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KMID : 0880220100480060856
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Journal of Microbiology
2010 Volume.48 No. 6 p.856 ~ p.861
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The role of carbohydrate-binding module (CBM) repeat of a multimodular xylanase (XynX) from Clostridium thermocellum in cellulose and xylan binding
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Thangaswamy Selvaraj
Kim Sung-Kyum
Kim Yong-Ho
Jeong Yu-Seok
Kim Yu-Jeong
Nguyen Dinh Phuong
Kim Jung-Ho
Kim Hoon
Jung Kyung-Hwa
Yun Han-Dae
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Abstract
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A non-cellulosomal xylanase from Clostridium thermocellum, XynX, consists of a family-22 carbohydratebinding module (CBM22), a family-10 glycoside hydrolase (GH10) catalytic module, two family-9 carbohydrate-binding modules (CBM9-I and CBM9-II), and an S-layer homology (SLH) module. E. coli BL21(DE3) (pKM29), a transformant carrying xynX′, produced several truncated forms of the enzyme. Among them, three major active species were purified by SDS-PAGE, activity staining, gel-slicing, and diffusion from the gel. The truncated xylanases were different from each other only in their C-terminal regions. In addition to the CBM22 and GH10 catalytic modules, XynX1 had the CBM9-I and most of the CBM9-II, XynX2 had the CBM9-I and about 40% of the CBM9-II, and XynX3 had about 75% of the CBM9-I. The truncated xylanases showed higher binding capacities toward Avicel than those toward insoluble xylan. XynX1 showed a higher affinity toward Avicel (70.5%) than XynX2 (46.0%) and XynX3 (42.1%); however, there were no significant differences in the affinities toward insoluble xylan. It is suggested that the CBM9 repeat, especially CBM9-II, of XynX plays a role in xylan degradation in nature by strengthening cellulose binding rather than by enhancing xylan binding.
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KEYWORD
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Clostridium thermocellum XynX, truncated xylanases, gel-elution, carbohydrate-binding, module, cellulose and xylan binding
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