TÜBİTAK Uluslararası İkili İşbirliği Projesi, 2018 - 2020
Protein-inorganic
nanoflowers, composed of protein and copper(II)phosphate (Cu3(PO4)2),
have recently grabbed people’s attention since being
first described by Richard Zare and co-workers. Many researchers
synthesized the protein-inorganic hybrid nanoflowers (hNFs) using different metal
ions (Ca2+, Co2+, Zn2+, Mn+2 etc.)
with some proteins. Compared with free enzymes,
enzyme-inorganic hybrid nano-structures (or enzyme-immobilized nano-structures)
have been showed superior catalytic activity and
stability against extraordinary pHs and temperatures as well as the presence of
additives.
However,
there is no study about how the three-dimensional structures of proteins
changes when attachment of proteins onto inorganic nanoflowers are materialized.
Besides many advantages of immobilized form of proteins, the understanding the changes
of proteins structures in the inorganic nanoflowers will open new roads to
explore many different applications and new methodologies.
Considering
their many advantages, protein- immobilized nanoflowers with the combined
functionalities of the protein and inorganic material will have important
applications such as biosensors, bioanalytical devices, biofuel cells and
industrial biocatalysis. However, it still remains a big challenge for scientists
to assemble bioinorganic hybrid structures into the complex hierarchical
architectures for their wide potential applications.