Evidence map›Paper›PMID 38650254›Full record

ReviewBioresources and bioprocessing2021

Pectinolytic lyases: a comprehensive review of sources, category, property, structure, and catalytic mechanism of pectate lyases and pectin lyases.

Ling Zheng, Yinxiao Xu, Qian Li, Benwei Zhu

Open access · diamondAbstract readReview
In one paragraph

Review in Bioresources and bioprocessing, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
10.0field-weighted citation impact, top 2% 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

23 citing papers in PubMed, 78 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. International journal of molecular sciences · 2026
    Article
  6. A novel recombinant oligogalacturonide lyase fromFrontiers in bioengineering and biotechnology · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Origin and evolution of auxin-mediated acid growth.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Article
  13. Review
  14. Article
  15. The Utilization byFoods (Basel, Switzerland) · 2024
    Article
  16. High qualityISME communications · 2024
    Article
  17. Article
  18. Review
  19. Article
  20. Review
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 at 1 institution in 1 country.

Ling ZhengCollege of Food Science and Light Industry, Nanjing Tech University, Nanjing, 211816, P. R. China.
Yinxiao XuCollege of Food Science and Light Industry, Nanjing Tech University, Nanjing, 211816, P. R. China.
Qian LiCollege of Food Science and Light Industry, Nanjing Tech University, Nanjing, 211816, P. R. China.
Benwei ZhuCollege of Food Science and Light Industry, Nanjing Tech University, Nanjing, 211816, P. R. China. zhubenwei@njtech.edu.cn.
Nanjing Tech University · CN

Funding

national natural science foundation of china 31601410
6 · The paper itself

Abstract

Pectate lyases and pectin lyases have essential roles in various biotechnological applications, such as textile industry, paper making, pectic wastewater pretreatment, juice clarification and oil extraction. They can effectively cleave the α-1,4-glycosidic bond of pectin molecules back bone by β-elimination reaction to produce pectin oligosaccharides. In this way, it will not generate highly toxic methanol and has the advantages of good enzymatic selectivity, less by-products, mild reaction conditions and high efficiency. However, numerous researches have been done for several decades; there are still no comprehensive reviews to summarize the recent advances of pectate lyases and pectin lyases. This review tries to fill this gap by providing all relevant information, including the substrate, origin, biochemical properties, sequence analysis, mode of action, the three-dimensional structure and catalytic mechanism.

Indexed as

Biochemical propertiesCatalytic mechanismPectate lyasePectin lyaseSequence analysisStructure

Identifiers

PMID38650254
PMCPMC10992409
OpenAlexW3193754864

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.