Barley lipid-transfer protein as heavy metal scavenger

A lipid-transfer protein was isolated from a domestic cultivar of brewer’s barley grain, Hordeum vulgare. The presence of Cu (II), Pb (II), Cd (II) and Zn (II) ions in its structure and its ability to bind Hg (II) and Ni (II) ions is known. We investigated its ability to bind other metal ions by differential pulse polarography. Here we demonstrate that the lipid-transfer protein has an affinity to bind Co (II) and Pb (II) and has no affinity towards Cd (II), Cu (II), Zn (II) and Cr (III). These results suggest a new possible role of barley lipid-transfer protein for phytoextraction.