1. Carbohydrate-binding modules influence substrate specificity of an endoglucanase from Clostridium thermocellum.
- Author
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Ichikawa, Shunsuke, Yoshida, Mitsuki, Karita, Shuichi, Kondo, Makoto, and Goto, Masakazu
- Subjects
CELLULASE ,XYLANASES ,CLOSTRIDIUM thermocellum - Abstract
Most cellulases contain carbohydrate-binding modules (CBMs) that largely contribute to their activity for insoluble substrates.Clostridium thermocellumCel5E is an endoglucanase having xylanolytic activity. The Cel5E originally has a family 11 CBM preferentially binding to β-1,4- and β-1,3-1,4-mixed linkage glucans. In this study, we replaced the CBM with a different type of CBM, either a family 3 microcrystalline cellulose-directed CBM fromClostridium josuiscaffoldin, or a family 6 xylan-directed CBM fromClostridium stercorariumxylanase 11A. Chimeric endoglucanases showed enhanced activity that was affected by CBM binding specificity. These chimeric enzymes could efficiently degrade milled lignocellulosic materials, such as corn hulls, because of heterologous components in the plant cell wall, indicating that diverse CBMs play roles in degradation of lignocellulosic materials. Substrate specificities of an endoglucanase, Cel5E fromClostridium thermocellumwere affected by fusion of different type CBMs. [ABSTRACT FROM PUBLISHER]
- Published
- 2016
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