Role of Cellulose-Binding Domain of Exocellulase I from White Rot Basidiomycete Irpex lacteus

概要

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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.
社団法人日本生物工学会の論文
2001-04-25