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Development of enzymatically-active bacterial cellulose membranes through stable immobilization of an engineered β-galactosidase

AuthorsEstevinho, Berta N.; Samaniego, Nuria; Talens Perales, David ; Fabra, María José ; López-Rubio, Amparo ; Polaina Molina, Julio ; Marín Navarro, Julia
KeywordsProtein immobilization
Carbohydrate binding module
Bacterial cellulose
Issue Date18-Apr-2018
CitationInternational Journal of Biological Macromolecules 115: 476-482 (2018)
AbstractEnzymatically-active bacterial cellulose (BC) was prepared by non-covalent immobilization of a hybrid enzyme composed by a β-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 β-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.
Publisher version (URL)https://doi.org/10.1016/j.ijbiomac.2018.04.081
Appears in Collections:(IATA) Artículos
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