Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 1539-1543 |
| Number of pages | 5 |
| Journal | Phytochemistry |
| Volume | 17 |
| Issue number | 9 |
| Publication status | Published - 1978 |
Keywords
- cereal β-d-glucans.
- endo-1,3-/gb-d-glucanase
- germinated rye
- Gramineae
- Secale cereale