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.
A better understanding of structure-function relationships of enzymes allows revelation of key structural motifs or elements. Here, we studied the structural basis of the substrate promiscuity of EH
0
, a family IV esterase, isolated from a sample of the
Sorghum bicolor
rhizosphere microbiome exposed to technical cashew nut shell liquid.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.