Isolation and properties of a (1,3)-beta-D-glucanase from Ruminococcus flavefaciens.

@article{Erfle1991IsolationAP,
  title={Isolation and properties of a (1,3)-beta-D-glucanase from Ruminococcus flavefaciens.},
  author={John Erfle and Ronald M. Teather},
  journal={Applied and environmental microbiology},
  year={1991},
  volume={57 1},
  pages={122-9}
}
A (1,3)-beta-D-glucanase [(1,3)-beta-D-glucan-3-glucanohydrolase] from Ruminococcus flavefaciens grown on milled filter paper was purified 3,700-fold (19% yield) and appeared as a single major protein and activity band upon polyacrylamide gel electrophoresis. The enzyme did not hydrolyze 1,6-beta linkages (pustulan) or 1,3-beta linkages in glucans with frequent 1,6-beta-linkage branch points (scleroglucan). Curdlan and carboxymethylpachyman were hydrolyzed at 50% the rate of laminarin. The… CONTINUE READING