Enzymic and Structural Properties of Crystalline Yeast Cell Lytic Enzyme from a Species of Fungi Imperfecti

Crystalline β-glucanase able to disrupt the cells of living yeast was studied from enzymic, structural and immunological view points. The enzyme degraded yeast glucan and laminarin rapidly, but it produced only very little reducing sugar and, hence, was supposed to be endo β-1,3-glucanase of a “more random” type, such as the C1 component of cellulase. The enzyme did not act on oligosaccharides composed of 2 to 9 glucose units. Serological differentiation among some yeast cell lytic enzymes using γ-immunoglobulin against the crystalline enzyme revealed the absence of an immunologically common structural unit among them. C-Terminal sequence of -Asp-Ala-Gly-Ser was established for the enzyme protein which was composed of a single polypeptide with 196 residues of 17 amino acids.