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Chitosan-degrading activities induced by glucosamine (GlcN) orN -acetylglucosamine (GlcNAc) were found in a culture filtrate ofTrichoderma reesei PC-3-7. One of the chitosan-degrading enzymes was purified to homogeneity by precipitation with ammonium sulfate followed by anion-exchange and hydrophobic-interaction chromatographies. The enzyme was monomeric, and its molecular mass was 93 kDa. The optimum pH and temperature of the enzyme were 4.0 and 50°C, respectively. The activity was stable in the pH range 6.0 to 9.0 and at a temperature below 50°C. Reaction product analysis from the viscosimetric assay and thin-layer chromatography and1 H nuclear magnetic resonance spectroscopy clearly indicated that the enzyme was an exo-type chitosanase, exo-β-d -glucosaminidase, that releases GlcN from the nonreducing end of the chitosan chain.1 H nuclear magnetic resonance spectroscopy also showed that the exo-β-d -glucosaminidase produced a β-form of GlcN, demonstrating that the enzyme is a retaining glycanase. Time-dependent liberation of the reducing sugar from partially acetylated chitosan with exo-β-d -glucosaminidase and the partially purified exo-β-d -N -acetylglucosaminidase fromT. reesei PC-3-7 suggested that the exo-β-d -glucosaminidase cleaves the glycosidic link of either GlcN-β(1→4)-GlcN or GlcN-β(1→4)-GlcNAc.

Purification and Characterization of Exo-β- d -Glucosaminidase from a Cellulolytic Fungus, Trichoderma reesei PC-3-7