Chi18A, the Endochitinase in the Cellulosome of the Thermophilic, Cellulolytic Bacterium
            <i>Clostridium thermocellum</i>

Zverlov, Vladimir V.; Fuchs, Klaus-Peter; Schwarz, Wolfgang H.

doi:10.1128/aem.68.6.3176-3179.2002

Cited by 53 publications

(33 citation statements)

References 29 publications

(30 reference statements)

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“…The xylanases are members of family 11 of glycosyl hydrolases, and mannanase is a member of family 5. A pectate lyase of family 9 has been observed in cellulosomes (63), and these A cellulosomal chitinase has been reported for C. thermocellum (67). This suggests the possibility that cellulosomes not only degrade lignocelluloses, but also degrade chitin, which occurs in fungi and which comprises the exoskeleton of many insects.…”

Section: Hemicellulases and Other Enzymesmentioning

confidence: 79%

Cellulosomes from Mesophilic Bacteria

et al. 2003

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Section: Hemicellulases and Other Enzymesmentioning

confidence: 79%

Cellulosomes from Mesophilic Bacteria

et al. 2003

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“…T and F7 (Schimming et al, 1992;Zverlov et al, 2002), two xylanase genes in strains ATCC 27405 and F1 (>99?3 %), cellobiose phosphorylase Cbp in strains YM4 and F1 (99?6 %) and CelK in strains F7 and YW20 (99?8 %), which contain only a few differences. Thus the C. thermocellum strains isolated in the Northern hemisphere seem to be quite homogeneous, as was also suggested from the physiological characteristics of different isolates (McBee, 1954).…”

Section: Discussionmentioning

confidence: 99%

Lic16A of Clostridium thermocellum, a non-cellulosomal, highly complex endo-β-1,3-glucanase bound to the outer cell surface

Fuchs¹,

Zverlov

Velikodvorskaya

et al. 2003

Microbiology

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Clostridium thermocellum produces one major b-1,3-glucanase. Genomic DNA fragments containing the gene were cloned from two strains, DSM1237T (6848 bp) and F7 (9766 bp).Overlapping sequences were 99?9 % identical. The nucleotide sequences contained reading frames for a putative transposase, endo-b-1,3-1,4-glucanase CelC, a putative transcription regulator of the LacI type, b-1,3-glucanase Lic16A and a putative membrane protein. The licA genes of both strains encoded an identical protein of 1324 aa with a calculated molecular mass of 148 kDa. Lic16A is an unusually complex protein consisting of a leader peptide, a threefold repeat of an S-layer homologous module (SLH), an unknown module, a catalytic module of glycosyl hydrolase family 16 and a fourfold repeat of a carbohydrate-binding module of family CBM4a. The recombinant Lic16A protein was characterized as an endo-1,3(4)-b-glucanase with a specific activity of 2680 and 340 U mg 21 and a K m of 0?94 and 2?1 mg ml 21 towards barley b-glucan and laminarin, respectively. It was specific for b-glucans containing b-1,3-linkages with an optimum temperature of 70˚C at pH 6?0. The N-terminal SLH modules were cleaved from the protein as well in Escherichia coli as in C. thermocellum, but nevertheless bound tightly to the rest of the protein. Lic16A was located on the cell surface from which it could be purified after fractionated solubilization. Its inducible production allowed C. thermocellum to grow on b-1,3-or b-1,3-1,4-glucan.

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“…As described below, our data indicate that the LacI-like protein regulates the expression of the gene cluster by binding to the promoter region. The fourth gene cluster consists of celA, chiA, and orfZ (366). CelA is a noncellulosomal endoglucanase.…”

Section: Cellulase Gene Clustersmentioning

confidence: 99%

Cellulase, Clostridia, and Ethanol

Demain

Newcomb

2005

Microbiol Mol Biol Rev

804

579

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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), the binding of the cellulosomes to cellulose and to the cell surface, cellulase genetics, regulation of their synthesis, cocultures, ethanol tolerance, and metabolic pathway engineering for maximizing ethanol yield.

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Chi18A, the Endochitinase in the Cellulosome of the Thermophilic, Cellulolytic Bacterium Clostridium thermocellum

Cited by 53 publications

References 29 publications

Cellulosomes from Mesophilic Bacteria

Cellulosomes from Mesophilic Bacteria

Lic16A of Clostridium thermocellum, a non-cellulosomal, highly complex endo-β-1,3-glucanase bound to the outer cell surface

Cellulase, Clostridia, and Ethanol

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