An exo-1,3 β-glucanase was purified from blastoconidia of 1001. The purified enzyme appeared as a single protein band by PAGE, and split into two subunits ( approximately 63000 and 44000) when analysed by SDS-PAGE. The pI of the enzyme was 4 and a of 1.7 mg ml was estimated for laminarin as substrate. Despite its very reduced activity on the synthetic substrate -nitrophenyl β--glucoside, exo-1,3-β-glucanase hydrolysed 1,3-β-glucan by an exo-splitting mechanism and was inhibited by glucono-δ-lactone and by Hg and Ag cations. The active exo-glucanase was mainly located in the periplasm, but it was also present inside the cytoplasmic membrane in small amounts and was secreted into the culture medium. The electrophoretic mobility of the enzyme from all three locations was the same.


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