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- W2007154881 abstract "The core fragment (designated P-42), devoid of the cellulose-binding domain (CBD) in the C-terminus and prepared from Irpex lacteus exocellulase I (Ex-1), was isolated by limited proteolysis using papain. Both the hydrolytic activity and binding ability of the isolated P-42 toward insoluble cellulose were lower than those of the native Ex-1, whereas Ex-1 and P-42 showed similar hydrolytic activities toward soluble substrates. These results indicate that the CBD of I. lacteus Ex-1 is the important domain which could enhance hydrolytic activity and binding ability of the enzyme toward insoluble cellulose. In addition, the isolated P-42 was different from the native Ex-1 in terms of enzymatic properties such as pH and temperature stabilities. These differences in stability, with regard to pH and temperature, between P-42 and the native Ex-1 are probably due to the O-linked sugar chains existing in the linker region." @default.
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- W2007154881 date "2001-01-01" @default.
- W2007154881 modified "2023-10-06" @default.
- W2007154881 title "Role of cellulose-binding domain of exocellulase I from White rot basidiomycete Irpex lacteus" @default.
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- W2007154881 doi "https://doi.org/10.1016/s1389-1723(01)80151-1" @default.
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