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Lea Hembach

Researcher at University of Münster

Publications -  6
Citations -  112

Lea Hembach is an academic researcher from University of Münster. The author has contributed to research in topics: Chitin & Chemistry. The author has an hindex of 4, co-authored 5 publications receiving 53 citations.

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

TL;DR: 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 the basic understanding of their modes of action and increasing their usefulness in industrial applications.
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Unique subsite specificity and potential natural function of a chitosan deacetylase from the human pathogen Cryptococcus neoformans

TL;DR: The detailed functional analysis of CnCda4, a chitin deacetylase with unusual subsite specificity resulting in a preference for chitosan rather than chitIn, is described, showing that the enzyme probably helps the pathogen to evade the host immune system by furtherDeacetylating exposed chitan, making the fungus less susceptible to host immunosurveillance.
Posted ContentDOI

A single intracellular protein governs the critical transition from an individual to a coordinated population response during quorum sensing: Origins of primordial language

TL;DR: This work explains for the first time, the cell-density-dependent synchronicity of QS responses as the function of a single protein, the LuxR-like activator, capable of coordinating the temporal response of a population of cells in the absence of cell-to-cell communication.
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In silico and in vitro analysis of an Aspergillus niger chitin deacetylase to decipher its subsite sugar preferences.

TL;DR: In this paper, the crystal structure of an Aspergillus niger CDA (AngCDA) was determined using molecular dynamics simulations, backed up with a variety of in vitro activity assays using different well-defined polymeric and oligomeric substrates.