Screening and Enzymatic-producing Study of Chitin Deacetylase Producing Bacteria-Lysinibacillus sp.
Shipin gongye ke-ji, 2022 In order to biodegrade natural chitin, in this study, chitin was used as the sole carbon source, obtain chitin deacetylase strains which could produce chitosan from natural chitin by biological method.
Xin MENG +4 more
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Cloning and Characterization of Chitin Deacetylase from Euphausia superba. [PDF]
Int J Mol SciChitin deacetylase (CDA) can catalyze the deacetylation of chitin to produce chitosan. In this study, we identified and characterized a chitin deacetylase gene from Euphausia superba (EsCDA-9k), and a soluble recombinant protein chitin deacetylase from Euphausia superba of molecular weight 45 kDa was cloned, expressed, and purified.
Wang X, Tan J, Zou H, Wang F, Xu J.
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Chitin Deacetylases: Properties and Applications [PDF]
Marine Drugs, 2010 Chitin deacetylases, occurring in marine bacteria, several fungi and a few insects, catalyze the deacetylation of chitin, a structural biopolymer found in countless forms of marine life, fungal cell and spore walls as well as insect cuticle and peritrophic matrices.
Riccardo A.A. Muzzarelli +2 more
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Preparation of Defined Chitosan Oligosaccharides Using Chitin Deacetylases [PDF]
International Journal of Molecular Sciences, 2020 During the past decade, detailed studies using well-defined ‘second generation’ chitosans have amply proved that both their material properties and their biological activities are dependent on their molecular structure, in particular on their degree of polymerisation (DP) and their fraction of acetylation (FA). Recent evidence suggests that the pattern
Martin Bonin +3 more
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Chitin Deacetylases: Structures, Specificities, and Biotech Applications [PDF]
Polymers, 2018 Depolymerization and de-N-acetylation of chitin by chitinases and deacetylases generates a series of derivatives including chitosans and chitooligosaccharides (COS), which are involved in molecular recognition events such as modulation of cell signaling and morphogenesis, immune responses, and host-pathogen interactions.
Laia Grifoll-Romero +4 more
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Polycistronic Expression System for Pichia pastoris Composed of Chitino- and Chitosanolytic Enzymes
Frontiers in Bioengineering and Biotechnology, 2021 Chitin is one of the most abundant biopolymers. Due to its recalcitrant nature and insolubility in accessible solvents, it is often considered waste and not a bioresource. The products of chitin modification such as chitosan and chitooligosaccharides are
Michal B. Kaczmarek +8 more
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The influence of selected ionic liquids on activity of chitin deacetylase
Chemical and Process Engineering, 2016 Chitin deacetylase is the only known enzyme which is able to deacetylate N-acetyl-D-glucosamine units in chitin or chitosan chains. As chitin can hardly be dissolved in organic/inorganic solvents, new solvents are still searched.
Aspras Izabela +4 more
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Rational Design of a Potential New Nematicide Targeting Chitin Deacetylase. [PDF]
J Agric Food ChemIn a previously published study, the authors devised a molecular topology QSAR (quantitative structure-activity relationship) approach to detect novel fungicides acting as inhibitors of chitin deacetylase (CDA). Several of the chosen compounds exhibited noteworthy activity.
Galvez-Llompart M +9 more
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Chitin Heterodisaccharide, Released from Chitin by Chitinase and Chitin Oligosaccharide Deacetylase, Enhances the Chitin-Metabolizing Ability of Vibrio parahaemolyticus [PDF]
Journal of Bacteriology, 2019 We demonstrate that β- N -acetyl- d -glucosaminyl-(1,4)- d -glucosamine (GlcNAc-GlcN) enhances the chitin-metabolizing ability of V. parahaemolyticus .
Takako, Hirano +5 more
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Cloning, expression and activity identification of chitin deacetylase gene from Saccharomyces cerevisiae [PDF]
Zhongguo niangzaoTo construct a non-methanol induced expression vector and engineering strain for chitin deacetylase in Pichia pastoris, two chitin deacetylase genes ScCDA1 and ScCDA2 were amplified and cloned from Saccharomyces cerevisiae and subjected to bioinformatics
HU Shiqi
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