Selenium modification of β-lactoglobulin (β-Lg) and its biological activity.

β-Lg is a major whey protein in cow's milk. This study was aimed to find a new kind of organic selenium compound synthesized with β-Lg and selenium dioxide as raw materials under the conditions of vacuum and low temperature. Fourier transformed infrared spectroscopy revealed that seleno-β-lactoglobulin (Se-β-Lg) displayed a strong band at 878cm(-1), belonging to SeO. Circular dichroism spectra results indicated that the conformation of Se-β-Lg was transformed and α-helical, and unordered structures were increased by 9% and 11.2%, respectively, while β-sheet and β-turn were reduced by 14.2% and 6%, respectively. Electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry results showed that there were two protein bands (1-Seβ-Lg and 2-Seβ-Lg) in Se-β-Lg, only one β-Lg connected with selenate in 1-Seβ-Lg, but two β-Lgs, connected to each other, and with selenate, in 2-Seβ-Lg. Morphological observation and hematoxylin and eosin staining indicated that Se-β-lg could induce K562 cell apoptosis. These results indicated that Se-β-Lg could be synthesized by selenium conjugating β-Lg and it had antitumor activity.