Evidence map›Paper›PMID 9020869›Full record

ArticleThe Biochemical journal1997

The beta-D-xylosidase of Trichoderma reesei is a multifunctional beta-D-xylan xylohydrolase.

M C Herrmann, M Vrsanska, M Jurickova, J Hirsch, P Biely, C P Kubicek

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.7field-weighted citation impact, top 19% 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

33 citing papers in PubMed, 103 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Non-Specific GH30_7 Endo-β-1,4-xylanase fromMolecules (Basel, Switzerland) · 2021
    Article
  6. Article
  7. Review
  8. The Change in the Composition ofMicrobiology insights · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

6 authors at 3 institutions in 2 countries.

M C HerrmannSection Microbial Biochemistry, Institute of Biochemical Technology and Microbiology, Wien, Austria.
M Vrsanska
M Jurickova
J Hirsch
P Biely
C P Kubicek
Slovak Academy of Sciences · SKInstitute of Chemistry of the Slovak Academy of Sciences · SKTU Wien · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An extracellular multifunctional beta-D-xylan xylohydrolase, previously described as beta-xylosidase, was purified from Trichoderma reesei RUT C-30 to physical homogeneity. The active enzyme was a 100 (+/-5) kDa glycosylated monomer that exhibited a pl of 4.7. Its activity was optimal at pH 4 and it was stable between pH 3 and 6. Its temperature-stability was moderate (70 degrees zero of activity remaining after 60 min at 50 degrees C) and optimal activity was observed at 60 degrees C. It is capable of hydrolysing beta-1.4-xylo-oligosaccharides [degree of polymerization (DP) 2-7], the apparent Vmax increasing with increasing chain length. The enzyme also attacked debranched beech-wood (Lenzing) xylan and 4-O-methylglucuronoxylan, forming xylose as the only end product. The K(m) for xylan was 0.7 g/l. For this reason we consider the enzyme to be a beta-D-xylan xylohydrolase. The enzyme also exhibits alpha-L-arabinofuranosidase activity on 4-nitrophenyl alpha-L-arabinofuranoside, and evidence is presented that this is not caused by an impurity in the enzyme preparation. The beta-D-xylan xylohydrolase exhibits glycosyltransferase activity with xylo-oligosaccharides and at high concentrations of 4-nitrophenyl beta-D-xylopyranoside (4-Nph-beta-Xyl). The enzyme hydrolyses beta-1, 4-linkages preferentially to beta-1,3-linkages, and beta-1,2-linked xylo-oligosaccharides are not hydrolysed at all. The enzyme liberates terminal beta-1,4-xylopyranose residues linked to a 2-O-substituted xylopyranose residue, but not that linked to a 3-O-substituted xylopyranose residue. The enzyme does not attack methyl, methyl 1-thio-benzyl or butyl l-thio-beta-D-xylopyranosides and 4-naphthyl, 2-naphthyl and phenyl beta-D-xylopyranosides.

Indexed as

Amino Acid SequenceCarbohydrate SequenceChemical PhenomenaChemistry, PhysicalFungal ProteinsGlycosylationMolecular Sequence DataMultienzyme ComplexesSubstrate SpecificityTreesTrichodermaXyloseXylosidasesexo-1,4-beta-D-xylosidaseFungal ProteinsMultienzyme ComplexesXyloseXylosidases

Identifiers

PMID9020869
PMCPMC1218079
OpenAlexW1767841730

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.