Purification and characterization of 1,3-β-d-glucanase from Eisenia foetida

1,3-β-d-glucanase from the earthworm Eisenia foetida was purified to electrophoretically homogeneous state. The molecular weight of the purified enzyme was estimated 42,000 by SDS-PAGE. The N-terminal amino acid sequence of the enzyme was very similar to those of CCF-I from E. foetida and CCF-like protein from Aprorrectodea caliginosa. The enzyme was most active at pH 6.0 and 60 °C, and stable at pH 6.0-10.5 and 60 °C. The enzyme was inhibited by metal ions Mn2+, Cu2+, Fe2+, Al3+, and hydrolyzed 1,3-β-d-linked oligosaccharides (triose, tetraose, and pentose) into glucose, and biose as end products.