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Journal articles on the topic 'Cellulose – Microbiology'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 February 2022

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1

Gaudin, Christian, Anne Belaich, Stéphanie Champ, and Jean-Pierre Belaich. "CelE, a Multidomain Cellulase fromClostridium cellulolyticum: a Key Enzyme in the Cellulosome?" Journal of Bacteriology 182, no. 7 (April 1, 2000): 1910–15. http://dx.doi.org/10.1128/jb.182.7.1910-1915.2000.

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ABSTRACT CelE, one of the three major proteins of the cellulosome ofClostridium cellulolyticum, was characterized. The amino acid sequence of the protein deduced from celE DNA sequence led us to the supposition that CelE is a three-domain protein. Recombinant CelE and a truncated form deleted of the putative cellulose binding domain (CBD) were obtained. Deletion of the CBD induces a total loss of activity. Exhibiting rather low levels of activity on soluble, amorphous, and crystalline celluloses, CelE is more active onp-nitrophenyl–cellobiose than the other cellulases from this organism charac

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2

Krauss, Jan, Vladimir V. Zverlov, and Wolfgang H. Schwarz. "In VitroReconstitution of the Complete Clostridium thermocellum Cellulosome and Synergistic Activity on Crystalline Cellulose." Applied and Environmental Microbiology 78, no. 12 (April 20, 2012): 4301–7. http://dx.doi.org/10.1128/aem.07959-11.

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ABSTRACTArtificial cellulase complexes active on crystalline cellulose were reconstitutedin vitrofrom a native mix of cellulosomal enzymes and CipA scaffoldin. Enzymes containing dockerin modules for binding to the corresponding cohesin modules were prepared from culture supernatants of aC. thermocellum cipAmutant. They were reassociated to cellulosomes via dockerin-cohesin interaction. Recombinantly produced mini-CipA proteins with one to three cohesins either with or without the carbohydrate-binding module (CBM) and the complete CipA protein were used as the cellulosomal backbone. The bindin

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Hetzler, Stephan, Daniel Bröker, and Alexander Steinbüchel. "Saccharification of Cellulose by Recombinant Rhodococcus opacus PD630 Strains." Applied and Environmental Microbiology 79, no. 17 (June 21, 2013): 5159–66. http://dx.doi.org/10.1128/aem.01214-13.

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ABSTRACTThe noncellulolytic actinomyceteRhodococcus opacusstrain PD630 is the model oleaginous prokaryote with regard to the accumulation and biosynthesis of lipids, which serve as carbon and energy storage compounds and can account for as much as 87% of the dry mass of the cell in this strain. In order to establish cellulose degradation inR. opacusPD630, we engineered strains that episomally expressed six different cellulase genes fromCellulomonas fimiATCC 484 (cenABC,cex,cbhA) andThermobifida fuscaDSM43792 (cel6A), thereby enablingR. opacusPD630 to degrade cellulosic substrates to cellobiose

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4

Lynd, Lee R., Paul J. Weimer, Willem H. van Zyl, and Isak S. Pretorius. "Microbial Cellulose Utilization: Fundamentals and Biotechnology." Microbiology and Molecular Biology Reviews 66, no. 3 (September 2002): 506–77. http://dx.doi.org/10.1128/mmbr.66.3.506-577.2002.

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SUMMARY Fundamental features of microbial cellulose utilization are examined at successively higher levels of aggregation encompassing the structure and composition of cellulosic biomass, taxonomic diversity, cellulase enzyme systems, molecular biology of cellulase enzymes, physiology of cellulolytic microorganisms, ecological aspects of cellulase-degrading communities, and rate-limiting factors in nature. The methodological basis for studying microbial cellulose utilization is considered relative to quantification of cells and enzymes in the presence of solid substrates as well as apparatus a

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Caspi, Jonathan, Yoav Barak, Rachel Haimovitz, Diana Irwin, Raphael Lamed, David B. Wilson, and Edward A. Bayer. "Effect of Linker Length and Dockerin Position on Conversion of a Thermobifida fusca Endoglucanase to the Cellulosomal Mode." Applied and Environmental Microbiology 75, no. 23 (October 9, 2009): 7335–42. http://dx.doi.org/10.1128/aem.01241-09.

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ABSTRACT We have been developing the cellulases of Thermobifida fusca as a model to explore the conversion from a free cellulase system to the cellulosomal mode. Three of the six T. fusca cellulases (endoglucanase Cel6A and exoglucanases Cel6B and Cel48A) have been converted in previous work by replacing their cellulose-binding modules (CBMs) with a dockerin, and the resultant recombinant “cellulosomized” enzymes were incorporated into chimeric scaffolding proteins that contained cohesin(s) together with a CBM. The activities of the resultant designer cellulosomes were compared with an equival

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Kudanga, T., and E. Mwenje. "Extracellular cellulase production by tropical isolates of Aureobasidium pullulans." Canadian Journal of Microbiology 51, no. 9 (September 1, 2005): 773–76. http://dx.doi.org/10.1139/w05-053.

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Cellulase production by Aureobasidium pullulans from the temperate regions has remained speculative, with most studies reporting no activity at all. In the current study, tropical isolates from diverse sources were screened for cellulase production. Isolates were grown on a synthetic medium containing cell walls of Msasa tree (Brachystegia sp.) as the sole carbon source, and their cellulolytic activities were measured using carboxymethyl cellulose and α-cellulose as substrates. All isolates studied produced carboxymethyl cellulase (endoglucanase) and alpha-cellulase (exoglucanase) activity. En

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Wang, Hongliang, Fabio Squina, Fernando Segato, Andrew Mort, David Lee, Kirk Pappan, and Rolf Prade. "High-Temperature Enzymatic Breakdown of Cellulose." Applied and Environmental Microbiology 77, no. 15 (June 17, 2011): 5199–206. http://dx.doi.org/10.1128/aem.00199-11.

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ABSTRACTCellulose is an abundant and renewable biopolymer that can be used for biofuel generation; however, structural entrapment with other cell wall components hinders enzyme-substrate interactions, a key bottleneck for ethanol production. Biomass is routinely subjected to treatments that facilitate cellulase-cellulose contacts. Cellulases and glucosidases act by hydrolyzing glycosidic bonds of linear glucose β-1,4-linked polymers, producing glucose. Here we describe eight high-temperature-operating cellulases (TCel enzymes) identified from a survey of thermobacterial and archaeal genomes. T

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Zhou, Qingxin, Jintao Xu, Yanbo Kou, Xinxing Lv, Xi Zhang, Guolei Zhao, Weixin Zhang, Guanjun Chen та Weifeng Liu. "Differential Involvement of β-Glucosidases from Hypocrea jecorina in Rapid Induction of Cellulase Genes by Cellulose and Cellobiose". Eukaryotic Cell 11, № 11 (21 вересня 2012): 1371–81. http://dx.doi.org/10.1128/ec.00170-12.

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ABSTRACTAppropriate perception of cellulose outside the cell by transforming it into an intracellular signal ensures the rapid production of cellulases by cellulolyticHypocrea jecorina. The major extracellular β-glucosidase BglI (CEL3a) has been shown to contribute to the efficient induction of cellulase genes. Multiple β-glucosidases belonging to glycosyl hydrolase (GH) family 3 and 1, however, exist inH. jecorina. Here we demonstrated that CEL1b, like CEL1a, was an intracellular β-glucosidase displayingin vitrotransglycosylation activity. We then found evidence that these two major intracell

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Liu, Wenjin, Xiao-Zhou Zhang, Zuoming Zhang, and Y. H. Percival Zhang. "Engineering of Clostridium phytofermentans Endoglucanase Cel5A for Improved Thermostability." Applied and Environmental Microbiology 76, no. 14 (May 28, 2010): 4914–17. http://dx.doi.org/10.1128/aem.00958-10.

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ABSTRACT A family 5 glycoside hydrolase from Clostridium phytofermentans was cloned and engineered through a cellulase cell surface display system in Escherichia coli. The presence of cell surface anchoring, a cellulose binding module, or a His tag greatly influenced the activities of wild-type and mutant enzymes on soluble and solid cellulosic substrates, suggesting the high complexity of cellulase engineering. The best mutant had 92%, 36%, and 46% longer half-lives at 60°C on carboxymethyl cellulose, regenerated amorphous cellulose, and Avicel, respectively.

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Murashima, Koichiro, Akihiko Kosugi, and Roy H. Doi. "Synergistic Effects on Crystalline Cellulose Degradation between Cellulosomal Cellulases from Clostridium cellulovorans." Journal of Bacteriology 184, no. 18 (September 15, 2002): 5088–95. http://dx.doi.org/10.1128/jb.184.18.5088-5095.2002.

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ABSTRACT Clostridium cellulovorans produces a multienzyme cellulose-degrading complex called the cellulosome. In this study, we determined the synergistic effects on crystalline cellulose degradation by three different recombinant cellulosomes containing either endoglucanase EngE, endoglucanase EngH, or exoglucanase ExgS bound to mini-CbpA, a part of scaffolding protein CbpA. EngE, EngH, and ExgS are classified into the glycosyl hydrolase families 5, 9, and 48, respectively. The assembly of ExgS and EngH with mini-CbpA increased the activity against insoluble cellulose 1.5- to 3-fold, although

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Blair, Benjie G., and Kevin L. Anderson. "Regulation of cellulose-inducible structures of Clostridium cellulovorans." Canadian Journal of Microbiology 45, no. 3 (March 1, 1999): 242–49. http://dx.doi.org/10.1139/w99-004.

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Scanning electron microscopy was used to detect ultrastructural protuberances on the cellulolytic anaerobe Clostridium cellulovorans. Numerous ultrastructural protuberances were observed on cellulose-grown cells, but few were detected on glucose-, fructose-, cellobiose-, or carboxymethylcellulose (CMC)-grown cells. Formation of these protuberances was detected within 2 h of incubation in cellulose medium, but 4 h incubation was required before numerous structures were observed on the cells. When a soluble carbohydrate or CMC was mixed with cellulose-grown cells, the ultrastructural protuberanc

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Yadav, Vikas, Bruce J. Paniliatis, Hai Shi, Kyongbum Lee, Peggy Cebe, and David L. Kaplan. "Novel In Vivo-Degradable Cellulose-Chitin Copolymer from Metabolically Engineered Gluconacetobacter xylinus." Applied and Environmental Microbiology 76, no. 18 (July 23, 2010): 6257–65. http://dx.doi.org/10.1128/aem.00698-10.

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ABSTRACT Despite excellent biocompatibility and mechanical properties, the poor in vitro and in vivo degradability of cellulose has limited its biomedical and biomass conversion applications. To address this issue, we report a metabolic engineering-based approach to the rational redesign of cellular metabolites to introduce N-acetylglucosamine (GlcNAc) residues into cellulosic biopolymers during de novo synthesis from Gluconacetobacter xylinus. The cellulose produced from these engineered cells (modified bacterial cellulose [MBC]) was evaluated and compared with cellulose produced from normal

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13

Murashima, Koichiro, Akihiko Kosugi, and Roy H. Doi. "Synergistic Effects of Cellulosomal Xylanase and Cellulases from Clostridium cellulovorans on Plant Cell Wall Degradation." Journal of Bacteriology 185, no. 5 (March 1, 2003): 1518–24. http://dx.doi.org/10.1128/jb.185.5.1518-1524.2003.

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ABSTRACT Plant cell walls are comprised of cellulose and hemicellulose and other polymers that are intertwined, and this complex structure presents a barrier to degradation by pure cellulases or hemicellulases. In this study, we determined the synergistic effects on corn cell wall degradation by the action of cellulosomal xylanase XynA and cellulosomal cellulases from Clostridium cellulovorans. XynA minicellulosomes and cellulase minicellulosomes were found to degrade corn cell walls synergistically but not purified substrates such as xylan and crystalline cellulose. The mixture of XynA and ce

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Bae, Jungu, Kouichi Kuroda, and Mitsuyoshi Ueda. "Proximity Effect among Cellulose-Degrading Enzymes Displayed on the Saccharomyces cerevisiae Cell Surface." Applied and Environmental Microbiology 81, no. 1 (October 10, 2014): 59–66. http://dx.doi.org/10.1128/aem.02864-14.

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ABSTRACTProximity effect is a form of synergistic effect exhibited when cellulases work within a short distance from each other, and this effect can be a key factor in enhancing saccharification efficiency. In this study, we evaluated the proximity effect between 3 cellulose-degrading enzymes displayed on theSaccharomyces cerevisiaecell surface, that is, endoglucanase, cellobiohydrolase, and β-glucosidase. We constructed 2 kinds of arming yeasts through genome integration: ALL-yeast, which simultaneously displayed the 3 cellulases (thus, the different cellulases were near each other), and MIX-

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15

Mohand-Oussaid, O., S. Payot, E. Guedon, E. Gelhaye, A. Youyou, and H. Petitdemange. "The Extracellular Xylan Degradative System inClostridium cellulolyticum Cultivated on Xylan: Evidence for Cell-Free Cellulosome Production." Journal of Bacteriology 181, no. 13 (July 1, 1999): 4035–40. http://dx.doi.org/10.1128/jb.181.13.4035-4040.1999.

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ABSTRACT In this study, we demonstrate that the cellulosome ofClostridium cellulolyticum grown on xylan is not associated with the bacterial cell. Indeed, the large majority of the activity (about 90%) is localized in the cell-free fraction when the bacterium is grown on xylan. Furthermore, about 70% of the detected xylanase activity is associated with cell-free high-molecular-weight complexes containing avicelase activity and the cellulosomal scaffolding protein CipC. The same repartition is observed with carboxymethyl cellulase activity. The cellulose adhesion of xylan-grown cells is sharply

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Mingardon, Florence, Angélique Chanal, Chantal Tardif, Edward A. Bayer, and Henri-Pierre Fierobe. "Exploration of New Geometries in Cellulosome-Like Chimeras." Applied and Environmental Microbiology 73, no. 22 (September 28, 2007): 7138–49. http://dx.doi.org/10.1128/aem.01306-07.

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ABSTRACT In this study, novel cellulosome chimeras exhibiting atypical geometries and binding modes, wherein the targeting and proximity functions were directly incorporated as integral parts of the enzyme components, were designed. Two pivotal cellulosomal enzymes (family 48 and 9 cellulases) were thus appended with an efficient cellulose-binding module (CBM) and an optional cohesin and/or dockerin. Compared to the parental enzymes, the chimeric cellulases exhibited improved activity on crystalline cellulose as opposed to their reduced activity on amorphous cellulose. Nevertheless, the variou

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López-Contreras, Ana M., Krisztina Gabor, Aernout A. Martens, Bernadet A. M. Renckens, Pieternel A. M. Claassen, John van der Oost, and Willem M. de Vos. "Substrate-Induced Production and Secretion of Cellulases by Clostridium acetobutylicum." Applied and Environmental Microbiology 70, no. 9 (September 2004): 5238–43. http://dx.doi.org/10.1128/aem.70.9.5238-5243.2004.

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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 t

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Yi-Heng, Zhang Percival, and Lee R. Lynd. "Regulation of Cellulase Synthesis in Batch and Continuous Cultures of Clostridium thermocellum." Journal of Bacteriology 187, no. 1 (January 1, 2005): 99–106. http://dx.doi.org/10.1128/jb.187.1.99-106.2005.

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ABSTRACT Regulation of cell-specific cellulase synthesis (expressed in milligrams of cellulase per gram [dry weight] of cells) by Clostridium thermocellum was investigated using an enzyme-linked immunosorbent assay protocol based on antibody raised against a peptide sequence from the scaffoldin protein of the cellulosome (Zhang and Lynd, Anal. Chem. 75:219-227, 2003). The cellulase synthesis in Avicel-grown batch cultures was ninefold greater than that in cellobiose-grown batch cultures. In substrate-limited continuous cultures, however, the cellulase synthesis with Avicel-grown cultures was 1

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Mingardon, Florence, Angï¿½lique Chanal, Ana M. Lï¿½pez-Contreras, Cyril Dray, Edward A. Bayer, and Henri-Pierre Fierobe. "Incorporation of Fungal Cellulases in Bacterial Minicellulosomes Yields Viable, Synergistically Acting Cellulolytic Complexes." Applied and Environmental Microbiology 73, no. 12 (April 27, 2007): 3822–32. http://dx.doi.org/10.1128/aem.00398-07.

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ABSTRACT Artificial designer minicellulosomes comprise a chimeric scaffoldin that displays an optional cellulose-binding module (CBM) and bacterial cohesins from divergent species which bind strongly to enzymes engineered to bear complementary dockerins. Incorporation of cellulosomal cellulases from Clostridium cellulolyticum into minicellulosomes leads to artificial complexes with enhanced activity on crystalline cellulose, due to enzyme proximity and substrate targeting induced by the scaffoldin-borne CBM. In the present study, a bacterial dockerin was appended to the family 6 fungal cellula

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Somkuti, G. A. "Synthesis of Cellulase by Mucor pusillus and Mucor miehei." Microbiology 81, no. 1 (January 1, 2000): 1–6. http://dx.doi.org/10.1099/00221287-81-1-1.

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Strains of Mucor pusillus and M. miehei were found to synthesize β-1,4-glucan glucanohydrolase (cellulase) in a complex medium. The inducible enzyme complex hydrolysed carboxymethylcellulose, acid-swollen cellulose and unmodified cellulose.

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Schmoll, Monika, André Schuster, Roberto do Nascimento Silva, and Christian P. Kubicek. "The G-Alpha Protein GNA3 of Hypocrea jecorina (Anamorph Trichoderma reesei) Regulates Cellulase Gene Expression in the Presence of Light." Eukaryotic Cell 8, no. 3 (January 9, 2009): 410–20. http://dx.doi.org/10.1128/ec.00256-08.

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ABSTRACT Although the enzymes enabling Hypocrea jecorina (anamorph Trichoderma reesei) to degrade the insoluble substrate cellulose have been investigated in some detail, little is still known about the mechanism by which cellulose signals its presence to the fungus. In order to investigate the possible role of a G-protein/cyclic AMP signaling pathway, the gene encoding GNA3, which belongs to the adenylate cyclase-activating class III of G-alpha subunits, was cloned. gna3 is clustered in tandem with the mitogen-activated protein kinase gene tmk3 and the glycogen phosphorylase gene gph1. The gn

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Mba Medie, Felix, Iskandar Ben Salah, Michel Drancourt, and Bernard Henrissat. "Paradoxical conservation of a set of three cellulose-targeting genes in Mycobacterium tuberculosis complex organisms." Microbiology 156, no. 5 (May 1, 2010): 1468–75. http://dx.doi.org/10.1099/mic.0.037812-0.

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The genome of the tuberculosis agent Mycobacterium tuberculosis encodes a putative cellulose-binding protein (CBD2), one candidate cellulase (Cel12), and one fully active cellulase (Cel6). This observation is puzzling, because cellulose is a major component of plant cell walls, whereas M. tuberculosis is a human pathogen without known contact with plants. In order to investigate the biological role of such cellulose-targeting genes in M. tuberculosis we report here the search for and transcription analysis of this set of genes in the genus Mycobacterium. An in silico search for cellulose-targe

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Demain, Arnold L., Michael Newcomb, and J. H. David Wu. "Cellulase, Clostridia, and Ethanol." Microbiology and Molecular Biology Reviews 69, no. 1 (March 2005): 124–54. http://dx.doi.org/10.1128/mmbr.69.1.124-154.2005.

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SUMMARY Biomass conversion to ethanol as a liquid fuel by the thermophilic and anaerobic clostridia offers a potential partial solution to the problem of the world's dependence on petroleum for energy. Coculture of a cellulolytic strain and a saccharolytic strain of Clostridium on agricultural resources, as well as on urban and industrial cellulosic wastes, is a promising approach to an alternate energy source from an economic viewpoint. This review discusses the need for such a process, the cellulases of clostridia, their presence in extracellular complexes or organelles (the cellulosomes), t

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Rincón, Marco T., Sheila I. McCrae, James Kirby, Karen P. Scott, and Harry J. Flint. "EndB, a Multidomain Family 44 Cellulase from Ruminococcus flavefaciens 17, Binds to Cellulose via a Novel Cellulose-Binding Module and to Another R. flavefaciens Protein via a Dockerin Domain." Applied and Environmental Microbiology 67, no. 10 (October 1, 2001): 4426–31. http://dx.doi.org/10.1128/aem.67.10.4426-4431.2001.

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ABSTRACT The mechanisms by which cellulolytic enzymes and enzyme complexes in Ruminococcus spp. bind to cellulose are not fully understood. The product of the newly isolated cellulase geneendB from Ruminococcus flavefaciens 17 was purified as a His-tagged product after expression inEscherichia coli and found to be able to bind directly to crystalline cellulose. The ability to bind cellulose is shown to be associated with a novel cellulose-binding module (CBM) located within a region of 200 amino acids that is unrelated to known protein sequences. EndB (808 amino acids) also contains a catalyti

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Aro, Nina, Marja Ilmén, Anu Saloheimo, and Merja Penttilä. "ACEI of Trichoderma reesei Is a Repressor of Cellulase and Xylanase Expression." Applied and Environmental Microbiology 69, no. 1 (January 2003): 56–65. http://dx.doi.org/10.1128/aem.69.1.56-65.2003.

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ABSTRACT We characterized the effect of deletion of the Trichoderma reesei (Hypocrea jecorina) ace1 gene encoding the novel cellulase regulator ACEI that was isolated based on its ability to bind to and activate in vivo in Saccharomyces cerevisiae the promoter of the main cellulase gene, cbh1. Deletion of ace1 resulted in an increase in the expression of all the main cellulase genes and two xylanase genes in sophorose- and cellulose-induced cultures, indicating that ACEI acts as a repressor of cellulase and xylanase expression. Growth of the strain with a deletion of the ace1 gene on different

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Cunha, Eva S., Christine L. Hatem, and Doug Barrick. "Insertion of Endocellulase Catalytic Domains into Thermostable Consensus Ankyrin Scaffolds: Effects on Stability and Cellulolytic Activity." Applied and Environmental Microbiology 79, no. 21 (August 23, 2013): 6684–96. http://dx.doi.org/10.1128/aem.02121-13.

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ABSTRACTDegradation of cellulose for biofuels production holds promise in solving important environmental and economic problems. However, the low activities (and thus high enzyme-to-substrate ratios needed) of hydrolytic cellulase enzymes, which convert cellulose into simple sugars, remain a major barrier. As a potential strategy to stabilize cellulases and enhance their activities, we have embedded cellulases of extremophiles into hyperstable α-helical consensus ankyrin domain scaffolds. We found the catalytic domains CelA (CA, GH8;Clostridium thermocellum) and Cel12A (C12A, GH12;Thermotoga m

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Gupta, Pratima, Kalpana Samant, and Avinash Sahu. "Isolation of Cellulose-Degrading Bacteria and Determination of Their Cellulolytic Potential." International Journal of Microbiology 2012 (2012): 1–5. http://dx.doi.org/10.1155/2012/578925.

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Eight isolates of cellulose-degrading bacteria (CDB) were isolated from four different invertebrates (termite, snail, caterpillar, and bookworm) by enriching the basal culture medium with filter paper as substrate for cellulose degradation. To indicate the cellulase activity of the organisms, diameter of clear zone around the colony and hydrolytic value on cellulose Congo Red agar media were measured. CDB 8 and CDB 10 exhibited the maximum zone of clearance around the colony with diameter of 45 and 50 mm and with the hydrolytic value of 9 and 9.8, respectively. The enzyme assays for two enzyme

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Han, Sung O., Hideaki Yukawa, Masayuki Inui, and Roy H. Doi. "Effect of carbon source on the cellulosomal subpopulations of Clostridium cellulovorans." Microbiology 151, no. 5 (May 1, 2005): 1491–97. http://dx.doi.org/10.1099/mic.0.27605-0.

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Clostridium cellulovorans produces a cellulase enzyme complex called the cellulosome. When cells were grown on different carbon substrates such as Avicel, pectin, xylan, or a mixture of all three, the subunit composition of the cellulosomal subpopulations and their enzymic activities varied significantly. Fractionation of the cellulosomes (7–11 fractions) indicated that the cellulosome population was heterogeneous, although the composition of the scaffolding protein CbpA, endoglucanase EngE and cellobiohydrolase ExgS was relatively constant. One of the cellulosomal fractions with the greatest

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Jahn, Courtney E., Dija A. Selimi, Jeri D. Barak, and Amy O. Charkowski. "The Dickeya dadantii biofilm matrix consists of cellulose nanofibres, and is an emergent property dependent upon the type III secretion system and the cellulose synthesis operon." Microbiology 157, no. 10 (October 1, 2011): 2733–44. http://dx.doi.org/10.1099/mic.0.051003-0.

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Dickeya dadantii is a plant-pathogenic bacterium that produces cellulose-containing biofilms, called pellicles, at the air–liquid interface of liquid cultures. D. dadantii pellicle formation appears to be an emergent property dependent upon at least three gene clusters, including cellulose synthesis, type III secretion system (T3SS) and flagellar genes. The D. dadantii cellulose synthesis operon is homologous to that of Gluconacetobacter xylinus, which is used for industrial cellulose production, and the cellulose nanofibres produced by D. dadantii were similar in diameter and branching patter

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Cai, Shichun, Jiabao Li, Fen Ze Hu, Kegui Zhang, Yuanming Luo, Benjamin Janto, Robert Boissy, Garth Ehrlich, and Xiuzhu Dong. "Cellulosilyticum ruminicola, a Newly Described Rumen Bacterium That Possesses Redundant Fibrolytic-Protein-Encoding Genes and Degrades Lignocellulose with Multiple Carbohydrate- Borne Fibrolytic Enzymes." Applied and Environmental Microbiology 76, no. 12 (April 16, 2010): 3818–24. http://dx.doi.org/10.1128/aem.03124-09.

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ABSTRACT Cellulosilyticum ruminicola H1 is a newly described bacterium isolated from yak (Bos grunniens) rumen and is characterized by its ability to grow on a variety of hemicelluloses and degrade cellulosic materials. In this study, we performed the whole-genome sequencing of C. ruminicola H1 and observed a comprehensive set of genes encoding the enzymes essential for hydrolyzing plant cell wall. The corresponding enzymatic activities were also determined in strain H1; these included endoglucanases, cellobiohydrolases, xylanases, mannanase, pectinases, and feruloyl esterases and acetyl ester

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Xu, Feng, Hanshu Ding, and Ani Tejirian. "Detrimental effect of cellulose oxidation on cellulose hydrolysis by cellulase." Enzyme and Microbial Technology 45, no. 3 (September 2009): 203–9. http://dx.doi.org/10.1016/j.enzmictec.2009.06.002.

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Han, Sung Ok, Hideaki Yukawa, Masayuki Inui, and Roy H. Doi. "Regulation of Expression of Cellulosomal Cellulase and Hemicellulase Genes in Clostridium cellulovorans." Journal of Bacteriology 185, no. 20 (October 15, 2003): 6067–75. http://dx.doi.org/10.1128/jb.185.20.6067-6075.2003.

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ABSTRACT The regulation of expression of the genes encoding the cellulases and hemicellulases of Clostridium cellulovorans was studied at the mRNA level with cells grown under various culture conditions. A basic pattern of gene expression and of relative expression levels was obtained from cells grown in media containing poly-, di- or monomeric sugars. The cellulase (cbpA and engE) and hemicellulase (xynA) genes were coordinately expressed in medium containing cellobiose or cellulose. Growth in the presence of cellulose, xylan, and pectin gave rise to abundant expression of most genes (cbpA-ex

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Kosugi, Akihiko, Yoshihiko Amano, Koichiro Murashima, and Roy H. Doi. "Hydrophilic Domains of Scaffolding Protein CbpA Promote Glycosyl Hydrolase Activity and Localization of Cellulosomes to the Cell Surface of Clostridium cellulovorans." Journal of Bacteriology 186, no. 19 (October 1, 2004): 6351–59. http://dx.doi.org/10.1128/jb.186.19.6351-6359.2004.

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ABSTRACT CbpA, the scaffolding protein of Clostridium cellulovorans cellulosomes, possesses one family 3 cellulose binding domain, nine cohesin domains, and four hydrophilic domains (HLDs). Among the three types of domains, the function of the HLDs is still unknown. We proposed previously that the HLDs of CbpA play a role in attaching the cellulosome to the cell surface, since they showed some homology to the surface layer homology domains of EngE. Several recombinant proteins with HLDs (rHLDs) and recombinant EngE (rEngE) were examined to determine their binding to the C. cellulovorans cell w

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Derda, Monika, Jadwiga Winiecka-Krusnell, Markus B. Linder, and Ewert Linder. "Labeled Trichoderma reesei Cellulase as a Marker for Acanthamoeba Cyst Wall Cellulose in Infected Tissues." Applied and Environmental Microbiology 75, no. 21 (September 4, 2009): 6827–30. http://dx.doi.org/10.1128/aem.01555-09.

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ABSTRACT Some protozoans are able to encyst as a protective response to a harmful environment. The cyst wall usually contains chitin as its main structural constituent. Acanthamoeba is an exception since its cyst wall contains cellulose. Specific cytochemical differentiation between cellulose and chitin by microscopy has not been possible due to the similarity of the constituent β-1,4-linked hexose backbones of these molecules. Thus, various fluorescent brightening agents and lectins bind to both cellulose and chitin. The identification of Acanthamoeba spp., which is based primarily on morphol

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DAS, ARPAN, TANMAY PAUL, SUMAN KUMAR HALDER, CHIRANJIT MAITY, PRADEEP KUMAR DAS MOHAPATRA, BIKASH RANJAN PATI, and KESHAB CHANDRA MONDAL. "Study on Regulation of Growth and Biosynthesis of Cellulolytic Enzymes from Newly Isolated Aspergillus fumigatus ABK9." Polish Journal of Microbiology 62, no. 1 (2013): 31–43. http://dx.doi.org/10.33073/pjm-2013-004.

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This study was aimed to evaluate the pattern of cellulase biosynthesis from Aspergillusfumigatus ABK9 under submerged fermentation. Production was increased concomitantly with fungal growth up to 72 h and reached maximum (Xmax -6.72 g/l) with specific growth rate (mu max) of 0.126/h. Highest specific rate of enzyme production (q ) was found at initial medium pH of 5.0 and incubation temperature of 30 degrees C. At the same time, in the presence of 2-deoxy-D-glucose concentration of 0.5 mg/ml, the production of cellulolytic enzymes, viz, carboxymethyl cellulase activity (CMCase), filter paper d

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Wen, Fei, Jie Sun, and Huimin Zhao. "Yeast Surface Display of Trifunctional Minicellulosomes for Simultaneous Saccharification and Fermentation of Cellulose to Ethanol." Applied and Environmental Microbiology 76, no. 4 (December 18, 2009): 1251–60. http://dx.doi.org/10.1128/aem.01687-09.

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ABSTRACT By combining cellulase production, cellulose hydrolysis, and sugar fermentation into a single step, consolidated bioprocessing (CBP) represents a promising technology for biofuel production. Here we report engineering of Saccharomyces cerevisiae strains displaying a series of uni-, bi-, and trifunctional minicellulosomes. These minicellulosomes consist of (i) a miniscaffoldin containing a cellulose-binding domain and three cohesin modules, which was tethered to the cell surface through the yeast a-agglutinin adhesion receptor, and (ii) up to three types of cellulases, an endoglucanase

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Patel, Milind A., Mark S. Ou, Roberta Harbrucker, Henry C. Aldrich, Marian L. Buszko, Lonnie O. Ingram, and K. T. Shanmugam. "Isolation and Characterization of Acid-Tolerant, Thermophilic Bacteria for Effective Fermentation of Biomass-Derived Sugars to Lactic Acid." Applied and Environmental Microbiology 72, no. 5 (May 2006): 3228–35. http://dx.doi.org/10.1128/aem.72.5.3228-3235.2006.

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ABSTRACT Biomass-derived sugars, such as glucose, xylose, and other minor sugars, can be readily fermented to fuel ethanol and commodity chemicals by the appropriate microbes. Due to the differences in the optimum conditions for the activity of the fungal cellulases that are required for depolymerization of cellulose to fermentable sugars and the growth and fermentation characteristics of the current industrial microbes, simultaneous saccharification and fermentation (SSF) of cellulose is envisioned at conditions that are not optimal for the fungal cellulase activity, leading to a higher-than-

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Doud, Devin F. R., Robert M. Bowers, Frederik Schulz, Markus De Raad, Kai Deng, Angela Tarver, Evan Glasgow, et al. "Function-driven single-cell genomics uncovers cellulose-degrading bacteria from the rare biosphere." ISME Journal 14, no. 3 (November 21, 2019): 659–75. http://dx.doi.org/10.1038/s41396-019-0557-y.

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AbstractAssigning a functional role to a microorganism has historically relied on cultivation of isolates or detection of environmental genome-based biomarkers using a posteriori knowledge of function. However, the emerging field of function-driven single-cell genomics aims to expand this paradigm by identifying and capturing individual microbes based on their in situ functions or traits. To identify and characterize yet uncultivated microbial taxa involved in cellulose degradation, we developed and benchmarked a function-driven single-cell screen, which we applied to a microbial community inh

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Chen, Xin-ai, Nobuhiro Ishida, Nemuri Todaka, Risa Nakamura, Jun-ichi Maruyama, Haruo Takahashi, and Katsuhiko Kitamoto. "Promotion of Efficient Saccharification of Crystalline Cellulose by Aspergillus fumigatus Swo1." Applied and Environmental Microbiology 76, no. 8 (February 19, 2010): 2556–61. http://dx.doi.org/10.1128/aem.02499-09.

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ABSTRACT Swollenin is a protein from Trichoderma reesei that has a unique activity for disrupting cellulosic materials, and it has sequence similarity to expansins, plant cell wall proteins that have a loosening effect that leads to cell wall enlargement. In this study we cloned a gene encoding a swollenin-like protein, Swo1, from the filamentous fungus Aspergillus fumigatus, and designated the gene Afswo1. AfSwo1 has a bimodular structure composed of a carbohydrate-binding module family 1 (CBM1) domain and a plant expansin-like domain. AfSwo1 was produced using Aspergillus oryzae for heterolo

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Gold, Nicholas D., and Vincent J. J. Martin. "Global View of the Clostridium thermocellum Cellulosome Revealed by Quantitative Proteomic Analysis." Journal of Bacteriology 189, no. 19 (July 20, 2007): 6787–95. http://dx.doi.org/10.1128/jb.00882-07.

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ABSTRACT A metabolic isotope-labeling strategy was used in conjunction with nano-liquid chromatography-electrospray ionization mass spectrometry peptide sequencing to assess quantitative alterations in the expression patterns of subunits within cellulosomes of the cellulolytic bacterium Clostridium thermocellum, grown on either cellulose or cellobiose. In total, 41 cellulosomal proteins were detected, including 36 type I dockerin-containing proteins, which count among them all but three of the known docking components and 16 new subunits. All differential expression data were normalized to the

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Lochner, Adriane, Richard J. Giannone, Miguel Rodriguez, Manesh B. Shah, Jonathan R. Mielenz, Martin Keller, Garabed Antranikian, David E. Graham, and Robert L. Hettich. "Use of Label-Free Quantitative Proteomics To Distinguish the Secreted Cellulolytic Systems of Caldicellulosiruptor bescii and Caldicellulosiruptor obsidiansis." Applied and Environmental Microbiology 77, no. 12 (April 15, 2011): 4042–54. http://dx.doi.org/10.1128/aem.02811-10.

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ABSTRACTThe extremely thermophilic, Gram-positive bacteriaCaldicellulosiruptor besciiandCaldicellulosiruptor obsidiansisefficiently degrade both cellulose and hemicellulose, which makes them relevant models for lignocellulosic biomass deconstruction to produce sustainable biofuels. To identify the shared and unique features of secreted cellulolytic apparatuses fromC. besciiandC. obsidiansis, label-free quantitative proteomics was used to analyze protein abundance over the course of fermentative growth on crystalline cellulose. Both organisms' secretomes consisted of more than 400 proteins, of

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Cann, Isaac K. O., Svetlana Kocherginskaya, Michael R. King, Bryan A. White, and Roderick I. Mackie. "Molecular Cloning, Sequencing, and Expression of a Novel Multidomain Mannanase Gene from Thermoanaerobacterium polysaccharolyticum." Journal of Bacteriology 181, no. 5 (March 1, 1999): 1643–51. http://dx.doi.org/10.1128/jb.181.5.1643-1651.1999.

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ABSTRACT The manA gene of Thermoanaerobacterium polysaccharolyticum was cloned in Escherichia coli. The open reading frame of manA is composed of 3,291 bases and codes for a preprotein of 1,097 amino acids with an estimated molecular mass of 119,627 Da. The start codon is preceded by a strong putative ribosome binding site (TAAGGCGGTG) and a putative −35 (TTCGC) and −10 (TAAAAT) promoter sequence. The ManA of T. polysaccharolyticum is a modular protein. Sequence comparison and biochemical analyses demonstrate the presence of an N-terminal leader peptide, and three other domains in the followin

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OGAWA, KIHACHIRO, DAISUKE TOYAMA, and NOBORU FUJII. "Microcrystalline cellulose-hydrolyzing cellulase (endo-cellulase) from Trichoderma reesei CDU-11." Journal of General and Applied Microbiology 37, no. 3 (1991): 249–59. http://dx.doi.org/10.2323/jgam.37.249.

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Chérif, Mohamed, Nicole Benhamou, and Richard R. Bélanger. "Occurrence of cellulose and chitin in the hyphal walls of Pythium ultimum: a comparative study with other plant pathogenic fungi." Canadian Journal of Microbiology 39, no. 2 (February 1, 1993): 213–22. http://dx.doi.org/10.1139/m93-030.

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Exoglucanase, a β-1, 4-glucan cellobiohydrolase with specific affinity for β-1, 4-linked glucans, and wheat germ agglutinin, a lectin with N-acetylglucosamine-binding specifity, were used for localizing cellulosic β-1, 4-glucans and chitin in the cell walls of six plant pathogenic fungi. Both chitin and cellulose were found to occur in the cell walls of the oomycete fungus Pythium ultimum whereas only cellulose was present in those of Phythophthora parasitica var. nicotianae, another oomycete fungus. The two compounds were also simultaneously detected in the cell walls of two ascomycetes, Ophi

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VIJAYARAGHAVAN, PONNUSWAMY, and S. G. PRAKASH VINCENT. "Purification and Characterization of Carboxymethyl Cellulase from Bacillus sp. Isolated from a Paddy Field." Polish Journal of Microbiology 61, no. 1 (2012): 51–55. http://dx.doi.org/10.33073/pjm-2012-006.

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A microorganism hydrolyzing carboxymethyl cellulose was isolated from a paddy field and identified as Bacillus sp. Production of cellulase by this bacterium was found to be optimal at pH 6.5, 37 degrees C and 150 rpm of shaking. This cellulase was purified to homogeneity by the combination of ammonium sulphate precipitation, DEAE cellulose, and sephadex G-75 gel filtration chromatography. The cellulase was purified up to 14.5 fold and had a specific activity of 246 U/mg protein. The enzyme was a monomeric cellulase with a relative molecular mass of 58 kDa, as determined by SDS-PAGE. The enzyme

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Park, Yoen Ju, and Jinru Chen. "Inactivation of Shiga Toxin-Producing Escherichia coli (STEC) and Degradation and Removal of Cellulose from STEC Surfaces by Using Selected Enzymatic and Chemical Treatments." Applied and Environmental Microbiology 77, no. 24 (October 14, 2011): 8532–37. http://dx.doi.org/10.1128/aem.06450-11.

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ABSTRACTSome Shiga toxin-producingEscherichia coli(STEC) strains produce extracellular cellulose, a long polymer of glucose with β-1-4 glycosidic bonds. This study evaluated the efficacies of selected enzymatic and chemical treatments in inactivating STEC and degrading/removing the cellulose on STEC surfaces. Six cellulose-producing STEC strains were treated with cellulase (0.51 to 3.83 U/15 ml), acetic and lactic acids (2 and 4%), as well as an acidic and alkaline sanitizer (manufacturers' recommended concentrations) under appropriate conditions. Following each treatment, residual amounts of

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Gilad, Rachel, Larisa Rabinovich, Sima Yaron, Edward A. Bayer, Raphael Lamed, Harry J. Gilbert, and Yuval Shoham. "CelI, a Noncellulosomal Family 9 Enzyme from Clostridium thermocellum, Is a Processive Endoglucanase That Degrades Crystalline Cellulose." Journal of Bacteriology 185, no. 2 (January 15, 2003): 391–98. http://dx.doi.org/10.1128/jb.185.2.391-398.2003.

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ABSTRACT The family 9 cellulase gene celI of Clostridium thermocellum, was previously cloned, expressed, and characterized (G. P. Hazlewood, K. Davidson, J. I. Laurie, N. S. Huskisson, and H. J. Gilbert, J. Gen. Microbiol. 139:307-316, 1993). We have recloned and sequenced the entire celI gene and found that the published sequence contained a 53-bp deletion that generated a frameshift mutation, resulting in a truncated and modified C-terminal segment of the protein. The enzymatic properties of the wild-type protein were characterized and found to conform to those of other family 9 glycoside hy

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Jun, Hyun-Sik, Meng Qi, Joshua Gong, Emmanuel E. Egbosimba, and Cecil W. Forsberg. "Outer Membrane Proteins of Fibrobacter succinogenes with Potential Roles in Adhesion to Cellulose and in Cellulose Digestion." Journal of Bacteriology 189, no. 19 (July 20, 2007): 6806–15. http://dx.doi.org/10.1128/jb.00560-07.

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ABSTRACT Comparative analysis of binding of intact glucose-grown Fibrobacter succinogenes strain S85 cells and adhesion-defective mutants AD1 and AD4 to crystalline and acid-swollen (amorphous) cellulose showed that strain S85 bound efficiently to both forms of cellulose while mutant Ad1 bound to acid-swollen cellulose, but not to crystalline cellulose, and mutant Ad4 did not bind to either. One- and two-dimensional electrophoresis (2-DE) of outer membrane cellulose binding proteins and of outer membranes, respectively, of strain S85 and adhesion-defective mutant strains in conjunction with ma

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Woodward, Jonathan. "Immobilized cellulases for cellulose utilization." Journal of Biotechnology 11, no. 4 (September 1989): 299–311. http://dx.doi.org/10.1016/0168-1656(89)90015-1.

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Qi, Meng, Hyun-Sik Jun та Cecil W. Forsberg. "Cel9D, an Atypical 1,4-β-d-Glucan Glucohydrolase from Fibrobacter succinogenes: Characteristics, Catalytic Residues, and Synergistic Interactions with Other Cellulases". Journal of Bacteriology 190, № 6 (18 січня 2008): 1976–84. http://dx.doi.org/10.1128/jb.01667-07.

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ABSTRACT The increasing demands of renewable energy have led to the critical emphasis on novel enzymes to enhance cellulose biodegradation for biomass conversion. To identify new cellulases in the ruminal bacterium Fibrobacter succinogenes, a cell extract of cellulose-grown cells was separated by ion-exchange chromatography and cellulases were located by zymogram analysis and identified by peptide mass fingerprinting. An atypical family 9 glycoside hydrolase (GH9), Cel9D, with less than 20% identity to typical GH9 cellulases, was identified. Purified recombinant Cel9D enhanced the production o

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