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 ( λ max = 343 ± 2 nm) indicated that the tryptophan residue i...

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Bibliographic Details
Published in:Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2007-11, Vol.60 (2), p.213-220
Main Authors: Kwaambwa, H.M., Maikokera, R.
Format: Article
Language:English
Subjects:
Coagulant protein
Hydrogen-Ion Concentration
Ionic strength
Moringa oleifera
Moringa oleifera - chemistry
Plant Proteins - chemistry
Plant Proteins - isolation & purification
Protein conformation
Quencher
Reproducibility of Results
Seeds - chemistry
Sensitivity and Specificity
Solutions - chemistry
Spectrometry, Fluorescence - methods
Steady-state fluorescence
Stern–Volmer equation
Surface Properties
Tryptophan
α-Helix
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Summary: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 ( λ 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.
ISSN:0927-7765
1873-4367
DOI:10.1016/j.colsurfb.2007.06.015