Abstract
The some properties of a highly purified lytic enzyme from Basidiomycetes species have been investigated.
The enzyme activity was stable at acidic pH, but inactivated rapidly under neutral and alkaline conditions. The optimum pH of the activity was 4.0. Heating at 100°C for 30min inactivated only 20% of the original activity, and even after 120°C for 30min measurable activity still remained.
Laminarin and yeast glucan, predominantly composed of β-(1, 3)-linked glucan, were hydrolyzed by the enzyme into glucose and oligosaccharides, and from the latter more glucose were released on further incubation. On the other hand, β-(1, 4)-glucan and β-(1, 6)-glucan, such as cellulose, chitin and luteose, were not affected by this preparation.
These findings suggested that the lytic enzyme is an endo-β-(1, 3)-glucanase that can randomly hydrolyze β-(1, 3)-glucosidic linkage.
When living cells of Saccharomyces cerevisiae were treated with this enzyme, the lysis occured in some sites of the cell wall, and if suspended in the isotonic buffer solution, cells were transformed into typical protoplasts after several intermediate stages.
