Owing
to their outstanding catalytic properties, enzymes represent
powerful tools for carrying out a wide range of (bio)chemical transformations
with high proficiency. In this context, enzymes with high biocatalytic
promiscuity are somewhat neglected. Here, we demonstrate that a meticulous
modification of a synthetic shell that surrounds an immobilized enzyme
possessing broad substrate specificity allows the resulting nanobiocatalyst
to be endowed with enantioselective properties while maintaining
a high level of substrate promiscuity. Our results show that control
of the enzyme nano-environment enables tuning of both substrate specificity
and enantioselectivity. Further, we demonstrate that our strategy
of enzyme supramolecular engineering allows the enzyme to be endowed
with markedly enhanced stability in an organic solvent (i.e., acetonitrile). The versatility of the method was assessed with
two additional substrate-promiscuous and structurally different enzymes,
for which improvements in enantioselectivity and stability were
confirmed. We expect this method to promote the use of supramolecularly
engineered promiscuous enzymes in industrially relevant biocatalytic
processes.
Gold nanoparticles (AuNPs), owing to their intrinsic plasmonic properties, are widely used in applications ranging from nanotechnology and nanomedicine to catalysis and bioimaging. Capitalising on the ability of AuNPs to...
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