RT Journal Article
T1 Coimmobilization of lipases exhibiting three very different stability ranges. Reuse of the active enzymes and selective discarding of the inactivated ones
A1 Carballares, Diego
A1 Rocha Martin, Javier
A1 Fernandez Lafuente, Roberto
AB Lipase B from Candida antarctica (CALB) and lipases from Candida rugosa (CRL) and Rhizomucor miehei (RML) have been coimmobilized on octyl and octyl-Asp agarose beads. CALB was much more stable than CRL, that was significantly more stable than RML. This forces the user to discard immobilized CALB and CRL when only RML has been inactivated, or immobilized CALB when CRL have been inactivated. To solve this problem, a new strategy has been proposed using three different immobilization protocols. CALB was covalently immobilized on octyl-vinyl sulfone agarose and blocked with Asp. Then, CRL was immobilized via interfacial activation. After coating both immobilized enzymes with polyethylenimine, RML could be immobilized via ion exchange. That way, by incubating in ammonium sulfate solutions, inactivated RML could be released enabling the reuse of coimmobilized CRL and CALB to build a new combi-lipase. Incubating in triton and ammonium sulfate solutions, it was possible to release inactivated CRL and RML, enabling the reuse of immobilized CALB when CRL was inactivated. These cycles could be repeated for 3 full cycles, maintaining the activity of the active and immobilized enzymes.
PB Elsevier
SN 0141-8130, ESSN: 1879-0003
YR 2022
FD 2022-02-24
LK https://hdl.handle.net/20.500.14352/71832
UL https://hdl.handle.net/20.500.14352/71832
LA eng
NO Ministerio de Ciencia e Innovación (MICINN)
DS Docta Complutense
RD 6 oct 2024