The fluorescence studies of coagulating protein extracted from Moringa oleifera seeds have been studied using steady-state intrinsic fluorescence.
The fluorescence spectra are dominated by tryptophan emission and the emission peak maximum ( max = 343±2 nm) indicated that the tryptophan
residue is not located in the hydrophobic core of the protein. Changes in solution pH affected the protein conformation as indicated by changes in
the tryptophan fluorescence above pH 9 whereas the ionic strength had minimal effect. The exposure and environments of the tryptophan residue
were determined using collisional quenchers.