Spectroscopic Studies on Denaturants and Guluronate Lyase from a Marine Bacterium

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The denaturation and renaturation of a poly (α-L-guluronate) lyase from a marine bacterium with sodium dodecyl sulfate, guanidine hydrochloride (GHCI), and urea were investigated mainly by reflection of changes in the enzyme activity, far- and near-ultraviolet circular dichroism, and fluorescence. Amino acid analysis of the enzyme was also done to characterize the protein. The enzyme activity was lost with 6M GHCI and 3M urea in the assay mixture, but not 3% sodium dodecyl sulfate with the high activity. However, the far-ultraviolet circular dichroic spectra indicated that the secondary structure was hardly affected by treatment with 6M GHCI, but was influenced by 3M urea and 3% sodium dodecyl sulfate. By contrast, the near-ultraviolet circular dichroic spectra were attenuated by treatment with 6M GHCI and 3M urea, suggesting changes in the environments of tryptophan residues. Removal of the denaturants by dialysis almost restored all of the original protein conformation. The enzyme was more susceptible to denaturation by urea than by GHCI.
社団法人日本農芸化学会の論文
1995-05-23