Evidence map›Paper›PMID 11319105›Full record

ArticleApplied and environmental microbiology2001

Purification and characterization of two different alpha-L-rhamnosidases, RhaA and RhaB, from Aspergillus aculeatus.

P Manzanares, H C van den Broeck, L H de Graaff, J Visser

Abstract read
In one paragraph

Article in Applied and environmental microbiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

18 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. α-L-rhamnosidase: production, properties, and applications.World journal of microbiology & biotechnology · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Crystallization and preliminary crystallographic analysis of the family GH78 alpha-L-rhamnosidase RhaB from Bacillus sp. GL1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006
    Article
  17. Article
  18. 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

4 authors.

P ManzanaresSection Molecular Genetics of Industrial Microorganisms, Wageningen University, NL-6703 HA Wageningen, The Netherlands.
H C van den Broeck
L H de Graaff
J Visser

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two proteins exhibiting alpha-L-rhamnosidase activity, RhaA and RhaB, were identified upon fractionation and purification of a culture filtrate from Aspergillus aculeatus grown on hesperidin. Both proteins were shown to be N glycosylated and had molecular masses of 92 and 85 kDa, of which approximately 24 and 15%, respectively, were contributed by carbohydrate. RhaA and RhaB, optimally active at pH 4.5 to 5, showed K(m) and V(max) values of 2.8 mM and 24 U/mg (RhaA) and 0.30 mM and 14 U/mg (RhaB) when tested for p-nitrophenyl-alpha-L-rhamnopyranoside. Both enzymes were able to hydrolyze alpha-1,2 and alpha-1,6 linkages to beta-D-glucosides. Using polyclonal antibodies, the corresponding cDNA of both alpha-L-rhamnosidases, rhaA and rhaB, was cloned. On the basis of the amino acid sequences derived from the cDNA clones, both proteins are highly homologous (60% identity).

Indexed as

Amino Acid SequenceAspergillusCarbohydrate ConformationCatalysisCloning, MolecularDNA, ComplementaryGlucosidesGlycoside HydrolasesGlycosylationHydrogen-Ion ConcentrationKineticsMolecular Sequence DataMolecular WeightRhamnoseSequence AlignmentSequence Analysis, DNAalpha-L-rhamnosidaseDNA, ComplementaryGlucosidesGlycoside HydrolasesRhamnose

Identifiers

PMID11319105
PMCPMC92860

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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.