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KMID : 0379120050330020075
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Korean Journal of Mycology
2005 Volume.33 No. 2 p.75 ~ p.80
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Purification and Characterization of Carboxymethyl Cellulase from Loweporus roseoalbus
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Jang Hyung-Soo
Yoo Kwan-Hee
Kim Jun-Ho
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Abstract
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A carboxymethyl cellulase (CMCase) has been purified from Loweporus roseoalbus. The molecular weight of the purified CMCase was estimated to be 28.5 kDa by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The maximum activity of the purified CMCase was observed at pH 4.0 and $30^{\circ}C$, and stable for pH 3 to 5 to maintain 60% activity. The CMCase activity was activated by SDS and inhibited by PMSF and 1,10-phenanthroline. The enzyme activity was also decreased by the addition of ethylene diamine tetraacetic acid (EDTA), suggesting that the purified CMCase is metalloenzyme.
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KEYWORD
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CMCase, Loweporus roseoalbus, SDS-PAGE
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