A Large Gene Cluster for the
            <i>Clostridium cellulovorans</i>
            Cellulosome

Tamaru, Yutaka; Karita, Shuichi; Ibrahim, Atef M.; Chan, Helen M.; Doi, Roy H.

doi:10.1128/jb.182.20.5906-5910.2000

Cited by 94 publications

(75 citation statements)

References 21 publications

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“…However, C. cellulovorans grown on cellobiose and CMC does exhibit a high cellulase activity and transcription of cellulase genes. This suggests that cellulases may be produced on certain soluble carbohydrates, such as cellobiose, but that (poly)cellulosome assembly and detachment from the cell wall need some "triggering" from the presence of insoluble microcrystalline cellulose (60,166,665). Analysis of mRNA transcripts in the ruminal bacterium R. flavefaciens FD-1 has revealed somewhat contradictory results.…”

Section: Molecular Biology Of Cellulase Enzymesmentioning

confidence: 94%

“…C. cellulovorans and C. acetobutylicum belong to group I within the Clostridiaceae and are more distant from C. thermocellum and C. cellulolyticum; however, the cellulosome components of C. cellulovorans are surprisingly similar to those of C. cellulolyticum. The cellulosome genes of these clostridia are clustered, and Tamaru et al (665) suggested that C. cellulovorans could have acquired its cellulosome gene cluster through horizontal gene transfer from a common ancestor. The cellulosome of C. cellulolyticum is the best understood among mesophilic clostridia and is discussed as a model system here (43).…”

Section: Cellulase Enzyme Systemsmentioning

confidence: 99%

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Microbial Cellulose Utilization: Fundamentals and Biotechnology

Lynd

Weimer

Zyl³

et al. 2002

Microbiol Mol Biol Rev

4,014

2,868

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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 and analysis for cellulose-grown continuous cultures. Quantitative description of cellulose hydrolysis is addressed with respect to adsorption of cellulase enzymes, rates of enzymatic hydrolysis, bioenergetics of microbial cellulose utilization, kinetics of microbial cellulose utilization, and contrasting features compared to soluble substrate kinetics. A biological perspective on processing cellulosic biomass is presented, including features of pretreated substrates and alternative process configurations. Organism development is considered for “consolidated bioprocessing” (CBP), in which the production of cellulolytic enzymes, hydrolysis of biomass, and fermentation of resulting sugars to desired products occur in one step. Two organism development strategies for CBP are examined: (i) improve product yield and tolerance in microorganisms able to utilize cellulose, or (ii) express a heterologous system for cellulose hydrolysis and utilization in microorganisms that exhibit high product yield and tolerance. A concluding discussion identifies unresolved issues pertaining to microbial cellulose utilization, suggests approaches by which such issues might be resolved, and contrasts a microbially oriented cellulose hydrolysis paradigm to the more conventional enzymatically oriented paradigm in both fundamental and applied contexts

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Section: Molecular Biology Of Cellulase Enzymesmentioning

confidence: 94%

Section: Cellulase Enzyme Systemsmentioning

confidence: 99%

Microbial Cellulose Utilization: Fundamentals and Biotechnology

Lynd

Weimer

Zyl³

et al. 2002

Microbiol Mol Biol Rev

4,014

2,868

View full text Add to dashboard Cite

show abstract

“…This domain is non-catalytic by nature, but it plays a significant role in the enzymatic activity of the cellulosomal enzymes. The binding of CBM with the cellulosic substrate nullifies the hydrogen bonding and brings the cellulosomal enzymes close to the cellulose, thus making the breakdown more efficient compared to the free enzymes (Lynd et al 2002;Tamaru et al 2000;Caspi et al 2008).…”

Section: Carbohydrate-binding Modulementioning

confidence: 99%

“…The anchoring of cellulosome to the cell surface is made by surface layer homology (SLH) domain through Tamaru et al 2000). The SLH forms a protein layer outside of the cell wall, which is highly conserved in the cellulosomal bacteria (Desvaux et al 2006).…”

Section: Surface Layer Homology Domainmentioning

confidence: 99%

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Bioprospecting thermostable cellulosomes for efficient biofuel production from lignocellulosic biomass

Arora

Behera

Sharma

et al. 2015

Bioresour. Bioprocess.

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The adverse climatic conditions due to continuous use of fossil-derived fuels are the driving factors for the development of renewable sources of energy. Current biofuel research focuses mainly on lignocellulosic biomass (LCB) such as agricultural, industrial and municipal solid wastes due to their abundance and renewability. Although many mesophilic cellulolytic microorganisms have been reported, efficient and economical bioconversion to simple sugars is still a challenge. Thermostable cellulolytic enzymes play an indispensible role in degradation of the complex polymeric structure of LCB into fermentable sugar stream due to their higher flexibility with respect to process configurations and better specific activity than the mesophilic enzymes. In some anaerobic thermophilic/thermotolerant microorganisms, few cellulases are organized as unique multifunctional enzyme complex, called the cellulosome. The use of cellulosomal multienzyme complexes for saccharification seems to be a promising and cost-effective alternative for complete breakdown of cellulosic biomass. This paper aims to explore and review the important findings in cellulosomics and forward the path for new cutting-edge opportunities in the success of biorefineries. Herein, we summarize the protein structure, regulatory mechanisms and their expression in the host cells. Furthermore, we discuss the recent advances in specific strategies used to design new multifunctional cellulosomal enzymes, which can function as lignocellulosic biocatalysts and evaluate the roadblocks in the yield and stability of such designer thermozymes with overall progress in lignocellulose-based biorefinery.

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Solubilization of cellulosomal cellulases by fusion with cellulose‐binding domain of noncellulosomal cellulase engd from Clostridium cellulovorans

2003

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Clostridium cellulovorans produces a cellulase complex (cellulosome) as well as noncellulosomal cellulases. In this study, we determined a factor that affected the solubility of the cellulosomal cellulase EngB and the noncellulosomal EngD when they were expressed in Escherichia coli. The catalytic domains of EngB and EngD formed inclusion bodies when expressed in E. coli. On the other hand, both catalytic domains containing the C-terminal cellulose-binding domain (CBD) of EngD were expressed in soluble form. Fusion with the CBD of EngD also helped increased the solubility of cellulosomal cellulase EngL upon expression in E. coli. These results indicate that the CBD of EngD plays an important role in the soluble expression of the catalytic domains of EngB, EngL, and EngD. The possible mechanisms of solubilization by fusion of the catalytic domain with the CBD from EngD are discussed.

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A Large Gene Cluster for the Clostridium cellulovorans Cellulosome

Cited by 94 publications

References 21 publications

Microbial Cellulose Utilization: Fundamentals and Biotechnology

Microbial Cellulose Utilization: Fundamentals and Biotechnology

Bioprospecting thermostable cellulosomes for efficient biofuel production from lignocellulosic biomass

Solubilization of cellulosomal cellulases by fusion with cellulose‐binding domain of noncellulosomal cellulase engd from Clostridium cellulovorans

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