CORDIS provides links to public deliverables and publications of HORIZON projects.
Links to deliverables and publications from FP7 projects, as well as links to some specific result types such as dataset and software, are dynamically retrieved from OpenAIRE .
Exploitable results
The lamA gene from Thermotoga neapolitana was cloned and sequenced. It consists of a catalytic domain flanked by two non-catalytic domains, possibly mediating binding to β-1,3-glucan. It is one of the most thermostable β-1,3-glucanase known to date. Its gene is preceded by the β-glucosidase gene bglB, possibly functioning as a co-regulated operon. The BglB protein is a β-1,3-glucosidase (laminaribiase) and together with LamA completely hydrolyses β-1,3-glucan to glucose monomers. Thermotoga strains possess two β-glucosidases genes, which are expressed. They belong to different glycosyl hydrolases families (1 and 3).
In contrast to β-1,4-glucanase genes, no genes for β-1,3-glucanases could be identified in Anaerocellum thermophilium.
A publicly accessible server was set up (CAZY) where all hitherto known protein moduls identified in glycosyl hydrolases can be browsed. Each entry is linked to different data bases.
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