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KMID : 0379119860140010079
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Korean Journal of Mycology
1986 Volume.14 No. 1 p.79 ~ p.84
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Enzymatic Properties of a Cellulase from Ganoderma lucidum
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Abstract
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A cellulose-degrading enzyme from Ganoderma lucidum was partially purified by ammonium sulfate precipitation and its enzymatic properties were studied. The enzyme had an optimum pH for activity at 4.0, and its stability range was pH 4.0∼7.0. The optimum temperature was 55℃ and the enzyme retained 80% original activity after heated at 50℃ for 60 min. The activation energy of the enzyme for CMC degradation was calculated and found to be 6.2 Kcal/mole. The enzyme was activated by the addition of Co^(++), Mn^(++), but slightly inactivated by Hg^(++). Various enzyme inhibitors and chemical reagents did not affect the enzyme activity. The enzyme acted on native cellulose as well as CMC. The Michaelis constant for CMC was calculated to be 2.4 ㎎ glucose eq/㎖.
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