Carbohydrate-binding modules influence substrate specificity of an endoglucanase from Clostridium thermocellum
| Autor: | Makoto Kondo, Shunsuke Ichikawa, Masakazu Goto, Shuichi Karita, Mitsuki Yoshida |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
0106 biological sciences
0301 basic medicine Recombinant Fusion Proteins Gene Expression Cellulase 01 natural sciences Applied Microbiology and Biotechnology Biochemistry Lignin Analytical Chemistry Microbiology Substrate Specificity Cell wall Clostridium thermocellum 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins 010608 biotechnology Clostridium stercorarium Cellulose Molecular Biology Glucans Binding selectivity Enzyme Assays Endo-1 4-beta Xylanases biology Chemistry Hydrolysis Organic Chemistry General Medicine biology.organism_classification Protein Structure Tertiary Kinetics 030104 developmental biology Metabolic Engineering biology.protein Xylanase Carbohydrate-binding module Carrier Proteins Biotechnology Protein Binding |
| Zdroj: | Bioscience, biotechnology, and biochemistry. 80(1) |
| ISSN: | 1347-6947 |
| Popis: | Most cellulases contain carbohydrate-binding modules (CBMs) that largely contribute to their activity for insoluble substrates. Clostridium thermocellum Cel5E 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 from Clostridium josui scaffoldin, or a family 6 xylan-directed CBM from Clostridium stercorarium xylanase 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|