Evidence map›Paper›PMID 40126806›Full record

ArticleApplied biochemistry and biotechnology2025

Biochemical Characterization of a GH11 Xylanase from Xylanase-Producing Trichoderma citrinoviride.

Beom Soo Kim, Bo Min Jeong, Dongeon Kim, Soo Rin Kim, In Jung Kim

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Article in Applied biochemistry and biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

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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

5 citing papers in PubMed.

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4 · The record

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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.

Beom Soo KimDivision of Applied Life Sciences, Institute of Agriculture and Life Science, Gyeongsang National University, Jinju, 52828, South Korea.
Bo Min JeongDivision of Applied Life Sciences, Institute of Agriculture and Life Science, Gyeongsang National University, Jinju, 52828, South Korea.
Dongeon KimDivision of Applied Life Sciences, Institute of Agriculture and Life Science, Gyeongsang National University, Jinju, 52828, South Korea.
Soo Rin KimSchool of Food Science and Biotechnology, Kyungpook National University, Daegu, 41566, South Korea.
In Jung KimDepartment of Food Science & Technology, Institute of Agriculture and Life Science, Gyeongsang National University, Jinju, 52828, South Korea. ij0308@gnu.ac.kr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Xylan, a prevalent component of lignocellulose, ranks as the second most abundant carbohydrate in nature. Endo-1,4-xylanase, pivotal for its ability to cleave β-1,4-glycosidic linkages within xylan, is crucial for various applications in the food/feed processing, biofuel production, and paper/pulp industries. Although Trichoderma citrinoviride is renowned for its robust xylan-degrading capacity, the biochemical properties of xylanases derived from T. citrinoviride remain largely uncharacterized. Therefore, this study was conducted to explore the biochemical characteristics of a glycoside hydrolase family 11 xylanase derived from T. citrinoviride (TciGH11). This newly identified enzyme efficiently hydrolyzed beechwood xylan into xylooligosaccharides, exhibiting optimal activity at pH 4.5 and 50 °C, with a specific activity of 1801.5 U mg

Indexed as

Endo-1,4-beta XylanasesFungal ProteinsTrichodermaXylansGlucuronatesHydrogen-Ion ConcentrationHydrolysisKineticsOligosaccharidesSubstrate SpecificityEndo-1,4-beta XylanasesFungal ProteinsGlucuronatesOligosaccharidesXylansxylooligosaccharideGlycoside hydrolase family 11Trichoderma citrinovirideXylanXylanase

Identifiers

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Registered trials

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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.