Evidence map›Paper›PMID 36178516›Full record

ReviewApplied microbiology and biotechnology2022

Insights into promiscuous chitosanases: the known and the unknown.

Haipeng Su, Jianan Sun, Zhenrong Jia, Hongjun Zhao, Xiangzhao Mao

Abstract readReview
PubMed Publisher
In one paragraph

Review in Applied microbiology and biotechnology, 2022. 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
0.3field-weighted citation impact, top 44% 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, 6 citations in OpenAlex.

  1. Article
  2. Review
  3. Enzymatic Properties of Chitosanase fromFoods (Basel, Switzerland) · 2026
    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

5 authors at 2 institutions in 1 country.

Haipeng SuCollege of Food Science and Engineering, Ocean University of China, No. 5 Yushan Road, Qingdao, 266003, China.
Jianan SunCollege of Food Science and Engineering, Ocean University of China, No. 5 Yushan Road, Qingdao, 266003, China.
Zhenrong JiaCollege of Food Science and Engineering, Ocean University of China, No. 5 Yushan Road, Qingdao, 266003, China.
Hongjun ZhaoCollege of Food Science and Engineering, Ocean University of China, No. 5 Yushan Road, Qingdao, 266003, China.
Xiangzhao MaoCollege of Food Science and Engineering, Ocean University of China, No. 5 Yushan Road, Qingdao, 266003, China. xzhmao@ouc.edu.cn.ORCID http://orcid.org/0000-0002-6315-1338
Ocean University of China · CNQingdao National Laboratory for Marine Science and Technology · CN

Funding

Agriculture Research System of China CARS-48National Natural Science Foundation of China 31922072National Natural Science Foundation of China U21A20271
6 · The paper itself

Abstract

Chitosanase, a glycoside hydrolase (GH), catalyzes the cleavage of β-1,4-glycosidic bonds in polysaccharides and is widely distributed in nature. Many organisms produce chitosanases, and numerous chitosanases in the GH families have been intensely studied. The reported chitosanases mainly cleaved the inter-glucosamine glycosidic bonds, while substrate specificity is not strictly unique due to the existence of bifunctional or multifunctional activity profiles. The promiscuity of chitosanases is essential for the different pathways of biomass polysaccharide conversion and understanding of the chitosanase evolutionary process. However, the reviews for this aspect are completely unknown. This review provides an overview of the promiscuous activities, also considering the substrate and product specificity of chitosanases observed to date. These contribute to important implications for the future discovery and research of promiscuous chitosanases and applications related to biomass conversion. KEY POINTS: • The promiscuity of chitosanases is reviewed for the first time. • The current review provides insights into the substrate specificity of chitosanases. • The mode-product relationship and prospect of promiscuous chitosanases are highlighted.

Indexed as

ChitosanGlycoside HydrolasesGlucosamineSubstrate SpecificityChitosanchitosanaseGlucosamineGlycoside HydrolasesChitosanaseGlycoside hydrolasePolysaccharidesPromiscuitySubstrate specificity

Identifiers

PMID36178516
OpenAlexW4298088231

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.