Abstract:
The successful development of stable biosensors incorporating entrapped proteins
suffers from poor understanding of the properties of the entrapped biomolecules. This
thesis reports on the use of fluorescence spectroscopy to investigate the properties of
proteins entrapped in sol-gel processed silicate materials. Two different single tryptophan
(Trp) proteins were investigated in this thesis, the Ca2
+ binding protein cod III
parvalbumin (C3P) and the salicylate binding protein human serum albumin (HSA).
Furthermore, the reactive single cysteine (Cys) residue within C3P and HSA were labelled
with the probes iodoacetoxynitrobenzoxadiazole (C3P) and acrylodan (C3P and HSA) to
further examine the structure, stability and function of the free and entrapped proteins.
The results show that both C3P and HSA can be successfully entrapped into sol-gelderived
matrices with retention of function and conformational flexibility.
