The Role of Carbohydrate-Binding Module (CBM) Repeat of a Multimodular Xylanase (XynX) from Clostridium thermocellum in Cellulose and Xylan Binding

Thangaswamy Selvaraj; Sung Kyum Kim; Yong Ho Kim; Yu Seok Jeong; Yu-Jeong Kim; Nguyen Dinh Phuong; Kyung Hwa Jung; Jungho Kim; Han Dae Yun; Hoon Kim

doi:10.1007/s12275-010-0285-5

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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: Thangaswamy Selvaraj ¹, Sung Kyum Kim ¹, Yong Ho Kim ¹, Yu Seok Jeong ¹, Yu-Jeong Kim ¹, Nguyen Dinh Phuong ¹, Kyung Hwa Jung ², Jungho Kim ¹, Han Dae Yun ³, Hoon Kim ¹; Journal of Microbiology 2010;48(6):856-861.
DOI: https://doi.org/10.1007/s12275-010-0285-5
Published online: January 9, 2011

¹Department of Agricultural Chemistry, Sunchon National University, Suncheon 540-742, Republic of Korea, ²Amicogen, Inc., 694-4 Sangchon, Jinsung, Jinju 660-852, Republic of Korea, ³Division of Applied Life Science, and Research Institute of Life Science, Gyeongsang National University, Chinju 660-701, Republic of Korea¹Department of Agricultural Chemistry, Sunchon National University, Suncheon 540-742, Republic of Korea, ²Amicogen, Inc., 694-4 Sangchon, Jinsung, Jinju 660-852, Republic of Korea, ³Division of Applied Life Science, and Research Institute of Life Science, Gyeongsang National University, Chinju 660-701, Republic of Korea

Corresponding author: Hoon Kim , Tel: +82-61-750-3294,

Received: 2 August 2010 • Accepted: 15 September 2010

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Abstract

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.

Keywords: Clostridium thermocellum XynX;truncated xylanases;gel-elution;carbohydrate-binding module;cellulose and xylan binding

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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

J. Microbiol. 2010;48(6):856-861. Published online January 9, 2011

DOI: https://doi.org/10.1007/s12275-010-0285-5

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