Metal Selectivity of Hevea Protein Isolated from Natural Rubber Latex Skim Serum

  • Abstract
  • Keywords
  • References
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  • Abstract

    Hevea protein isolated from skim serum, a by-product of centrifugation process, contains useful proteins in extracting metal. It can be used directly from the source or purified before reacting with metal solutions. Those proteins bind with metal at varying degrees. Upon exposure from as low as 2 ppm concentration to up to 20 ppm metal solution concentration, different binding characteristics were seen. The reasons of such inconsistency in the characteristics might be due to the existence of some of the metal itself in the NRL serum. Mg++ and Zn++ are common metal found in NRL products and those metals would show the slightest in binding with hevea protein. Other metals which were covered in this scope of study shows a good binding characteristics disregard of the group of metals belongs. Selectivity was measured from the final concentration of metal in percentage. In most cases, lead, copper and cadmium show good interaction with hevea proteins.


  • Keywords

    Natural rubber latex, Hevea protein, metal selectivity

  • References

      [1] Dudev, T. and C. Lim, Principles governing Mg, Ca, and Zn binding and selectivity in proteins. Chemical Reviews, 2003. 103(3): p. 773-788.

      [2] Mejáre, M. and L. Bülow, Metal-binding proteins and peptides in bioremediation and phytoremediation of heavy metals. TRENDS in Biotechnology, 2001. 19(2): p. 67-73.

      [3] Scott, D.J., et al., Activation and inhibition of rubber transferases by metal cofactors and pyrophosphate substrates. Phytochemistry, 2003. 64(1): p. 123-134.

      [4] Ovečka, M. and T. Takáč, Managing heavy metal toxicity stress in plants: biological and biotechnological tools. Biotechnology advances, 2014. 32(1): p. 73-86.

      [5] Shriver, D., P. Atkins, and C. Langford, Inorganic5Chemistry, 1994. Oxford University Press, Oxford.

      [6] Arnold, F.H., Metal-affinity separations: a new dimension in protein processing. Nature biotechnology, 1991. 9(2): p. 151-156.

      [7] Guo, M., et al., Binding between lead ions and the high-abundance serum proteins. Chemosphere, 2014. 112: p. 472-480.

      [8] Ueda, E., P. Gout, and L. Morganti, Current and prospective applications of metal ion–protein binding. Journal of Chromatography A, 2003. 988(1): p. 1-23.

      [9] Exley, C. and M.J. Mold, The binding, transport and fate of aluminium in biological cells. Journal of Trace Elements in Medicine and Biology, 2015. 30: p. 90-95.

      [10] Liu, T., et al., Transcriptional profiling of Arabidopsis seedlings in response to heavy metal lead (Pb). Environmental and Experimental Botany, 2009. 67(2): p. 377-386.

      [11] Campbell, M., K. & Farrell, S. Biochemistry, 6th edition. Thomson Brooks, 2009.

      [12] Kinoshita, H., et al., Biosorption of heavy metals by lactic acid bacteria and identification of mercury binding protein. Research in microbiology, 2013. 164(7): p. 701-709.

      [13] Binet, M.R., et al., Detection and characterization of zinc-and cadmium-binding proteins in Escherichia coli by gel electrophoresis and laser ablation-inductively coupled plasma-mass spectrometry. Analytical biochemistry, 2003. 318(1): p. 30-38.




Article ID: 27710
DOI: 10.14419/ijet.v7i4.14.27710

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