Characterization of the carbohydrase productions of an ectomycorrhizal fungus, Tricholoma matsutake (Yamada 2005). The main factors for this decrease are believed to be the accumulation of humus in pine tree forests, death of the trees caused by Bursaphelenchus xylophilus (Steiner et Buhrer) Nickle (the pine wilt nematode) (Futai 2003), acid rain, and the collection of immature fruit bodies from the fi eld.This fungus has low ability to decompose polysaccharides for use as a growth substrate and grows slowly on artifi cial media (about 2 cm growth/month) (Hur et al. 2001). Therefore, only glucose and a few other mono-and disaccharides can be used to grow this fungus (Kawai and Abe 1976). This fungus has not previously been known to use any other polysaccharides except starch (Lee et al. 1998).Ohta (1994) reported that Lyophyllum shimeji (Kawamura) Hongo, classifi ed as an ectomycorrhizal fungus, forms mature fruit bodies within a bottle containing a barley grain in a cultivation medium without a host plant. He mentioned that a suffi cient quantity of starch used as a carbon source was able to supply the factor that allows successful fruit-body formation without raising the osmotic pressure in the medium (Ohta 1997). The fruit-body formation of this fungus in artifi cial cultivation was reported by Watanabe et al. (1994) and Yoshida and Fujimoto (1994) at about the same time. Ohta (1997) noted the importance of the amylase systems of this fungus based on their ability to use barley starch as a growth substrate.We examined the amylase systems used during the fruitbody formation of L. shimeji in barley grain medium. We showed for the fi rst time that the amylase is a glucoamylase with a high hydrolyzing ability (Kusuda et al. 2004).The demand for the artifi cial cultivation of T. matsutake has grown stronger because of the success of the artifi cial cultivation of L. shimeji, but it has not yet been accomplished. Therefore, we investigated the starch-hydrolyzing ability (amylase production systems) of T. matsutake.We found that this fungus exhibited weak α-amylase (Kusuda et al. 2003) and α-glucosidase as a weak activity in a static culture fi ltrate. On the other hand, no glucoamylase activity was detected in the static culture fi ltrate. Surprisingly, we discovered that β-glucosidase demonstrated strong