Substrate specificity of three kinds of cellulase preparations (A, N, and B
β) isolated from the gastric teeth of
D. auricularia was investigated on various celluloic substrates. Each preparation had endo-type action, and cellulase B
β had more random action than cellulases A and N toward CM-cellulose. Kinetic constants (Km value: mg/m
l) of the enzymes toward CM-cellulose and H
3PO
4-swollen cellulose were as follows: cellulase A, 0.3 and 1.0; cellulase N, 1.6 and 3.3; and cellulase B
β, 5.0 and 4.2; respectively.
The modes of action of cellulases A and N on cellooligosaccharides were examined. Cellulase A hydrolyzed G
6 into G
4+G
2 and G
3+G
3 in a molar ratio of 4:1, and G
5 into G
4+G
1 and G
3+G
2 in a molar ratio of 1:4. In the case of cellulase N, G
6 was cleaved into G
4+G
2 and G
3+G
3 in a molar ratio of 8:1, and G
5 was hydrolyzed into G
4+G
1 and G
3+G
2 in a molar ratio of 1:4. Synergistic action between cellulases A and B
β in the saccharification activities toward crystalline cellulose was higher than that toward amorphous cellulose.
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