ArticleWorld journal of microbiology & biotechnology2019
Bioproduction of N-acetyl-glucosamine from colloidal α-chitin using an enzyme cocktail produced by Aeromonas caviae CHZ306.
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.
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Who cites it
9 citing papers in PubMed, 25 citations in OpenAlex.
- Functional Characterization and Antifungal Activity of Insect-Derived Chitinases Expressed inPolymers · 2026Article
- Highly efficient chitinase production fromFrontiers in microbiology · 2026Article
- The Impact of Chitinase Binding Domain Truncation on the Properties ofMarine drugs · 2025Article
- NMR Fingerprinting of Conventional and Genetically Modified Soybean Plants with AtAREB1 Transcription Factors.ACS omega · 2024Article
- Activity of a Recombinant Chitinase of thePolymers · 2024Article
- Enhanced production of N-acetyl-glucosaminidase by marine Aeromonas caviae CHZ306 in bioreactor.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Article
- Endochitinase and Chitobiosidase Production by MarineBioengineering (Basel, Switzerland) · 2023Article
- Production of Thermophilic Chitinase byPolymers · 2021Article
- A Broad-Specificity Chitinase fromMarine drugs · 2021Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
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.
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