A fluorescence spectroscopic study of a coagulating protein extracted from Moringa oleifera seeds.
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 (lambda(max)=343+ or -2nm) 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.
Kwaambwa
H M
HM
University of Botswana, Department of Chemistry, Private Bag UB 00704, Gaborone, Botswana. kwaambwa@mopipi.ub.bw
Maikokera
R
R
D006863:Hydrogen-Ion Concentration; D029588:Moringa oleifera / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D015203:Reproducibility of Results; D012639:Seeds / Q000737:chemistry*; D012680:Sensitivity and Specificity; D012996:Solutions / Q000737:chemistry; D013050:Spectrometry, Fluorescence / Q000379:methods; D013499:Surface Properties
D010940:Plant Proteins; D012996:Solutions