Abstract

Purification of NRL protein was accompanied by extraction of waste proteins using salting out and multiple centrifugation methods. Both methods contributes to varying degree of yield and purified protein characteristics. However both methods produces protein that can bind metal efficiently. Conventionally, salting out method was used and it is uncommon to use multiple centrifuge to extract protein. The key aspects discussed here, were on how the pH condition exposed to the NRL waste leads to variation in hevea protein extracted amount and how metal binding featured in FTIR spectroscopy. The purified protein were reacted with metal solution of different strength to study the binding characteristics. Molecular weight cut-off (MWCO) size of dialyzing tube shows greater effect on the final protein extracted amount by about 50% when smaller size were used. Acidic condition favors part of proteins from waste in purification while some favors basic condition. Standard salting out method shows consistent profile in extracting metal compared to multiple centrifugation method from 30 to 80%.

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