J. Biochem, 1993, Vol. 114, No. 2 230-235
© 1993 Japanese Biochemical Society
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Mode of Action of Exo- and Endo-Type Cellulases from Irpex lacteus in the Hydrolysis of Cellulose with Different Crystallinities
*Department of Chemistry and Material Engineering, Faculty of Engineering, Shinshu University Wakasato, Nagano, Nagano 380
**Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University Tokida, Ueda, Nagano 386
***Department of Fisheries, College of Agriculture and Veterinary Medicine, Nihon University Setagaya-ku, Tokyo 154
The mode of action of two highly purified cellulases of exo- and endo-types from Irpex lacteus was investigated by using pure cellulosic substrates with different crystallinities derived from cellulose I. Exo-type cellulase saccharified all celluloses more effectively than endo-type enzyme, and the saccharification activities of both cellulases similarly increased with decreasing crystallinity of cellulose. The DP-lowering activity of exo-type cellulase remained similar for celluloses with higher crystallinity, while this cellulase showed a degradation mode resembling that of the endo-type enzyme for the substrates with lower crystallinity. Compared with exo-type cellulase, endo-type cellulase remarkably decreased the DP of cellulose with higher crystallinity, while this activity was abated for cellulose with lower crystallinity. Thus, the effects of both cellulases became similar in the degradation of amorphous substrates such as H3PO4-treated cellulose. Endo-type cellulase produced several kinds of cellooligosaccharide from all kinds of cellulose used, while the product of the exo-type enzyme was only cellobiose from crystalline cellulose such as cotton and cotton linter even after a 12-h incubation period. The results indicate that each cellulase shows a typical mode of action (exo or endo) for crystalline cellulose, but that their characteristic modes of attack may change with decreasing crystallinity of cellulose.
1Present address: 10-ban-4, Kouyama-3, Nerima-ku, Tokyo 176.