Evidence map›Paper›PMID 31542050›Full record

ArticleMicrobial cell factories2019

Cooperation of hydrolysis modes among xylanases reveals the mechanism of hemicellulose hydrolysis by Penicillium chrysogenum P33.

Yi Yang, Jinshui Yang, Ruonan Wang, Jiawen Liu, Yu Zhang, Liang Liu, Fengqin Wang, Hongli Yuan

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

4 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Optimization of xylanase production by Pichia kudriavzevii and Candida tropicalis isolated from the wood product workshop.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024
    Article
  3. Frontiers in microbiology · 2022
    Article
  4. 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

8 authors at 2 institutions in 1 country.

Yi YangState Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, 100193, China.
Jinshui YangState Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, 100193, China.
Ruonan WangState Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, 100193, China.
Jiawen LiuState Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, 100193, China.
Yu ZhangState Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, 100193, China.
Liang LiuState Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, 100193, China.
Fengqin WangCollege of Life Science, Henan Agricultural University, Zhengzhou, 450002, China.
Hongli YuanState Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, 100193, China. hlyuan@cau.edu.cn.ORCID http://orcid.org/0000-0002-9701-2424
China Agricultural University · CNHenan Agricultural University · CN

Funding

Project of State Key Laboratory of Agrobiotechnology 2017SKLAB7-15Shanxi "1331 Project" Collaborative Innovation Center and the special fund for Agro-scientific Research in the Public Interest 201403048-2
6 · The paper itself

Abstract

backgroundXylanases randomly cleave the internal β-1,4-glycosidic bonds in the xylan backbone and are grouped into different families in the carbohydrate-active enzyme (CAZy) database. Although multiple xylanases are detected in single strains of many filamentous fungi, no study has been reported on the composition, synergistic effect, and mode of action in a complete set of xylanases secreted by the same microorganism.

resultsAll three xylanases secreted by Penicillium chrysogenum P33 were expressed and characterized. The enzymes Xyl1 and Xyl3 belong to the GH10 family and Xyl3 contains a CBM1 domain at its C-terminal, whereas Xyl2 belongs to the GH11 family. The optimal temperature/pH values were 35 °C/6.0, 50 °C/5.0 and 55 °C/6.0 for Xyl1, Xyl2, and Xyl3, respectively. The three xylanases exhibited synergistic effects, with the maximum synergy observed between Xyl3 and Xyl2, which are from different families. The synergy between xylanases could also improve the hydrolysis of cellulase (C), with the maximum amount of reducing sugars (5.68 mg/mL) observed using the combination of C + Xyl2 + Xyl3. Although the enzymatic activity of Xyl1 toward xylan was low, it was shown to be capable of hydrolyzing xylooligosaccharides into xylose. Xyl2 was shown to hydrolyze xylan to long-chain xylooligosaccharides, whereas Xyl3 hydrolyzed xylan to xylooligosaccharides with a lower degree of polymerization.

conclusionsSynergistic effect exists among different xylanases, and it was higher between xylanases from different families. The cooperation of hydrolysis modes comprised the primary mechanism for the observed synergy between different xylanases. This study demonstrated, for the first time, that the hydrolysates of GH11 xylanases can be further hydrolyzed by GH10 xylanases, but not vice versa.

Indexed as

BiocatalysisEndo-1,4-beta XylanasesEnzyme StabilityFungal ProteinsGlucuronatesHot TemperatureHydrolysisMultigene FamilyOligosaccharidesPenicillium chrysogenumPolysaccharidesProtein DomainsXylansEndo-1,4-beta XylanasesFungal ProteinsGlucuronateshemicelluloseOligosaccharidesPolysaccharidesXylansxylooligosaccharideCooperationEnzymatic hydrolysisHydrolysis modePenicillium chrysogenumXylanase

Identifiers

PMID31542050
PMCPMC6754857
OpenAlexW2973421957

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.