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4 results on '"cellulovorans"'

1. Substrate-Induced Production and Secretion of Cellulases by Clostridium acetobutylicum

Author

Aernout A. Martens, Ana M. López-Contreras, Bernadet Renckens, John van der Oost, Willem M. de Vos, Pieternel A. M. Claassen, and Krisztina Gábor

Subjects
Clostridium acetobutylicum, Bioinformatics, Laboratorium voor Fysische chemie en Kolloïdkunde, Catabolite repression, Cellobiose, Cellulase, solvent production, Xylose, Polymerase Chain Reaction, Microbiology, Applied Microbiology and Biotechnology, Substrate Specificity, trichoderma-reesei, Cellulosome, chemistry.chemical_compound, Bacterial Proteins, thermocellum, Microbiologie, Gene cluster, gene, Physical Chemistry and Colloid Science, bacillus-subtilis, cellulose-binding domain, Trichoderma reesei, DNA Primers, VLAG, catabolite repression, degradation, Clostridium, Base Sequence, Ecology, biology, Reverse Transcriptase Polymerase Chain Reaction, cellulovorans, Physiology and Biotechnology, biology.organism_classification, Recombinant Proteins, Biochemistry, chemistry, gram-positive bacteria, AFSG Biobased Products, biology.protein, Cellular energy metabolism [UMCN 5.3], Food Science, Biotechnology
Abstract

Clostridium acetobutylicum ATCC 824 is a solventogenic bacterium that grows heterotrophically on a variety of carbohydrates, including glucose, cellobiose, xylose, and lichenan, a linear polymer of β-1,3- and β-1,4-linked β- d -glucose units. C. acetobutylicum does not degrade cellulose, although its genome sequence contains several cellulase-encoding genes and a complete cellulosome cluster of cellulosome genes. In the present study, we demonstrate that a low but significant level of induction of cellulase activity occurs during growth on xylose or lichenan. The celF gene, located in the cellulosome-like gene cluster and coding for a unique cellulase that belongs to glycoside hydrolase family 48, was cloned in Escherichia coli , and antibodies were raised against the overproduced CelF protein. A Western blot analysis suggested a possible catabolite repression by glucose or cellobiose and an up-regulation by lichenan or xylose of the extracellular production of CelF by C. acetobutylicum . Possible reasons for the apparent inability of C. acetobutylicum to degrade cellulose are discussed.

Published
2004
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2. Production by Clostridium acetobutylicum ATCC 824 of CelG, a cellulosomal glycoside hydrolase belonging to family 9

Author

John van der Oost, Pieternel A. M. Claassen, Hans Mooibroek, Willem M. de Vos, Aernout A. Martens, Nora Szijarto, and Ana M. López-Contreras

Subjects
Laboratorium voor Fysische chemie en Kolloïdkunde, acetone, Cellobiose, solvent production, medicine.disease_cause, Applied Microbiology and Biotechnology, butanol, Cellulosome, chemistry.chemical_compound, Clostridium, Microbiologie, Gene cluster, Glycoside hydrolase, cellulolyticum, Physical Chemistry and Colloid Science, Glucans, fermentation, degradation, Xylose, Ecology, biology, Physiology and Biotechnology, Recombinant Proteins, crystalline cellulose, Biochemistry, AFSG Biobased Products, Multigene Family, Biotechnology, Clostridium acetobutylicum, Glycoside Hydrolases, Molecular Sequence Data, Microbiology, Open Reading Frames, Bacterial Proteins, Cellulase, medicine, Amino Acid Sequence, Cellulose, Escherichia coli, Clostridium cellulovorans, VLAG, cellulovorans, cellulases, biology.organism_classification, Culture Media, chemistry, Food Science, domestic organic waste
Abstract

The genome sequence of Clostridium acetobutylicum ATCC 824, a noncellulolytic solvent-producing strain, predicts the production of various proteins with domains typical for cellulosomal subunits. Most of the genes coding for these proteins are grouped in a cluster similar to that found in cellulolytic clostridial species, such as Clostridium cellulovorans . CAC0916, one of the open reading frames present in the putative cellulosome gene cluster, codes for CelG, a putative endoglucanase belonging to family 9, and it was cloned and overexpressed in Escherichia coli . The overproduced CelG protein was purified by making use of its high affinity for cellulose and was characterized. The biochemical properties of the purified CelG were comparable to those of other known enzymes belonging to the same family. Expression of CelG by C. acetobutylicum grown on different substrates was studied by Western blotting by using antibodies raised against the purified E. coli -produced protein. Whereas the antibodies cross-reacted with CelG-like proteins secreted by cellobiose- or cellulose-grown C. cellulovorans cultures, CelG was not detectable in extracellular medium from C. acetobutylicum grown on cellobiose or glucose. However, notably, when lichenan-grown cultures were used, several bands corresponding to CelG or CelG-like proteins were present, and there was significantly increased extracellular endoglucanase activity.

Published
2003

3. Substrate-induced production and secretion of cellulases by Clostridium acetobutylicum

Author

Lopez Contreras, A.M., Gabor, K., Martens, A.A., Renckens, B.A.M., Claassen, P.A.M., van der Oost, J., de Vos, W.M., Lopez Contreras, A.M., Gabor, K., Martens, A.A., Renckens, B.A.M., Claassen, P.A.M., van der Oost, J., and de Vos, W.M.

Abstract

Clostridium acetobutylicum ATCC 824 is a solventogenic bacterium that grows heterotrophically on a variety of carbohydrates, including glucose, cellobiose, xylose, and lichenan, a linear polymer of beta-1,3- and beta-1,4-linked beta-D-glucose units. C. acetobutylicum does not degrade cellulose, although its genome sequence contains several cellulase-encoding genes and a complete cellulosome cluster of cellulosome genes. In the present study, we demonstrate that a low but significant level of induction of cellulase activity occurs during growth on xylose or lichenan. The celF gene, located in the cellulosome-like gene cluster and coding for a unique cellulase that belongs to glycoside hydrolase family 48, was cloned in Escherichia coli, and antibodies were raised against the overproduced CelF protein. A Western blot analysis suggested a possible catabolite repression by glucose or cellobiose and an up-regulation by lichenan or xylose of the extracellular production of CelF by C. acetobutylicum. Possible reasons for the apparent inability of C. acetobutylicum to degrade cellulose are discussed.

Published
2004

4. Production by Clostridium acetobutylicum ATCC 824 of CelG, a cellulosomal glycoside hydrolase belonging to family 9

Author

Lopez Contreras, A.M., Martens, A.A., Szijarto, N., Mooibroek, A., Claassen, P.A.M., van der Oost, J., de Vos, W.M., Lopez Contreras, A.M., Martens, A.A., Szijarto, N., Mooibroek, A., Claassen, P.A.M., van der Oost, J., and de Vos, W.M.

Abstract

The genome sequence of Clostridium acetobutylicum ATCC 824, a noncellulolytic solvent-producing strain, predicts the production of various proteins with domains typical for cellulosomal subunits. Most of the genes coding for these proteins are grouped in a cluster similar to that found in cellulolytic clostridial species, such as Clostridium cellulovorans. CAC0916, one of the open reading frames present in the putative cellulosome gene cluster, codes for CelG, a putative endoglucanase belonging to family 9, and it was cloned and overexpressed in Escherichia coli. The overproduced CelG protein was purified by making use of its high affinity for cellulose and was characterized. The biochemical properties of the purified CelG were comparable to those of other known enzymes belonging to the same family. Expression of CelG by C. acetobutylicum grown on different substrates was studied by Western blotting by using antibodies raised against the purified E. coli-produced protein. Whereas the antibodies cross-reacted with CelG-like proteins secreted by cellobiose- or cellulose-grown C. cellulovorans cultures, CelG was not detectable in extracellular medium from C. acetobutylicum grown on cellobiose or glucose. However, notably, when lichenan-grown cultures were used, several bands corresponding to CelG or CelG-like proteins were present, and there was significantly increased extracellular endoglucanase activity

Published
2003

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