Purification and properties of the endoglucanase C of Clostridium thermocellum produced in Escherichia coli |
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| Authors: | D Pétré J Millet R Longin P Béguin H Girard J P Aubert |
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| Affiliation: | 1. School of Chemistry, Shoolini University, Solan, 173212 HP India;2. Department of Chemistry, Army Cadet College Wing, Indian Military Academy, Dehradun,248007 UK India;3. Department of Microbiology, Shoolini University, Solan, 173212 HP India;1. Department of Geosciences, Virginia Tech, Blacksburg, VA 24061, USA;2. The Virginia Tech National Center for Earth and Environmental Nanotechnology Infrastructure, Virginia Tech, Blacksburg, VA 24061, USA;3. Department of Civil and Environmental Engineering, Virginia Tech, Blacksburg, VA 24061, USA;4. Department of Geological Sciences, University of Texas at El Paso, El Paso, TX 79968, USA;5. Infrastructure and Environment, School of Engineering, University of Glasgow, Glasgow, G12 8QQ, Scotland, United Kingdom;6. Geosciences Group, Earth Systems Science Division, Pacific Northwest National Laboratory, 902 Battelle Blvd., Richland, WA 99354, USA;7. Environmental Molecular Science Laboratory, Pacific Northwest National Laboratory, 902 Battelle Blvd., Richland, WA 99354, USA;1. School of Civil Engineering, Chongqing University, Chongqing 400045, PR China;2. Key Laboratory of New Technology for Construction of Cities in Mountain Area (Chongqing University), Ministry of Education, Chongqing 400045, PR China;1. Department of Dermatology, Wayne State University School of Medicine, Detroit, Michigan;2. Department of Dermatology, Wayne State University, Detroit, Michigan;3. Department of Dermatology, University of Connecticut Health Center, Farmington, Connecticut;4. Department of Dermatology, University of Florida, Gainesville, Florida;5. Division of Dermatology, Department of Medicine, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, California |
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| Abstract: | The celC gene, which codes for a new endoglucanase of Clostridium thermocellum, termed endoglucanase C, was found to be expressed when cloned in Escherichia coli. The enzyme was purified to electrophoretic homogeneneity from E. coli and its biochemical properties were studied. It differs from the previously studied endoglucanases A and B. In particular, endoglucanase C displays features common to endo- and exoglucanases, since it had a high activity on carboxymethylcellulose and on p-nitrophenyl-beta-D-cellobioside where only the agluconic bond was split. In addition, the enzyme was able to release cellobiose units from G3, G4 and G5 cellodextrins. Endoglucanase C was characterized by Western blot in a culture supernatant from C. thermocellum grown on cellulose, using an antiserum raised against the enzyme produced by E. coli. |
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