Characterization of an endo-1,3(4)-β-d-glucanase gene from Cellvibrio mixtus |
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Authors: | Harry Sakellaris John M. Pemberton John M. Manners |
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Affiliation: | Department of Microbiology, The University of Queensland, St. Lucia, Queensland, Australia; Cooperative Research Centre for Tropical Plant Pathology, The University of Queensland, St. Lucia, Queensland, Australia |
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Abstract: | Abstract An endo-1,3(4)-β- d -glucanase gene ( cwd2 ) of Cellvibrio mixtus encoding laminarinase activity was cloned on a 3.9-kb Pst I fragment. The Cwd2 enzyme, extracted from recombinant Escherichia coli , degraded both β-1,3 glucans and β-1,3–1,4 mixed-linkage glucans, was entohydrolytic and so conformed to the enzyme class 3.2.1.6. The pH and temperature optima of the enzyme were approximately 7 and 40°C respectively. The M r of specifically labelled Cwd2 was approximately 34 000. This gene was quite distinct from two other C. mixtus β-1,3 glucanases previously described. |
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Keywords: | Cellvibrio mixtus Endo-1,3,(4)-β-d-glucanase gene EC 3.2.1.6 |
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