Covalent Immobilization of Lipase on Bacterial Cellulose Membrane and Nanocellulose

The cellulose from Komagataeibacter hansenii is synthesized as a thin film at the surface of glucose based media. Strong acid hydrolysis release sections of crystalline cellulose chains in nanometric scale that leads to persistent suspensions in water. The cellulose anhydro-glucose hydroxyls are suitable to receive functional groups as enzymes, and lipases have great economic value being a valuable model for protein immobilization. In this work both, the membrane of bacterial cellulose as well the nanocellulose produced trough acid hydrolysis, was functionalized with a lipase. The bacterial cellulose membranes were produced by Hestrin-Schramm medium, and nanocelluloses produced from the pristine material was characterized using techniques as 13C solid state NMR and transmission electron microscopy (TEM). The pristine membranes and nanocellulose were functionalized with succinic acid as linker, then lipase was conjugated using EDC (N-(3-Dimethylaminopropyl)-N′-ethylcarbodiimide hydrochloride), and NHS (N-Hydroxysuccinimide). The effectiveness of the chemical process was characterized, and the lipase activity were measured. The presence of the succinic acid and amide linkage, as well physicalchemical changes on the functionalized polysaccharide. Hence, we inferred that after immobilization the enzyme maintained its activity in both cellulose and the cellulose membrane.