An endo-1,3-ß-d-glucanase from germinated rye was purified 58-fold by ion exchange chromatography on DEAE- and CM-cellulose, and by gel filtration on Bio Gel P-60. The enzyme had pH optima of 5.0 with laminarin and 5.7 with carboxymethyl pachyman and was stable up to 45°. Bovine serum albumin and certain chlorides increased the activity at low concentrations of buffer. With laminarin, the enzyme had a Km of 0.25 mg/ml and the MW was estimated to be 24 300. Isoelectric focusing indicated that the endo-1,3-/gb-d-glucanase was a basic protein. The properties of the enzyme are compared with those from other higher plants. © 1978.
|Number of pages||5|
|Publication status||Published - 1978|
- cereal β-d-glucans.
- germinated rye
- Secale cereale