Objective
The beta-glucanases of thermophilic bacteria have a great application potential due to their intrinsic stability. They often have an unusally complex molecular structure composed of catalytic and non-catalytic protein domains.
This project examines the structure and function of isolated domains from thermostable beta-1,3- and beta-1,3-1,4-glucanases. It investigates the mechanism of hydrolysis and the basis for substrate recognition and for thermostability. beta-glucanase clones from genomic libraries of Clostridium thermocellum, Anaerocellum thermophilum, and Thermotoga neapolitana are isolated and sequenced. Catalytic and non-catalytic gene domains are recognized by sequence comparison and separated by gene technological methods (PCR). Purified recombinant enzymes are characterized by their biochemical parameters such as substrate binding and specificity, pH optimum, stability. Isolated catalytic domains are investigated for the mechanism of substrate binding and hydrolysis.
Protein engineering with modification of the proteins will be performed to yield a bulk of new, highly stable beta-glucanases. New information on the mechanism of beta-glucan degradation in nature and on the function of non-catalytic domains is to be expected.
Fields of science (EuroSciVoc)
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Programme(s)
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Multi-annual funding programmes that define the EU’s priorities for research and innovation.
Topic(s)
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Calls for proposals are divided into topics. A topic defines a specific subject or area for which applicants can submit proposals. The description of a topic comprises its specific scope and the expected impact of the funded project.
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Funding Scheme
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Coordinator
80290 München
Germany
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