Evidence map›Paper›PMID 31612131›Full record

ReviewFrontiers in bioengineering and biotechnology2019

Enzymatic Modifications of Chitin, Chitosan, and Chitooligosaccharides.

Michal Benedykt Kaczmarek, Katarzyna Struszczyk-Swita, Xingkang Li, Miroslawa Szczęsna-Antczak, Maurycy Daroch

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in bioengineering and biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
14.4field-weighted citation impact, top 1% 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

104 citing papers in PubMed, 395 citations in OpenAlex.

  1. Complete genome sequence ofMicrobiology resource announcements · 2026
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  20. Characterization of extracellular chitin deacetylase fromCurrent research in microbial sciences · 2025
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44 more citing papers are in PubMed but not listed here.

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 2 countries.

Michal Benedykt KaczmarekInstitute of Technical Biochemistry, Lodz University of Technology, Łódź, Poland.
Katarzyna Struszczyk-SwitaInstitute of Technical Biochemistry, Lodz University of Technology, Łódź, Poland.
Xingkang LiSchool of Environment and Energy, Peking University Shenzhen Graduate School, Shenzhen, China.
Miroslawa Szczęsna-AntczakInstitute of Technical Biochemistry, Lodz University of Technology, Łódź, Poland.
Maurycy DarochSchool of Environment and Energy, Peking University Shenzhen Graduate School, Shenzhen, China.
Lodz University of Technology · PLPeking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chitin and its N-deacetylated derivative chitosan are two biological polymers that have found numerous applications in recent years, but their further deployment suffers from limitations in obtaining a defined structure of the polymers using traditional conversion methods. The disadvantages of the currently used industrial methods of chitosan manufacturing and the increasing demand for a broad range of novel chitosan oligosaccharides (COS) with a fully defined architecture increase interest in chitin and chitosan-modifying enzymes. Enzymes such as chitinases, chitosanases, chitin deacetylases, and recently discovered lytic polysaccharide monooxygenases had attracted considerable interest in recent years. These proteins are already useful tools toward the biotechnological transformation of chitin into chitosan and chitooligosaccharides, especially when a controlled non-degradative and well-defined process is required. This review describes traditional and novel enzymatic methods of modification of chitin and its derivatives. Recent advances in chitin processing, discovery of increasing number of new, well-characterized enzymes and development of genetic engineering methods result in rapid expansion of the field. Enzymatic modification of chitin and chitosan may soon become competitive to conventional conversion methods.

Indexed as

chitinchitinasechitin deacetylasechitooligosaccharideschitosanchitosanaseenzymatic modificationslytic polysaccharide monooxygenase

Identifiers

PMID31612131
PMCPMC6776590
OpenAlexW2975143944

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.