Biomimic nanozymes coassembled by
peptides or proteins and small
active molecules provide an effective strategy to design attractive
nanozymes. Although some promising nanozymes have been reported, rational
regulation for higher catalytic activity of biomimic nanozymes remains
challenging. Hence, we proposed a novel biomimic nanozyme by encapsulating
the coassembly of hemin/bovine serum albumin (BSA) in zeolite imidazolate
frameworks (ZIF-8) to achieve controllable tailoring of peroxidase-like
activity via the confinement effect. The assembly of Hemin@BSA was
inspired by the structure of horseradish peroxidase (HRP), in which
hemin served as the active cofactor surrounded by BSA as a blocking
pocket to construct a favorable hydrophobic space for substrate enrichment.
Benefiting from the confinement effect, ZIF-8 with a porous intracavity
was identified as the ideal outer layer for Hemin@BSA to accelerate
substrate transport and achieve internal circulation of peroxidase-like
catalysis, significantly enhancing its peroxidase-like activity. Especially,
the precise encapsulation of Hemin@BSA in ZIF-8 could also prevent
it from decomposition in harsh environments by rapid crystallization
around Hemin@BSA to form a protective shell. Based on the improved
peroxidase-like activity of Hemin@BSA@ZIF-8, several applications
were successfully performed for the sensitive detection of small molecules
including H2O2, glucose, and bisphenol A (BPA).
Satisfactory results highlight that using a ZIF-8 outer layer to encapsulate
Hemin@BSA offers a very effective and successful strategy to improve
the peroxidase-like activity and the stability of biomimic nanozymes,
broadening the potential application of biocatalytic metal–organic
frameworks (MOFs).