Abstract
The use of activated charcoal for enzyme recovery and purification was investigated and the optimum activated charcoal concentration and the minimum contact time needed for efficient decolorization of an alkaline protease preparation in terms of surface adsorption and retention of enzyme activity were found to be 7.5 g l−1 and 30 min, respectively. Elevated temperatures had a greater influence on the rate of decolorization which was faster when the protease was refluxed at 60 °C for 10–15 min. These data suggest that the efficient adsorption characteristics of activated charcoal can be exploited for cost-effective downstream processing of alkaline proteases and possibly other enzymes.
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Kumar, C.G.P. Activated charcoal: a versatile decolorization agent for the recovery and purification of alkaline protease. World Journal of Microbiology and Biotechnology 19, 243–246 (2003). https://doi.org/10.1023/A:1023644615956
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DOI: https://doi.org/10.1023/A:1023644615956