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.
Highlights
Purified protein from skim serum of NR latex concentrate protein contains hev proteins with various biological roles
A number of functional groups participate in metal binding in metalloproteins; the side chains of Glu, Tyr, Cys, His Arg, Lys, Asp and Met and free cysteines can potentially bind chelated metals, in practice they are rarely available in the appropriate reduced state [7].In new dimension of protein separations, the apparent affinity of a protein for a metal chelate depends strongly on the metal ion involved in coordination
multiple centrifuges (MC) purified protein is a physical method which only use centrifugal force which largely depends on speed, angle and density of proteins to the surrounding water layer that holds the protein
Summary
Purified protein from skim serum of NR latex concentrate protein contains hev proteins with various biological roles. Organism responds to heavy metals stress using different defense system, such as exclusion, compartmentalization, making complexes and the synthesis of binding proteins such as metallothioneins (MTs) or phytochelatins (PCs) [3]. The stability constant for complexation with imidazole follows the order Cu 2+ > Zn2+ and depends on the quantity of protein that can be loaded onto a given metal-chelate support [7]. Immobilized metal ion chromatography (IMAC) was used to purify protein by using metal binding concept, Ueda et al, (2003). Binding of proteins (or peptides) to metal ions is based on the interaction between an electron donating group present on a protein surface and a metal ion presenting one or more accessible coordination sites. The focused were to evaluate binding capability of different metals towards NRL waste proteins extractions. The finding was used in evaluating metal selectivity based on percentage of metal removed
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