Evidence map›Paper›PMID 31332537›Full record

ArticleWorld journal of microbiology & biotechnology2019

Bioproduction of N-acetyl-glucosamine from colloidal α-chitin using an enzyme cocktail produced by Aeromonas caviae CHZ306.

Flávio Augusto Cardozo, William Marcondes Facchinatto, Luiz Alberto Colnago, Sergio Paulo Campana-Filho, Adalberto Pessoa

Abstract read
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In one paragraph

Article in World journal of microbiology & biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

9 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Highly efficient chitinase production fromFrontiers in microbiology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Enhanced production of N-acetyl-glucosaminidase by marine Aeromonas caviae CHZ306 in bioreactor.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023
    Article
  7. Endochitinase and Chitobiosidase Production by MarineBioengineering (Basel, Switzerland) · 2023
    Article
  8. Article
  9. 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 2 countries.

Flávio Augusto CardozoDepartment of Microbiology, Biomedical Sciences Institute, University of Sao Paulo, 1374 Professor Lineu Prestes Ave., São Paulo, SP, 05508-000, Brazil. flavio.acardozo@gmail.com.ORCID http://orcid.org/0000-0002-1794-8880
William Marcondes FacchinattoSao Carlos Institute of Chemistry, University of Sao Paulo, Trabalhador Sao-Carlense Ave, 400, Sao Carlos, SP, 13560-970, Brazil.
Luiz Alberto ColnagoEmbrapa Instrumentation, R. XV de Novembro, 1452, Sao Carlos, SP, 13560-970, Brazil.
Sergio Paulo Campana-FilhoSao Carlos Institute of Chemistry, University of Sao Paulo, Trabalhador Sao-Carlense Ave, 400, Sao Carlos, SP, 13560-970, Brazil.
Adalberto PessoaDepartment of Biochemical and Pharmaceutical Technology, Faculty of Pharmaceutical Sciences, University of Sao Paulo, 580 Professor Lineu Prestes Ave, São Paulo, 05508-000, Brazil.
Universidade de São Paulo · BRBrazilian Agricultural Research Corporation · BR

Funding

Fundação de Amparo à Pesquisa do Estado de São Paulo 2012/16824-0Fundação de Amparo à Pesquisa do Estado de São Paulo 2013/18773-6Fundação de Amparo à Pesquisa do Estado de São Paulo 2016/20970-2
6 · The paper itself

Abstract

N-acetyl-D-glucosamine (GlcNAc) is an important amino-monosaccharide with great potential for biotechnological applications. It has traditionally been produced by the chemical hydrolysis of chitin, despite certain industrial and environmental drawbacks, including acidic wastes, low yields and high costs. Therefore, enzymatic production has gained attention as a promising environmentally-friendly alternative to the chemical processes. In this study we demonstrate the GlcNAc bioproduction from colloidal α-chitin using an enzyme cocktail containing endochitinases and exochitinases (chitobiosidases and N-acetyl-glucosaminidases). The enzyme cocktail was extracted after fermentation in a bioreactor by Aeromonas caviae CHZ306, a chitinolytic marine bacterium with great potential for chitinase production. Hydrolysis parameters were studied in terms of temperature, pH, enzyme and substrate concentration, and reaction time, achieving over 90% GlcNAc yield within 6 h. The use of colloidal α-chitin as substrate showed a substantial improvement of GlcNAc yields, when compared with β-chitin and α-chitin polymorphs. Such result is directly related to a significant decrease in crystallinity and viscosity from natural α-chitin, providing the chitinase with greater accessibility to the depolymerized chains. This study provides valuable information on the GlcNAc bioproduction from chitin using an enzymatic approach, addressing the key points for its production, including the enzyme cocktail composition and the substrate structures.

Indexed as

AcetylglucosamineAeromonas caviaeChitinChitinasesCulture MediaHydrogen-Ion ConcentrationHydrolysisMagnetic Resonance SpectroscopyMolecular WeightTemperatureViscosityX-Ray DiffractionAcetylglucosamineChitinChitinasesCulture MediaAeromonas caviaeChitinChitinasesEnzymatic hydrolysisEnzyme cocktailN-acetyl-glucosamine

Identifiers

PMID31332537
OpenAlexW2963479843

What OpenQuestion holds

Textmetadata
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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.