Evidence map›Paper›PMID 26052323›Full record

ArticleFrontiers in microbiology2015

Synergistic function of four novel thermostable glycoside hydrolases from a long-term enriched thermophilic methanogenic digester.

Meng Wang, Guo-Li Lai, Yong Nie, Shuang Geng, Liming Liu, Baoli Zhu, Zhongping Shi, Xiao-Lei Wu

Open access · goldAbstract read
In one paragraph

Article in Frontiers in microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

10 citing papers in PubMed, 23 citations in OpenAlex.

  1. An Investigation of the Secretome Composition ofInternational journal of molecular sciences · 2025
    Article
  2. Review
  3. Article
  4. Article
  5. Recent Advances in Function-based Metagenomic Screening.Genomics, proteomics & bioinformatics · 2018
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. 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 3 institutions in 1 country.

Meng WangSchool of Biotechnology, Jiangnan University Wuxi, China ; Department of Energy and Resources Engineering, College of Engineering, Peking University Beijing, China.
Guo-Li LaiDepartment of Energy and Resources Engineering, College of Engineering, Peking University Beijing, China ; Institute of Engineering (Baotou), College of Engineering, Peking University Baotou, China.
Yong NieDepartment of Energy and Resources Engineering, College of Engineering, Peking University Beijing, China ; Institute of Engineering (Baotou), College of Engineering, Peking University Baotou, China.
Shuang GengDepartment of Energy and Resources Engineering, College of Engineering, Peking University Beijing, China.
Liming LiuSchool of Biotechnology, Jiangnan University Wuxi, China.
Baoli ZhuInstitute of Microbiology, Chinese Academy of Sciences Beijing, China.
Zhongping ShiSchool of Biotechnology, Jiangnan University Wuxi, China.
Xiao-Lei WuDepartment of Energy and Resources Engineering, College of Engineering, Peking University Beijing, China ; Institute of Engineering (Baotou), College of Engineering, Peking University Baotou, China.
Peking University · CNJiangnan University · CNChinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In biofuel production from lignocellulose, low thermostability and product inhibition strongly restrict the enzyme activities and production process. Application of multiple thermostable glycoside hydrolases, forming an enzyme "cocktail", can result in a synergistic action and therefore improve production efficiency and reduce operational costs. Therefore, increasing enzyme thermostabilities and compatibility are important for the biofuel industry. In this study, we reported the screening, cloning and biochemical characterization of four novel thermostable lignocellulose hydrolases from a metagenomic library of a long-term dry thermophilic methanogenic digester community, which were highly compatible with optimal conditions and specific activities. The optimal temperatures of the four enzymes, β-xylosidase, xylanase, β-glucosidase, and cellulase ranged from 60 to 75°C, and over 80% residual activities were observed after 2 h incubation at 50°C. Mixtures of these hydrolases retained high residual synergistic activities after incubation with cellulose, xylan, and steam-exploded corncob at 50°C for 72 h. In addition, about 55% dry weight of steam-exploded corncob was hydrolyzed to glucose and xylose by the synergistic action of the four enzymes at 50°C for 48 h. This work suggested that since different enzymes from a same ecosystem could be more compatible, screening enzymes from a long-term enriching community could be a favorable strategy.

Indexed as

biofuels productioncellulaseenzyme cocktailenzyme compatibilitymetagenomexylanaseβ-glucosidaseβ-xylosidase

Identifiers

PMID26052323
PMCPMC4441150
OpenAlexW1552926456

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.