Biomimetic mineralization of lipase@MOF biocatalyst for ease of biodiesel synthesis: Structural insights into the catalytic behavior

A hybrid lipase@ZIF-8 biocatalyst was fabricated via a facile one-pot approach and coordination-driven self -assembly strategy. Entrapment immobilization of lipase in metal-organic frameworks (MOFs) was meticulously validated. The reduced Km value and apparent activation energy confirmed that the lipase@ZIF-8 registered a superior enzyme-substrate affinity than free ones. A concomitant conformational rearrangement occurred as lipase was encapsulated into the porous zeolite-like topologies, wherein lipase architectures presented more flexibility in character. An approximate 75% biodiesel yield was achieved when the biocomposites-catalyzed transesterification was conducted at given conditions. Notably, the lipase@ZIF-8 exhibited certain substrate -selectivity by deciphering the discrepancy in fatty acid profiles of the resulting biodiesel. Besides, the lipase@ZIF-8 biocomposites showed reasonable reusability and remained around 80% of initial activity after five cycles of transesterification. Consequently, the encapsulation of lipase into MOFs is a viable and sustainable avenue to address free lipase's intrinsic limitation, and underscores the immense potential in biodiesel production.

Automated summary

By encapsulating lipase into metal-organic frameworks, the affinity between the enzyme and substrate is improved, leading to higher biodiesel yield and substrate selectivity. The biocomposites also show reasonable reusability.