A chitin deacetylase of Podospora anserina has two functional chitin binding domains and a unique mode of action

Hoßbach, Janina; Bußwinkel, Franziska; Kranz, Andreas; Wattjes, Jasper; Cord‐Landwehr, Stefan; Moerschbacher, Bruno M.

doi:10.1016/j.carbpol.2017.11.015

Cited by 37 publications

(38 citation statements)

References 75 publications

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“…In contrast, regarding deacetylation performed by fungal CDAs, all three fungal CDAs shown in Fig. 2 are known to first deacetylate the chitin tetramer at the GlcNAc unit next to the reducing end and then either stop ( Pes CDA 22 ), continue to deacetylate the reducing end ( Pgt CDA 30 ), or deacetylate all four GlcNAc residues in a stepwise fashion ( Pa CDA 32 ). Regarding this deacetylation pattern, these three fungal CDAs are highly specific when using ideal enzyme-substrate ratios, but they are known to partially lose specificity when reaction conditions change 38 .…”

Section: Resultsmentioning

confidence: 99%

“… E. coli Rosetta2 (DE3) [pLysRARE2] Strep-tag II 22 Pgt CDA Puccinia graminis f.sp. tritici E. coli Rosetta2 (DE3) [pLysRARE2] Strep-tag II 30 Pa CDA Podospora anserina Hansenula polymorpha HIS6-tag 32 …”

Section: Methodsmentioning

confidence: 99%

“…The most promising approach towards the production of fully defined paCOS is the use of regio-selective chitin deacetylases (CDA, EC 3.5.1.41) for the partial deacetylation of chitin oligomers of defined DP 22 , 25 – 32 . The best-known example for such a CDA is NodB from Rhizobium bacteria which specifically deacetylates the non-reducing end unit of a chitin oligomer A n (n = DP) leading to the mono-deacetylated paCOS DA (n−1) 25 .…”

Section: Introductionmentioning

confidence: 99%

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Enzymatic production of all fourteen partially acetylated chitosan tetramers using different chitin deacetylases acting in forward or reverse mode

Hembach

Cord‐Landwehr

Moerschbacher

2017

Sci Rep

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Some of the most abundant biomolecules on earth are the polysaccharides chitin and chitosan of which especially the oligomeric fractions have been extensively studied regarding their biological activities. However, most of these studies have not been able to assess the activity of a single, defined, partially acetylated chitosan oligosaccharide (paCOS). Instead, they have typically analyzed chemically produced, rather poorly characterized mixtures, at best with a single, defined degree of polymerization (DP) and a known average degree of acetylation (DA), as no pure and well-defined paCOS are currently available. We here present data on the enzymatic production of all 14 possible partially acetylated chitosan tetramers, out of which four were purified (>95%) regarding DP, DA, and pattern of acetylation (PA). We used bacterial, fungal, and viral chitin deacetylases (CDAs), either to partially deacetylate the chitin tetramer; or to partially re-N-acetylate the glucosamine tetramer. Both reactions proceeded with surprisingly strong and enzyme-specific regio-specificity. These pure and fully defined chitosans will allow to investigate the particular influence of DP, DA, and PA on the biological activities of chitosans, improving our basic understanding of their modes of action, e.g. their molecular perception by patter recognition receptors, but also increasing their usefulness in industrial applications.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Enzymatic production of all fourteen partially acetylated chitosan tetramers using different chitin deacetylases acting in forward or reverse mode

Hembach

Cord‐Landwehr

Moerschbacher

2017

Sci Rep

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“…In the wildtype strain, expression levels of cda1 and cda5 were highly elevated during mycoparasitism and oxidative stress caused by ROS. Moreover, the CBMs present in these enzymes are important for substrate recognition of oligosaccharides and are implicated in enhancing deacetylase activity by increasing the accessibility of the substrate to the catalytic domain [62,118]. TaCDA3, TaCDA4 and TaCDA6 do not group with any of the other deacetylases, except for their T. reesei CDA4 orthologue.…”

Section: Discussionmentioning

confidence: 99%

Chitin and chitosan remodeling defines vegetative development and Trichoderma biocontrol

et al. 2020

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Fungal parasitism depends on the ability to invade host organisms and mandates adaptive cell wall remodeling to avoid detection and defense reactions by the host. All plant and human pathogens share invasive strategies, which aid to escape the chitin-triggered and chitin-targeted host immune system. Here we describe the full spectrum of the chitin/chitosan-modifying enzymes in the mycoparasite Trichoderma atroviride with a central role in cell wall remodeling. Rapid adaption to a variety of growth conditions, environmental stresses and host defense mechanisms such as oxidative stress depend on the concerted interplay of these enzymes and, ultimately, are necessary for the success of the mycoparasitic attack. To our knowledge, we provide the first in class description of chitin and associated glycopolymer synthesis in a mycoparasite and demonstrate that they are essential for biocontrol. Eight chitin synthases, six chitin deacetylases, additional chitinolytic enzymes, including six chitosanases, transglycosylases as well as accessory proteins are involved in this intricately regulated process. Systematic and biochemical classification, phenotypic characterization and mycoparasitic confrontation assays emphasize the importance of chitin and chitosan assembly in vegetative development and biocontrol in T. atroviride. Our findings critically contribute to understanding the molecular mechanism of chitin synthesis in filamentous fungi and mycoparasites with the overarching goal to selectively exploit the discovered biocontrol strategies.

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“…Interestingly, this can be counteracted by the co-application of LPMOs, which cleave polymer chain ends on the surface of crystalline chitin, as a result enhancing the activity of CDAs [98]. Moreover, several CDAs and CODs are known to possess a carbohydrate binding module (CBM) fused to their catalytic domain, therefore increasing the accessibility of the recalcitrant substrate to the active site [99].…”

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confidence: 99%

Enzymatic Modification of Native Chitin and Conversion to Specialty Chemical Products

Arnold

Brück²,

Garbe

et al. 2020

Marine Drugs

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Chitin is one of the most abundant biomolecules on earth, occurring in crustacean shells and cell walls of fungi. While the polysaccharide is threatening to pollute coastal ecosystems in the form of accumulating shell-waste, it has the potential to be converted into highly profitable derivatives with applications in medicine, biotechnology, and wastewater treatment, among others. Traditionally this is still mostly done by the employment of aggressive chemicals, yielding low quality while producing toxic by-products. In the last decades, the enzymatic conversion of chitin has been on the rise, albeit still not on the same level of cost-effectiveness compared to the traditional methods due to its multi-step character. Another severe drawback of the biotechnological approach is the highly ordered structure of chitin, which renders it nigh impossible for most glycosidic hydrolases to act upon. So far, only the Auxiliary Activity 10 family (AA10), including lytic polysaccharide monooxygenases (LPMOs), is known to hydrolyse native recalcitrant chitin, which spares the expensive first step of chemical or mechanical pre-treatment to enlarge the substrate surface. The main advantages of enzymatic conversion of chitin over conventional chemical methods are the biocompability and, more strikingly, the higher product specificity, product quality, and yield of the process. Products with a higher Mw due to no unspecific depolymerisation besides an exactly defined degree and pattern of acetylation can be yielded. This provides a new toolset of thousands of new chitin and chitosan derivatives, as the physio-chemical properties can be modified according to the desired application. This review aims to provide an overview of the biotechnological tools currently at hand, as well as challenges and crucial steps to achieve the long-term goal of enzymatic conversion of native chitin into specialty chemical products.

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A chitin deacetylase of Podospora anserina has two functional chitin binding domains and a unique mode of action

Cited by 37 publications

References 75 publications

Enzymatic production of all fourteen partially acetylated chitosan tetramers using different chitin deacetylases acting in forward or reverse mode

Enzymatic production of all fourteen partially acetylated chitosan tetramers using different chitin deacetylases acting in forward or reverse mode

Chitin and chitosan remodeling defines vegetative development and Trichoderma biocontrol

Enzymatic Modification of Native Chitin and Conversion to Specialty Chemical Products

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