Effects of pH and salt environment on the association of beta-lactoglobulin revealed by intrinsic fluorescence studies.

摘要: The effects of pH, ionic strength and heat on the structure beta-lactoglobulin (beta-lg) have been investigated by studying intrinsic tryptophan fluorescence protein. Between pH 2 9, for sodium chloride concentrations varying from 0.0 to 0.2 M, position emission maximum at 20 degrees C remained constant 328 nm, suggesting that hydrophobic environment fluorophores unchanged. intensity increased significantly 2, 7 9 reducing NaCl concentration solutions. most likely explanation this, supported recent light scattering data, is presence necessary beta-lg dimerize. At higher it was found dimerization accompanied a reduction in intensity. Thus, dissociation appears reduce self-quenching residues occurs within dimer. solutions heated below denaturation temperature reflected state association protein molecules. Above associated with aggregation, an irreversible increase observed. We also report what we believe be first front-face measurements globular gels, showing concentration.