furiosus. TmLac-CBM2 protein was bound to BC, with higher affinity at pH 6.5 than at pH 8.5 and with high specificity compared to the non-engineered enzyme. Both hydrated (HBC) and freeze-dried (DBC) bacterial cellulose showed equivalent enzyme binding efficiencies. Initial reaction rate of HBC-bound enzyme was higher than DBC-bound and both of them were lower than the free enzyme. However, enzyme performance was similar in all three cases for the hydrolysis of 5% lactose to a high extent. Reuse of the immobilized enzyme was limited by the stability of the ß-galactosidase module, whereas the CBM2 module provided stable attachment of the hybrid enzyme to the BC support, after long incubation periods (3 h) at 75 °C.


Asunto(s)
Celulosa/química , Gluconacetobacter xylinus/química , Membranas Artificiales , Ingeniería de Proteínas , Thermotoga maritima/enzimología , beta-Galactosidasa/química , beta-Galactosidasa/metabolismo , Estabilidad de Enzimas , Enzimas Inmovilizadas/química , Enzimas Inmovilizadas/genética , Enzimas Inmovilizadas/metabolismo , Hidrólisis , Lactasa/metabolismo , beta-Galactosidasa/genética
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