Identification and evolution of the cellulolytic microflora present during composting of cattle manure: On the role of actinomycetes sp

Godden, Bernard; Penninckx, Michel

doi:10.1016/s0769-2609(84)80044-7

Cited by 30 publications

(12 citation statements)

References 12 publications

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“…In one study, cellulolytic activity and the production of 14 CO 2 from [ 14 C]cellulose decreased with soil depth (711), suggesting that cellulose utilization is largely an aerobic process, and the primary cellulolytic bacterial isolates were Cytophaga species, although Bacillus and Cellulomonas strains were also isolated. In composting cattle manure, filamentous bacteria from the genera Micromonospora, Cytophaga, and Sporocytophaga were the most numerically abundant isolates and fungi were much less abundant (215). As in any isolation study, the identity of uncultured species and their contribution to the biological process under study were unclear.…”

Section: Ecological Aspects Of Cellulose-degrading Communitiesmentioning

confidence: 94%

Microbial Cellulose Utilization: Fundamentals and Biotechnology

Lynd

Weimer

Zyl³

et al. 2002

Microbiol Mol Biol Rev

4,047

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: Ecological Aspects Of Cellulose-degrading Communitiesmentioning

confidence: 94%

Microbial Cellulose Utilization: Fundamentals and Biotechnology

Lynd

Weimer

Zyl³

et al. 2002

Microbiol Mol Biol Rev

4,047

2,868

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“…Database BLAST searches using the C-terminal domains identified in this study revealed similarities with the C-terminal domains of numerous predicted proteins of other members of the Bacteroidetes. These species include Rhodothermus marinus (25), Cytophaga hutchinsonii (19), a Microscilla species, (16), Zobellia galactanovorans (8), Flavobacterium columnare, and Prevotella intermedia, a species that is also found in subgingival dental plaque. Interestingly, C-terminal-domain similarity can also be found with predicted proteins of the photosynthetic sulfur bacterium Chlorobium phaeobacteroides, showing that the CTD family is not limited to the phylum Bacteroidetes.…”

Section: Discussionmentioning

confidence: 99%

The RgpB C-Terminal Domain Has a Role in Attachment of RgpB to the Outer Membrane and Belongs to a Novel C-Terminal-Domain Family Found in Porphyromonas gingivalis

et al. 2006

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Porphyromonas gingivalis produces outer membrane-attached proteins that include the virulence-associated proteinases RgpA and RgpB (Arg-gingipains) and Kgp (Lys-gingipain). We analyzed the P. gingivalis outer membrane proteome and identified numerous proteins with C-terminal domains similar in sequence to those of RgpB, RgpA, and Kgp, indicating that these domains may have a common function. Using RgpB as a model to investigate the role of the C-terminal domain, we expressed RgpB as a full-length zymogen (recombinant RgpB [rRgpB]), with a catalytic Cys244Ala mutation [rRgpB(C244A)], or with the C-terminal 72 amino acids deleted (rRgpB435) in an Arg-gingipain P. gingivalis mutant (YH522AB) and an Arg-and Lys-gingipain mutant (YH522KAB). rRgpB was catalytically active and located predominantly attached to the outer membrane of both background strains. rRgpB(C244A) was inactive and outer membrane attached, with a typical attachment profile for both background strains according to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, but in YH522KAB, the prodomain was not removed. Thus, in vivo, RgpB export and membrane attachment are independent of the proteolytic activity of RgpA, RgpB, or Kgp. However, for maturation involving proteolytic processing of RgpB, the proteolytic activity of RgpB, RgpA, or Kgp is required. The C-terminally-truncated rRgpB435 was not attached to the outer membrane and was located as largely inactive, discrete 71-kDa and 48-kDa isoforms in the culture supernatant and the periplasm. These results suggest that the C-terminal domain is essential for outer membrane attachment and may be involved in a coordinated process of export and attachment to the cell surface.Porphyromonas gingivalis is a gram-negative anaerobe that is found predominantly in subgingival dental plaques associated with the destruction of the tooth's supporting tissues (14, 52; for reviews, see references 24, 26, and 32). P. gingivalis produces three major cysteine proteinases (gingipains), two of which, RgpA cat and RgpB (which are almost identical in sequence), are specific for Arg-Xaa cleavage (39, 49, 51) and one of which, Kgp cat , is specific for Lys-Xaa cleavage (34,38,50). The proteinases are encoded by rgpA, rgpB, and kgp and are produced as zymogens with a Sec-type leader peptide followed by a prodomain, the catalytic domain, and, in the cases of RgpA and Kgp, several sequence-related adhesin domains (50). The RgpA polyprotein is proteolytically processed to produce RgpA cat and several adhesins that are designated RgpA A1 , RgpA A2 , RgpA A3 , and RgpA A4 , while the Kgp polyprotein is processed to produce Kgp cat and the adhesins Kgp A1 , Kgp A2 , Kgp A3 , Kgp A4 , and Kgp A5 (32). The RgpA and Kgp proteinase and adhesin domains occur together as a surface-associated complex (32, 50), with relatively little of the complex found free in the extracellular milieu.RgpB is produced as a 736-amino-acid (aa) precursor with a Sec-type signal sequence that is predicted to be cleaved after Ala 24 and a prodomain cle...

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“…strain EC10 was isolated from cattle manure compost (Godden and Penninckx 1984). strain EC10 was isolated from cattle manure compost (Godden and Penninckx 1984).…”

Section: Organisms and Culture Conditionsmentioning

confidence: 99%

“…This strain, previously isolated from cattle manure compost (Godden and Penninckx 1984) and selected in a straw saccharification test (Ball and McCarthy 1988), degraded efficiently the hemicellulose fraction of straw (Godden et al 1989) and was expected to be good candidate for enzyme production. This strain, previously isolated from cattle manure compost (Godden and Penninckx 1984) and selected in a straw saccharification test (Ball and McCarthy 1988), degraded efficiently the hemicellulose fraction of straw (Godden et al 1989) and was expected to be good candidate for enzyme production.…”

Section: Introductionmentioning

confidence: 99%

Characterization of the multiple forms of ?-xylanase produced by a Streptomyces sp. growing on lignocellulose

Lumba

Penninckx

1992

Appl Microbiol Biotechnol

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Streptomyces sp. strain EC10 degraded efficiently the hemicellulose fraction of wheat straw. Three forms of fl-xylanases detected in the culture filtrate were purified by precipitation with a m m o n i u m sulphate, chromatography on DEAE-Sephadex A-50 and gel filtration on Sephadex G-100. The three purified enzymes (X~A, Xm and X'~) were homogeneous by polyacrylamide gel electrophoresis. The enzymes were typical non-debranching endo-fl-xylanases (1,4-fl-D-xylan xylanohydrolases; E.C.3.2.1.8) with respective relative molecular weights of 32,000, 22,000 and 21,000 and isoelectric points of 6.8, 8.9 and 5°2. The enzymes were highly specific for xylans and showed optimal activity at p H 7.0-8.0 and 60 ° C. The preparations were completely free from cellulolytic activity (endoglucanase) and showed high thermal stability. No synergy between the three enzymes was detected for complete xylan hydrolysis of deacetylated arabino-and glucuronoxylans.

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Identification and evolution of the cellulolytic microflora present during composting of cattle manure: On the role of actinomycetes sp

Cited by 30 publications

References 12 publications

Microbial Cellulose Utilization: Fundamentals and Biotechnology

Microbial Cellulose Utilization: Fundamentals and Biotechnology

The RgpB C-Terminal Domain Has a Role in Attachment of RgpB to the Outer Membrane and Belongs to a Novel C-Terminal-Domain Family Found in Porphyromonas gingivalis

Characterization of the multiple forms of ?-xylanase produced by a Streptomyces sp. growing on lignocellulose

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