Evidence map›Paper›PMID 11004164›Full record

ArticleJournal of bacteriology2000

Synergistic hydrolysis of carboxymethyl cellulose and acid-swollen cellulose by two endoglucanases (CelZ and CelY) from Erwinia chrysanthemi.

S Zhou, L O Ingram

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.6field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 92 citations in OpenAlex.

  1. EngineeringFrontiers in bioengineering and biotechnology · 2026
    Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Characteristics of a β-1,4-D endoglucanase from Trichoderma virens wholly applied in a palm-fruit husk-based diet for poultry layers.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2012
    Article
  11. Article
  12. Article
  13. Article
  14. Fungal biodegradation and enzymatic modification of lignin.International journal of biochemistry and molecular biology · 2010
    Article
  15. Review
  16. Synthetic biology and biomass conversion: a match made in heaven?Journal of the Royal Society, Interface · 2009
    Review
  17. Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives.Journal of industrial microbiology & biotechnology · 2008
    Review
  18. Microbial cellulose utilization: fundamentals and biotechnology.Microbiology and molecular biology reviews : MMBR · 2002
    Review
  19. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

S ZhouInstitute of Food and Agricultural Sciences, Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida 32611, USA.
L O Ingram
University of Florida · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Erwinia chrysanthemi produces a battery of hydrolases and lyases which are very effective in the maceration of plant cell walls. Although two endoglucanases (CelZ and CelY; formerly EGZ and EGY) are produced, CelZ represents approximately 95% of the total carboxymethyl cellulase activity. In this study, we have examined the effectiveness of CelY and CelZ alone and of combinations of both enzymes using carboxymethyl cellulose (CMC) and amorphous cellulose (acid-swollen cellulose) as substrates. Synergy was observed with both substrates. Maximal synergy (1.8-fold) was observed for combinations containing primarily CelZ; the ratio of enzyme activities produced was similar to those produced by cultures of E. chrysanthemi. CelY and CelZ were quite different in substrate preference. CelY was unable to hydrolyze soluble cellooligosaccharides (cellotetraose and cellopentaose) but hydrolyzed CMC to fragments averaging 10.7 glucosyl units. In contrast, CelZ readily hydrolyzed cellotetraose, cellopentaose, and amorphous cellulose to produce cellobiose and cellotriose as dominant products. CelZ hydrolyzed CMC to fragments averaging 3.6 glucosyl units. In combination, CelZ and CelY hydrolyzed CMC to products averaging 2.3 glucosyl units. Synergy did not require the simultaneous presence of both enzymes. Enzymatic modification of the substrate by CelY increased the rate and extent of hydrolysis by CelZ. Full synergy was retained by the sequential hydrolysis of CMC, provided CelY was used as the first enzyme. A general mechanism is proposed to explain the synergy between these two enzymes based primarily on differences in substrate preference.

Indexed as

Carbohydrate ConformationCarbohydrate SequenceCarboxymethylcellulose SodiumCellulaseCelluloseCellulose 1,4-beta-CellobiosidaseCloning, MolecularDickeya chrysanthemiGlycoside HydrolasesHydrogen-Ion ConcentrationHydrolysisKineticsMolecular Sequence DataOligosaccharidesRecombinant ProteinsSubstrate SpecificitycarboxymethylcellulaseCarboxymethylcellulose SodiumCellulaseCelluloseCellulose 1,4-beta-Cellobiosidaseendoglucanase ZGlycoside HydrolasesOligosaccharidesRecombinant Proteins

Identifiers

PMID11004164
PMCPMC94687
OpenAlexW2104454698

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.