title: Role of cellulose-binding domain of exocellulase I from white rot basidiomycete Irpex lacteus.
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.
authors.affiliation: Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University, 3-15-1 Tokida, Ueda 386-8567, Japan.
authors.forename: N
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authors.lastname: Hamada
authors.forename: R
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authors.lastname: Kodaira
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authors.lastname: Nogawa
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authors.lastname: Shinji
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authors.lastname: Ito
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authors.lastname: Amano
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authors.lastname: Shimosaka
authors.forename: T
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authors.lastname: Kanda
authors.forename: M
authors.initials: M
authors.lastname: Okazaki