Abstract
A cellulase from the extreme obligate halophilic fungus, Aspergillus flavus, isolated from a man-made solar saltern in Phetchaburi, Thailand, was purified by ammonium sulfate precipitation and using Sephadex G-100 gel filtration column chromatography. The cellulase was found to be approximately 55kDa by SDS-PAGE. Using CMC as a substrate, the specific activity of the cellulase was 62.9units (U)mg-1 with Vmax and Km values of 37.87molmin-1mg-1 and 3.02mgmL-1, respectively. Characterization of the enzyme revealed it to be an extremozyme, having an optimum activity at pH 10, 60°C, and 200gL-1 of NaCl. The enzyme activity was not significantly altered by the addition of divalent metal cations at 2mM and neither did ß-mercaptoethanol, while EDTA was found strongly inhibiting the cellulase. Compared with commercial cellulase, the purified cellulase from A. flavus was more active in the extremity of conditions, especially at pH 10, 60°C, and 150gL-1 NaCl, whereas the commercial cellulase had a very low activity.
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