Exploring the synergistic effects of enzyme@lactoferrin hybrid on biomimetic immobilization: Unveiling the impact on catalytic efficiency

Abstract

Metal-organic frameworks (MOFs) have gained attention as a hopeful material for enzyme immobilization due to their advantageous characteristics, for instance, high surface area and easy construction conditions. Nonetheless, the confinement effect and competing coordination often lead to partial or complete inactivation of the immobilized enzymes. In this study, we present a novel strategy, the lactoferrin-boosted one-pot embedding approach, which efficiently connects enzymes with lactoferrin (LF) hybrid Graphene Oxide (GO)//Pt Nanoparticles/MOF-74 (referred to as enzyme@LF@rGO/PtNP@MOF-74). This approach demonstrates a high embedding efficiency. By employing a hybrid of LF and GO/Pt Nanoparticles as synchronous ligands for Zn-MOF-74, we provide a suitable environment for enzyme immobilization, resulting in enhanced enzymatic activity. The lipase@LF@rGO/PtNP@MOF-74 exhibits improved stability and resistance to organic solvents and significantly enhanced in thermal stability of the lipase@LF@rGO/PtNP@MOF-74 comparing to the free enzyme. The lipase@LF@rGO/PtNP@MOF-74 displayed excellent long-term storage stability, which could protect more than 80 % of the initial activity for 8 weeks. Besides, the lipase@LF@rGO/PtNP@MOF-74 had high reusability, which showed a high degree of activity (more than 75 %) after 20 cycles. As a bio-macromolecule, lactoferrin possesses bio-affinity, creating a favorable microenvironment for enzymes and minimizing the impact of external factors on their conformation and activity during bio-macromolecule utilization.