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Barley lipid-transfer protein as heavy metal scavenger

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Abstract

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.

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Acknowledgements

This study is partially supported by Ministry of Sciences, Technology and Development, project No. 1934. The authors would like to thank Milisav Ilić for help during preparation of this paper.

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Authors and Affiliations

  1. Institute of General and Physical Chemistry, PO Box 551, 11001 Belgrade, Serbia and Montenegro

    S. Gorjanović, D. Sužnjević, M. Beljanski & J. Hranisavljević

Authors
  1. S. Gorjanović
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  2. D. Sužnjević
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  3. M. Beljanski
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  4. J. Hranisavljević
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Corresponding author

Correspondence to S. Gorjanović.

Additional information

Selected article from the Regional Symposium on Chemistry and Environment, Krusevac, Serbia, June 2003, organised by Dr. Branimir Jovancicevic

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Gorjanović, S., Sužnjević, D., Beljanski, M. et al. Barley lipid-transfer protein as heavy metal scavenger. Environ Chem Lett 2, 113–116 (2004). https://doi.org/10.1007/s10311-004-0084-5

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  • DOI: https://doi.org/10.1007/s10311-004-0084-5

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