Characterization of an endo-1,3(4)-beta-D-glucanase gene from Cellvibrio mixtus.
An endo-1,3(4)-beta-D-glucanase gene (cwd2) of Cellvibrio mixtus encoding laminarinase activity was cloned on a 3.9-kb PstI fragment. The Cwd2 enzyme, extracted from recombinant Escherichia coli, degraded both beta-1,3 glucans and beta-1,3-1,4 mixed-linkage glucans, was endohydrolytic and so conformed to the enzyme class 3.2.1.6. The pH and temperature optima of the enzyme were approximately 7 and 40 degrees C respectively. The M(r) of specifically labelled Cwd2 was approximately 34,000. This gene was quite distinct from two other C. mixtus beta-1,3 glucanases previously described.
Sakellaris
H
H
Department of Microbiology, University of Queensland, St. Lucia, Australia.
Pemberton
J M
JM
Manners
J M
JM
D002855:Chromatography, Thin Layer; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D044644:Endo-1,3(4)-beta-Glucanase; D005798:Genes, Bacterial; D006026:Glycoside Hydrolases / Q000235:genetics* / Q000378:metabolism; D006088:Gram-Negative Aerobic Bacteria / Q000201:enzymology* / Q000235:genetics; D011994:Recombinant Proteins / Q000378:metabolism; D015183:Restriction Mapping; D013379:Substrate Specificity
D011994:Recombinant Proteins; D006026:Glycoside Hydrolases; D044644:Endo-1,3(4)-beta-Glucanase