Abstract
Lutein had novel spectroscopic properties in the visible region on the formation of complexes with several proteins [S. Takagi, M. Shiroishi and T. Takagi, Agric. Biol. Chem., 44, 2111 (1980)]. The effects of pH, molar ratio of lutein to protein, and the variety of protein on the phenomenon was studied. The phenomenon was insensitive to these parameters. Solubilization into micelles of deoxycholate was found to induce no optical activity in contrast to bilirubin by Perrin et al. [J. H. Perrin and M. Wilsey, Chem. Commun., 769 (1971)].
It is strongly suggested in this paper that the observed changes in spectroscopic properties including the novel one in circular dichroism come chiefly from mutual interactions between lutein molecules in the complexes. Changes in spectroscopic properties comparable to those for lutein were observed with β-cryptoxanthin but not with canthaxanthin or ethyl β-apo-8'-carotenoate, although the latter two formed complexes with ovalbumin. The presence of at least one asymmetric carbon atom in the ionone rings seems to be essential for the novel spectro-scopic changes to be observed. The possible correlation of the trans-cis conformational change in the conjugated double bond system was discussed. The optical activity was presumed to come from the intermolecular dipole-dipole coupling with the chiral spatial orientation.
