posted on 2024-02-18, 12:14authored byIsil Akpinar, Xiaoliang Wang, Kira Fahy, Fanrui Sha, Shuliang Yang, Tae-woo Kwon, Partha Jyoti Das, Timur Islamoglu, Omar K. Farha, J. Fraser Stoddart
Enzymes
are natural catalysts for a wide range of metabolic chemical
transformations, including selective hydrolysis, oxidation, and phosphorylation.
Herein, we demonstrate a strategy for the encapsulation of enzymes
within a highly stable zirconium-based metal-organic framework. UiO-66-F4 was synthesized under mild conditions using an enzyme-compatible
amino acid modulator, serine, at a modest temperature in an aqueous
solution. Enzyme@UiO-66-F4 biocomposites were then formed
by an in situ encapsulation route in which UiO-66-F4 grows around the enzymes and, consequently, provides protection
for the enzymes. A range of enzymes, namely, lysozyme, horseradish
peroxidase, and amano lipase, were successfully encapsulated within
UiO-66-F4. We further demonstrate that the resulting biocomposites
are stable under conditions that could denature many enzymes. Horseradish
peroxidase encapsulated within UiO-66-F4 maintained its
biological activity even after being treated with the proteolytic
enzyme pepsin and heated at 60 °C. This strategy expands the
toolbox of potential metal-organic frameworks with different topologies
or functionalities that can be used as enzyme encapsulation hosts.
We also demonstrate that this versatile process of in situ encapsulation of enzymes under mild conditions (i.e., submerged
in water and at a modest temperature) can be generalized to encapsulate
enzymes of various sizes within UiO-66-F4 while protecting
them from harsh conditions (i.e., high temperatures, contact with
denaturants or organic solvents).