An exo-1,3-b-glucanase has been isolated from cultural filtrate of Trichoderma viride AZ36. The N-terminal sequence of the purified enzyme (m ¼ 61 ^ 1 kDa) showed no significant homology to other known glucanases. The 1,3-b-glucanase displayed high activity against laminarins, curdlan, and 1,3-b-oligoglucosides, but acted slowly on 1,3-1,4-b-oligoglucosides. No significant activity was detected against high molecular mass 1,3-1,4-bglucans. The enzyme carried out hydrolysis with inversion of the anomeric configuration. Whereas only glucose was released from the nonreducing terminus during hydrolysis of 1,3-b-oligoglucosides, transient accumulation of gentiobiose was observed during hydrolysis of laminarins
