Evidence map›Paper›PMID 33760931›Full record

ReviewApplied microbiology and biotechnology2021

Enzymatic degradation of xyloglucans by Aspergillus species: a comparative view of this genus.

Tomohiko Matsuzawa, Akira Watanabe, Takahiro Shintani, Katsuya Gomi, Katsuro Yaoi

Abstract readReview
PubMed Publisher
In one paragraph

Review in Applied microbiology and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.7field-weighted citation impact, top 36% 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

7 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Production of Isoprimeverose from Xyloglucan UsingJournal of applied glycoscience · 2025
    Article
  5. Review
  6. Article
  7. 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

5 authors at 2 institutions in 1 country.

Tomohiko MatsuzawaBioproduction Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Higashi, Tsukuba, Ibaraki, 305-8566, Japan. matsuzawa-tomohiko@aist.go.jp.ORCID http://orcid.org/0000-0001-9315-5383
Akira WatanabeDepartment of Bioindustrial Informatics and Genomics, Graduate School of Agricultural Science, Tohoku University, 468-1 Aoba, Aramaki, Aoba-ku, Sendai, 980-8572, Japan.
Takahiro ShintaniDepartment of Bioindustrial Informatics and Genomics, Graduate School of Agricultural Science, Tohoku University, 468-1 Aoba, Aramaki, Aoba-ku, Sendai, 980-8572, Japan.
Katsuya GomiDepartment of Bioindustrial Informatics and Genomics, Graduate School of Agricultural Science, Tohoku University, 468-1 Aoba, Aramaki, Aoba-ku, Sendai, 980-8572, Japan.
Katsuro YaoiBioproduction Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Higashi, Tsukuba, Ibaraki, 305-8566, Japan.
Tohoku University · JPNational Institute of Advanced Industrial Science and Technology · JP

Funding

Japan Society for the Promotion of Science 18H02132
6 · The paper itself

Abstract

Aspergillus species are closely associated with humanity through fermentation, infectious disease, and mycotoxin contamination of food. Members of this genus produce various enzymes to degrade plant polysaccharides, including starch, cellulose, xylan, and xyloglucan. This review focus on the machinery of the xyloglucan degradation using glycoside hydrolases, such as xyloglucanases, isoprimeverose-producing oligoxyloglucan hydrolases, and α-xylosidases, in Aspergillus species. Some xyloglucan degradation-related glycoside hydrolases are well conserved in this genus; however, other enzymes are not. Cooperative actions of these glycoside hydrolases are crucial for xyloglucan degradation in Aspergillus species. KEY POINTS: •Xyloglucan degradation-related enzymes of Aspergillus species are reviewed. •Each Aspergillus species possesses a different set of glycoside hydrolases. •The machinery of xyloglucan degradation of A. oryzae is overviewed.

Indexed as

GlucansXylansGlycoside HydrolasesSubstrate SpecificityGlucansGlycoside HydrolasesXylansxyloglucanAspergillusGlycoside hydrolaseOligosaccharideXyloglucanXyloglucanase

Identifiers

PMID33760931
OpenAlexW3137149584

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.