Embedding an enzyme in the metal-organic frameworks (MOFs) gives good protection to the fragile enzyme. However, this may also restrain the enzyme activity because of the decreased substrate accessibility. Encapsulation of lipase AK from Pseudomonas fluorescens for preparing the enzyme-MOF composite (AK@ZIF-8-PEI) was performed through a new strategy based on polyethyleneimine and enzyme induced in-situ growth of zeolitic imidazolate framework-8 (ZIF-8). Characterizations indicate that AK@ZIF-8-PEI has a honeycomb structure and the hierarchical porosity formed during the preparation, which provides adequate mass transfer channels for catalytic applications. Activity evaluation shows that specific activity of AK@ZIF-8-PEI is 8-fold than the commercial lipase powder. AK@ZIF-8-PEI is demonstrated as an efficient catalyst in kinetic resolution of α-naphthol enantiomers through enantioselective transesterification. Within 12 h, the conversion and substrate enantiomeric excess (ees) reaches 49.8 % and 96.4 %, achieving an improved resolution than previous researches.
Keywords: Enantiomeric resolution; Enzyme; Immobilizing; MOFs; PEI.
Copyright © 2023. Published by Elsevier B.V.