KMID : 0364819880260020122
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Korean Journal of Microbiology 1988 Volume.26 No. 2 p.122 ~ p.128
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Enzymatic Properties of Cellobiohydrolase immobilized in Soil
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Chung, Jong-Kang/Á¤Á¾°¢
Yang, Young-Ki/Rhee, Young-Ha/¾ç¿µ±â/¸ÍÁø¼ö
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Abstract
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1
The enzymatic properties of soil cellobiohydrolase were examined and compared with those of cdlobiohydrolase-active extracts from soil in the forms of enzyme-hnmic complex and humicfree enzyme, and cellobiohydrolase partially purified from Aspergilius niger. The pH optima of soil cellobiohydrolase and celloblohydrolase-humic complex were greater by 1.5-3.0 pH units than those of cdlobiohydrolase in humic-free extract and from A. niger. Soil cdbbiohydrolase and cellobiohydrolase-hamic complex were remarkably resistant to thermal denaturation and proteolysis. These results confirm that cellobiohydrolase in soil is stable in conditions which rapidly inactivate microbial cellobiohydrolase and that its stability is due to the immobilization of this enzyme by association with humic substances. The Michaelis-Menten constants (Km) for soil, cdlobiohydrobwe-humic complex, humicfree extract and cellobiohydrolase from A. niger were 22.1 mg/ ml, 11.3 mg/ ml, 10.6 mg/ ml and 4.5 mg/ml of Avicel, respectively.
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