Bioinspired enzymatic compartments constructed by spatiotemporally confined in situ self-assembly of catalytic peptide

Abstract

Bringing enzymes and substrates together in confined compartments within porous systems can offer enhanced catalytic efficiency and increased lifetimes for the encapsulated enzymes. Here, the authors construct enzymatic compartments by spatiotemporal control of the self-assembly of catalytic peptide TPE-Q18H in hollow glucan particles, and demonstrate enhanced substrate-binding affinity and reaction kinetics as well as increased thermostability and resistance to hydrolysis.