Article Abstract:
Research shows that family of carbohydrate-binding modules, comprising complex hydrolytic extracellular bacterial enzymes, possess different polysaccharide-binding specificities. Two modules flank Laminarinase Lam16A from Thermotoga nepolitana, which bind to different glucan molecules such as soluble laminarin and barley glucan at the N-terminus and curdlan, pustulan and yeast glucan at the C-terminus.
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Article Abstract:
Research has been conducted on Clostridium thermocellum which produced beta-1,3-glucanase. The authors report that Lic16A protein has been located on the cell surface, and that its production allowed C. thermocellum to grow on beta-1,3- or beta 1,3-1,4-glucan.
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Article Abstract:
The primary structure of the gene and the LamA protein of Thermotoga neapolitana was analyzed to determine the relationship between 1,3-beta- and 1,3-1,4-beta-glucanases. Analysis of the purified recombinant LamA protein fractions from Thermotoga neapolitana indicated the presence of enzymatic and purification profiles that were similar to the 52 kilodalton (kDa) glucanase. The purified 52 kDa beta-glucanase also resembled the processed form of the 73 kDa recombinant LamA which exhibited high specificity towards laminarin.
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