Enhanced thermostability of enzymes accommodated in thermo-responsive nanopores

The crowded and hydrophobic microenvironment was created for immobilized enzymes via the thermally-initiated shrinkage of PNIPAM polymers anchored in the nanopores of mesoporous silica. This extraordinary microenvironment can greatly enhance both the catalytic efficiency and thermostability of lipases, which provides a new approach for fabricating robust heterogeneous biocatalysts.