Levansucrase is a secretary enzyme of Acetobacter nitrogenifigens strain RG1. The enzyme shows enhanced activity in the presence of Hg in spite of being inhibited by other heavy metal ion Cd. In this study the structural characterization of levansucrase in native state as well as in the presence of Hg and Cd by CD spectroscopy is done. The secondary structures of the native enzyme and the enzyme treated with Hg and Cd on comparison by their CD spectra revealed that their spectra showed no significant difference indicating that both Hg as well as Cd had no effect on the overall secondary structure of the protein. The respective CD spectra on analysis revealed that they have almost identical percentage of secondary structural elements. The interaction of levansucrase with Hg as well as Cd was studied further by tryptophan fluorescence spectroscopy which on analysis revealed static quenching indicating protein-heavy metal complex formation. A blue shift in the tryptophan fluorescence spectra of Hg treated protein indicated that the tryptophan residues have moved to a more hydrophobic environment in the protein away from aqueous phase. The mechanism of interaction of enzyme with mercury and cadmium was determined from their tryptophan fluorescence spectra.
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