Abstract：
:Enzymatically-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.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Estevinho BN,Samaniego N,Talens-Perales D,Fabra MJ,López-Rubio A,Polaina J,Marín-Navarro Jdoi
10.1016/j.ijbiomac.2018.04.081subject
Has Abstractpub_date
2018-08-01 00:00:00pages
476-482eissn
0141-8130issn
1879-0003pii
S0141-8130(17)34806-7journal_volume
115pub_type
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