Indexed on: 26 Jun '12Published on: 26 Jun '12Published in: Langmuir
We report the biomacromolecular self-assembly of histidine acid phosphatase (HAP), an enzyme of significant biomedical and industrial importance, in the ionic liquid (IL) 1-butyl-3-methylimidazolium tetrafluoroborate ([BMIM][BF(4)]). The spontaneous self-assembly of HAP enzyme in [BMIM][BF(4)] results in the formation of HAP nanocapsules. The HAP enzyme molecules were found to retain their enzymatic activity after the self-assembly process, which enabled us to utilize self-assembled HAP capsules as self-catalyzing templates for the synthesis of a range of hollow metal nanoparticles (Au, Ag, Pd, and Ni) without employing any additional reducing agent. The hollow metal nanospheres with HAP encapsulated within their cavity were found to retain enzymatic activity for at least up to four cycles, as demonstrated in the case of Au-coated HAP capsules as the model system.