Ontology highlight
ABSTRACT:
SUBMITTER: Puopolo R
PROVIDER: S-EPMC7862302 | biostudies-literature | 2021 Feb
REPOSITORIES: biostudies-literature
Puopolo Rosanna R Sorrentino Ilaria I Gallo Giovanni G Piscitelli Alessandra A Giardina Paola P Le Goff Alan A Fiorentino Gabriella G
Scientific reports 20210204 1
The correct immobilization and orientation of enzymes on nanosurfaces is a crucial step either for the realization of biosensors, as well as to guarantee the efficacy of the developed biomaterials. In this work we produced two versions of a chimeric protein, namely ArsC-Vmh2 and Vmh2-ArsC, which combined the self-assembling properties of Vmh2, a hydrophobin from Pleurotus ostreatus, with that of TtArsC, a thermophilic arsenate reductase from Thermus thermophilus; both chimeras were heterologousl ...[more]